糖皮质激素对肉仔鸡骨骼肌蛋白代谢影响的研究
|
摘要
为探讨糖皮质激素对肉仔鸡骨骼肌蛋白代谢的影响,本研究从体内试验和体外试验两方面入手,体内试验用人为导入外源糖皮质激素的方法,体外试验离体培养骨骼肌成肌细胞并用糖皮质激素处理,观察糖皮质激素对蛋白的合成途径和蛋白的分解途径的数个关键基因mRNA的相对表达量的变化情况,为骨骼肌蛋白代谢的基因表达调控的网络构建以及研究骨骼肌蛋白代谢的详细的分子机制提供理论依据。
体内试验分两部分:试验一选取28日龄体重相近的AA雄性肉鸡288只,随机分为正常日粮组和高蛋白日粮组,经过三天日粮适应期后,每个组随机分为三个处理:糖皮质激素处理组(DEX)、对照组、限饲组,每个处理3个重复,每个重复12只鸡,糖皮质激素处理组8:30和20:30,腹部皮下注射地塞米松1.0mg/kg体重,对照组、限饲组注射与糖皮质激素处理组等体积的生理盐水,限饲组饲喂糖皮质激素处理组前一天的采食量。34日龄晚20:30开始禁食。禁食后再饲喂组在35日龄早上8:30再饲喂一小时后采样。各试验鸡均翅静脉采血,3000r/min离心10min,分离血浆,-20℃冷冻保存。取胸大肌(M. pectoralis major,PM),液氮速冻,-80℃贮存。同时取部分组织样品。取全部胸肌称重,测定胸肌指数(胸肌重/活体重),取右腿全部肌肉称重,测定腿肌指数(腿肌重/活体重)。结果表明,糖皮质激素能使日增重显著降低,采食量无显著影响。糖皮质激素能使血浆中尿酸、T-AA、胰岛素的浓度显著上升。糖皮质激素能显著上调蛋白质分解途径相关基因的表达,对蛋白质合成途径的相关基因的抑制作用不明显。高蛋白日粮对缓解糖皮质激素的作用不明显。试验二选取35日龄体重相近的AA雄性肉鸡72只,随机分为2个组:糖皮质激素处理组(DEX)和对照组,每个处理3个重复,每个重复6只鸡。36-38日龄,8:00和20:00,糖皮质激素处理组皮下注射地塞米松1.0mg/kg体重,对照组注射相同体积的生理盐水。38日龄20:00禁食12h,禁食后(每个处理3个重复,每个重复取4只鸡)空腹采血,然后每个处理分A、B两个处理进行灌服处理:A组灌服亮氨酸500mg/Kg体重,B组灌服生理盐水5ml,灌服后1h,各试验鸡均翅静脉采血,3000r/min离心10min,分离血浆,-20℃冷冻保存。取胸大肌(M. pectoralis major,PM),液氮速冻,-80℃贮存。同时取部分组织样品。取全部胸肌称重,测定胸肌指数(胸肌重/活体重),取右腿全部肌肉称重,测定腿肌指数(腿肌重/活体重)。结果表明,糖皮质激素能使日增重显著降低,采食量无显著影响。糖皮质激素能显著促进蛋白质分解途径相关基因的表达。灌服对缓解糖皮质激素的作用也不明显。
体外试验分两个试验:试验三培养骨骼肌成肌细胞,细胞在含有10%的胎牛血清的DMEM培养基中生长,当细胞铺满六孔板的70%时,更换成含有2%马血清的DMEM培养基诱导成肌细胞分化成肌管,分化时间为48h,分化成肌管的成肌细胞经过1h的无血清处理后,用处理液处理,试验分四个处理:正常培养基、地塞米松处理(1um)、胰岛素处理(100nm)、地塞米松和胰岛素共同处理(DEX:1um;INS:100nm),处理液处理3h。结果表明,糖皮质激素能显著抑制IGF-I mRNA的表达,显著上调MyoG mRNA的表达,INS能显著上调MyoG mRNA的表达,显著抑制蛋白质分解途径的相关基因的表达,在INS存在时,糖皮质激素能上调MyoD、Atrogin-1的表达,提示糖皮质激素参与了细胞的新陈代谢。试验四是使用已分化成肌管的成肌细胞经过1h的无血清处理后,再用处理液处理,试验分两个处理:正常培养基、RU486(100nm)和地塞米松(1um)共同处理,正常培养基处理4h,RU486处理1h后,再用RU486和DEX共同处理3h。结果表明,RU486对IGF-I、MyoD、MSTN、MuRF1mRNA的表达量均无显著影响,说明RU486能抑制DEX的作用。
In order to study the effects of glucocorticoids on the protein metabolism of skeletal muscles in broiler chickens (Gallus gallus domesticus), we did the experiments in vivo and in vitro. In vivo, we used exogenous glucocorticoids to induce stress on the later stage of broilers’development, and in vitro, we treated the myoblasts of broiler chickens with dexamethasone. The mRNA level of several genes which were important for the protein metabolism were measured looking forward to constructing genetic regulatory networks of skeletal muscle protein metabolism as well as finding out its’detailed molecular mechanism.
The experiments in vivo were separated into two parts. In trial 1, 144 male AA broilers of 28 day were allocated into 12 treatments according to body weigh, 12 broilers per treatment. At the age of 29d, chickens were randomly separated into two groups: the basal diet group and the high protein ration, of which the latter was derived from a basal diet group through a 3d adjustment. At the age of 32d, chickens were randomly subjected to one of the following three treatments for 3 days: subcutaneous injection of DEX (2mg/kg BM), sham-treated (2 mg/kg BM of saline, control), sham-treated and limited-fed treatment to keep the feed consumption as that of the DEX chickens in the previous day. BM was recorded daily. At the age of 35d, half chickens of each treatment were randomly exposed to fasting for 12h or fasting 12h and refeeding 1h before samples were obtained. A blood sample was drawn from a wing vein by using a heparinized syringe within 30s and collected in iced tubes. Plasma was obtained after centrifugation at 400g for 10 min at 4°C and was stored at ?20°C for further analysis. Immediately after the blood sample had been obtained, the chicks were selected and sacrificed by exsanguination, and then harvested and weighed the breast and thigh muscle respectively. A 1 to 2g sample was respectively obtained from left PM, cooled down in liquid nitrogen and stored at -80℃for further analysis. The muscle of right leg and whole breast were harvested and weighed respectively, the breast and thigh mass were expressed as percentage of body mass (%). After three days’treatment, DEX had a significantly decrease (P<0.01) on daily gain of broiler chickens, in contrast, DEX had no significant (P>0.05) effect on food intake. The concentration of plasma uric acid (UA), total amino acid (T-AA) and insulin (INS) were higher at both sampling ages. The mRNA level of several genes that are important for protein proteolysis were significantly higher after three days exposure. The effect of glucocorticoid was not significantly inhibited by the high protein ration. In trial 2, 72 male AA broilers of 35 day were allocated into 12 treatments according to body weigh, 6 broilers per treatment. At the age of 36d, chickens were randomly subjected to one of the following two treatments for 3 days: subcutaneous injection of DEX (2mg/kg BM), sham-treated (2mg/kg BM of saline, control). BM was recorded daily. At the age of 38d, chickens of each treatment were exposed to fasting for 12h before blood samples were obtained. A blood sample was drawn from a wing vein by using a heparinized syringe within 30s and collected in iced tubes. After obtained the blood samples, every treatment was randomly separated into two perfusing treatments, leucine (500mg/kg BM) and salt (5ml). After perfusing 1h, another blood sample was drawn from a wing vein by using a heparinized syringe within 30 s and collected in iced tubes. Plasma was obtained after centrifugation at 400g for 10 min at 4°C and was stored at ?20°C for further analysis. Immediately after the blood sample had been obtained, the chicks were selected and sacrificed by exsanguination, and then harvested and weighed the breast and thigh muscle respectively. A 1 to 2g sample was respectively obtained from left PM, cooled down in liquid nitrogen and stored at -80℃for further analysis. The muscle of right leg and whole breast were harvested and weighed respectively, the breast and thigh mass were expressed as percentage of body mass (%). After three days treatment, DEX had a significantly decrease (P<0.01) on daily gain of broiler chickens, in contrast, DEX had no significant effect on food intake. The mRNA level of several genes that are important for protein proteolysis were significantly higher after three days exposure, while the mRNA level of genes that are important for protein synthesis were not significantly affected. The effect of glucocorticoid was not significantly inhibited by the perfusing of leucine.
The experiments in vitro were separated into two parts also. In trial 3, cells were cultured in DMEM medium containing 10% heat-inactivated FBS, when cells were 70% confluent, the proliferation medium was replaced by a differentiation medium containing 2% horse serum. After 48h of differentiation, cells were incubated for 1h with serum-free DMEM and subjected to different treatments for three hours including serum-free DMEM, 1uM Dexamethasone, 100nM Insulin, 1uM Dexamethasone and 100nM Insulin, four random fields of each of the six replicates were selected. The mRNA level of IGF-I was significantly inhibited by the treatment of dexamethasone after three hours’treatment, and the mRNA level of MyoG was significantly increased by the treatment of dexamethasone. The mRNA level of MyoG was significantly increased by the treatment of insulin, and the mRNA levels of several genes that are important for protein proteolysis were significantly inhibited by the treatment of insulin after three hours’treatment. When insulin was in the medium, the mRNA level of MyoD and Atrogin-1 was significantly increased by the treatment of glucocorticoid, which indicated that glucocorticoids had taken part in the metabolism of myoblasts. In trial 4, after 48h of differentiation, cells were incubated for 1h with serum-free DMEM and subjected to different treatments for three hours including serum-free DMEM, 100nm and RU486 1uM Dexamethasone (after the treatment of RU486 alone for 1h, the cells were treated with RU486 and dexamethosone for 3h), two random fields of each of the six replicates were selected. The mRNA levels of IGF-I、MyoD、MSTN、MuRF1 were not significantly affected by the treatment, which indicated that the effects of dexamethasone could be inhibited by the RU486.
体内试验分两部分:试验一选取28日龄体重相近的AA雄性肉鸡288只,随机分为正常日粮组和高蛋白日粮组,经过三天日粮适应期后,每个组随机分为三个处理:糖皮质激素处理组(DEX)、对照组、限饲组,每个处理3个重复,每个重复12只鸡,糖皮质激素处理组8:30和20:30,腹部皮下注射地塞米松1.0mg/kg体重,对照组、限饲组注射与糖皮质激素处理组等体积的生理盐水,限饲组饲喂糖皮质激素处理组前一天的采食量。34日龄晚20:30开始禁食。禁食后再饲喂组在35日龄早上8:30再饲喂一小时后采样。各试验鸡均翅静脉采血,3000r/min离心10min,分离血浆,-20℃冷冻保存。取胸大肌(M. pectoralis major,PM),液氮速冻,-80℃贮存。同时取部分组织样品。取全部胸肌称重,测定胸肌指数(胸肌重/活体重),取右腿全部肌肉称重,测定腿肌指数(腿肌重/活体重)。结果表明,糖皮质激素能使日增重显著降低,采食量无显著影响。糖皮质激素能使血浆中尿酸、T-AA、胰岛素的浓度显著上升。糖皮质激素能显著上调蛋白质分解途径相关基因的表达,对蛋白质合成途径的相关基因的抑制作用不明显。高蛋白日粮对缓解糖皮质激素的作用不明显。试验二选取35日龄体重相近的AA雄性肉鸡72只,随机分为2个组:糖皮质激素处理组(DEX)和对照组,每个处理3个重复,每个重复6只鸡。36-38日龄,8:00和20:00,糖皮质激素处理组皮下注射地塞米松1.0mg/kg体重,对照组注射相同体积的生理盐水。38日龄20:00禁食12h,禁食后(每个处理3个重复,每个重复取4只鸡)空腹采血,然后每个处理分A、B两个处理进行灌服处理:A组灌服亮氨酸500mg/Kg体重,B组灌服生理盐水5ml,灌服后1h,各试验鸡均翅静脉采血,3000r/min离心10min,分离血浆,-20℃冷冻保存。取胸大肌(M. pectoralis major,PM),液氮速冻,-80℃贮存。同时取部分组织样品。取全部胸肌称重,测定胸肌指数(胸肌重/活体重),取右腿全部肌肉称重,测定腿肌指数(腿肌重/活体重)。结果表明,糖皮质激素能使日增重显著降低,采食量无显著影响。糖皮质激素能显著促进蛋白质分解途径相关基因的表达。灌服对缓解糖皮质激素的作用也不明显。
体外试验分两个试验:试验三培养骨骼肌成肌细胞,细胞在含有10%的胎牛血清的DMEM培养基中生长,当细胞铺满六孔板的70%时,更换成含有2%马血清的DMEM培养基诱导成肌细胞分化成肌管,分化时间为48h,分化成肌管的成肌细胞经过1h的无血清处理后,用处理液处理,试验分四个处理:正常培养基、地塞米松处理(1um)、胰岛素处理(100nm)、地塞米松和胰岛素共同处理(DEX:1um;INS:100nm),处理液处理3h。结果表明,糖皮质激素能显著抑制IGF-I mRNA的表达,显著上调MyoG mRNA的表达,INS能显著上调MyoG mRNA的表达,显著抑制蛋白质分解途径的相关基因的表达,在INS存在时,糖皮质激素能上调MyoD、Atrogin-1的表达,提示糖皮质激素参与了细胞的新陈代谢。试验四是使用已分化成肌管的成肌细胞经过1h的无血清处理后,再用处理液处理,试验分两个处理:正常培养基、RU486(100nm)和地塞米松(1um)共同处理,正常培养基处理4h,RU486处理1h后,再用RU486和DEX共同处理3h。结果表明,RU486对IGF-I、MyoD、MSTN、MuRF1mRNA的表达量均无显著影响,说明RU486能抑制DEX的作用。
In order to study the effects of glucocorticoids on the protein metabolism of skeletal muscles in broiler chickens (Gallus gallus domesticus), we did the experiments in vivo and in vitro. In vivo, we used exogenous glucocorticoids to induce stress on the later stage of broilers’development, and in vitro, we treated the myoblasts of broiler chickens with dexamethasone. The mRNA level of several genes which were important for the protein metabolism were measured looking forward to constructing genetic regulatory networks of skeletal muscle protein metabolism as well as finding out its’detailed molecular mechanism.
The experiments in vivo were separated into two parts. In trial 1, 144 male AA broilers of 28 day were allocated into 12 treatments according to body weigh, 12 broilers per treatment. At the age of 29d, chickens were randomly separated into two groups: the basal diet group and the high protein ration, of which the latter was derived from a basal diet group through a 3d adjustment. At the age of 32d, chickens were randomly subjected to one of the following three treatments for 3 days: subcutaneous injection of DEX (2mg/kg BM), sham-treated (2 mg/kg BM of saline, control), sham-treated and limited-fed treatment to keep the feed consumption as that of the DEX chickens in the previous day. BM was recorded daily. At the age of 35d, half chickens of each treatment were randomly exposed to fasting for 12h or fasting 12h and refeeding 1h before samples were obtained. A blood sample was drawn from a wing vein by using a heparinized syringe within 30s and collected in iced tubes. Plasma was obtained after centrifugation at 400g for 10 min at 4°C and was stored at ?20°C for further analysis. Immediately after the blood sample had been obtained, the chicks were selected and sacrificed by exsanguination, and then harvested and weighed the breast and thigh muscle respectively. A 1 to 2g sample was respectively obtained from left PM, cooled down in liquid nitrogen and stored at -80℃for further analysis. The muscle of right leg and whole breast were harvested and weighed respectively, the breast and thigh mass were expressed as percentage of body mass (%). After three days’treatment, DEX had a significantly decrease (P<0.01) on daily gain of broiler chickens, in contrast, DEX had no significant (P>0.05) effect on food intake. The concentration of plasma uric acid (UA), total amino acid (T-AA) and insulin (INS) were higher at both sampling ages. The mRNA level of several genes that are important for protein proteolysis were significantly higher after three days exposure. The effect of glucocorticoid was not significantly inhibited by the high protein ration. In trial 2, 72 male AA broilers of 35 day were allocated into 12 treatments according to body weigh, 6 broilers per treatment. At the age of 36d, chickens were randomly subjected to one of the following two treatments for 3 days: subcutaneous injection of DEX (2mg/kg BM), sham-treated (2mg/kg BM of saline, control). BM was recorded daily. At the age of 38d, chickens of each treatment were exposed to fasting for 12h before blood samples were obtained. A blood sample was drawn from a wing vein by using a heparinized syringe within 30s and collected in iced tubes. After obtained the blood samples, every treatment was randomly separated into two perfusing treatments, leucine (500mg/kg BM) and salt (5ml). After perfusing 1h, another blood sample was drawn from a wing vein by using a heparinized syringe within 30 s and collected in iced tubes. Plasma was obtained after centrifugation at 400g for 10 min at 4°C and was stored at ?20°C for further analysis. Immediately after the blood sample had been obtained, the chicks were selected and sacrificed by exsanguination, and then harvested and weighed the breast and thigh muscle respectively. A 1 to 2g sample was respectively obtained from left PM, cooled down in liquid nitrogen and stored at -80℃for further analysis. The muscle of right leg and whole breast were harvested and weighed respectively, the breast and thigh mass were expressed as percentage of body mass (%). After three days treatment, DEX had a significantly decrease (P<0.01) on daily gain of broiler chickens, in contrast, DEX had no significant effect on food intake. The mRNA level of several genes that are important for protein proteolysis were significantly higher after three days exposure, while the mRNA level of genes that are important for protein synthesis were not significantly affected. The effect of glucocorticoid was not significantly inhibited by the perfusing of leucine.
The experiments in vitro were separated into two parts also. In trial 3, cells were cultured in DMEM medium containing 10% heat-inactivated FBS, when cells were 70% confluent, the proliferation medium was replaced by a differentiation medium containing 2% horse serum. After 48h of differentiation, cells were incubated for 1h with serum-free DMEM and subjected to different treatments for three hours including serum-free DMEM, 1uM Dexamethasone, 100nM Insulin, 1uM Dexamethasone and 100nM Insulin, four random fields of each of the six replicates were selected. The mRNA level of IGF-I was significantly inhibited by the treatment of dexamethasone after three hours’treatment, and the mRNA level of MyoG was significantly increased by the treatment of dexamethasone. The mRNA level of MyoG was significantly increased by the treatment of insulin, and the mRNA levels of several genes that are important for protein proteolysis were significantly inhibited by the treatment of insulin after three hours’treatment. When insulin was in the medium, the mRNA level of MyoD and Atrogin-1 was significantly increased by the treatment of glucocorticoid, which indicated that glucocorticoids had taken part in the metabolism of myoblasts. In trial 4, after 48h of differentiation, cells were incubated for 1h with serum-free DMEM and subjected to different treatments for three hours including serum-free DMEM, 100nm and RU486 1uM Dexamethasone (after the treatment of RU486 alone for 1h, the cells were treated with RU486 and dexamethosone for 3h), two random fields of each of the six replicates were selected. The mRNA levels of IGF-I、MyoD、MSTN、MuRF1 were not significantly affected by the treatment, which indicated that the effects of dexamethasone could be inhibited by the RU486.
引文
岑石强,杨志明.成肌细胞在基因治疗和组织工程中的应用[J].中国修复重建外科杂志, 1999, 13 (3) : 173-177.
郭旭明,陈家伦.糖皮质激素受体拮抗剂-RU486的作用机制及临床研究[J].《国外医学》内分泌学分册,1993, 13(2): 64-67.
黄祯祥,洪涛,刘崇柏.医学病毒学基础及实验技术[M].科学出版社,1990:149-162.
刘丑生,赵兴波,李宁,赵有璋.动物肌肉生长发育调控的功能基因研究进展[J].中国畜牧杂志,2003,39(5):48-49.
刘立斌,周红雨.成肌细胞的临床应用现状及前景[J].中国修复重建外科杂志,2007,21(7): 767-770.
刘欣春,朱悦.胰岛素样生长因子-1对骨骼肌源性干细胞的促增殖效应[J].解剖学报,2008,39(1): 79-82.
龙定彪,张克英,陈代文,李建文,余冰.肌肉生长抑制素的研究进展[J].动物营养学报,2007,19: 498-502.
王兵,刘贻运,郑介柏,袁士翔.骨延长术中的骨钙素和胰岛素样因子-I的含量变化[J].中国矫形外科杂志,2002,9(3): 267-269.
王明若,王兴龙,韩文瑜.现代动物免疫学[M].吉林科技出版社,1996: 400-405.
王志钢,吴应积,旭日干. mTOR信号通路与细胞生长调控[J].生物物理学报,2007,23(5): 333-342.
魏宗友,徐柏林,郝志敏,王曙.氨基酸转运载体的研究进展[J].中国饲料,2010,13: 19-25.
薛慧良.胰岛素样生长因子系统的研究进展[J].生物学教学,2007,32(11):4-6.
张鹏,陈世益.成肌细胞在肌肉骨骼系统疾病基因治疗中的应用研究进展[J].中国运动医学杂志, 2003, 22 (5) : 483-486, 489.
朱伦,陈增良. mTOR的结构与功能[J].国际病理科学与临床杂志,2006,26: 31-34.
Anker S D, Clark A L, Kemp M, Salsbury C, Teixeira M M, Hellewell P G, Coats A J. Tumor necrosis factor and steroid metabolism in chronic heart failure: possible relation to muscle wasting[J]. Journal of the American College of Cardiology, 1997, 30: 997-1001.
Anthony G, Bernadette C, Michel J D. Nutrient supply enhances both IGF-I and MSTN mRNA levels in chicken skeletal muscle[J]. Domestic Animal Endocrinology, 2004, 26: 143-154.
Armstrong D G, Hogg C O. Type-I insulin-like growth factor receptor gene expression in the chick. Developmental changes and the effect of selection for increased growth on the amount of receptor mRNA[J]. Journal of Endocrinology, 1994, 12: 3-12.
Artaza J N, Bhasin S, Mallidis C, Taylo R W, Ma K, Gonzalez-Cadavid N F. Endogenous expression and localization of myostatin and its relation to myosin heavy chain distribution in C2C12 skeletal muscle cells[J]. Cellular Physiology, 2002, 190: 170-179.
Auclair D, Garrel D R, Chaouki Z A, Ferland L H. Activation of the ubiquitin pathway in rat skeletal muscle by catabolic doses of glucocorticoids[J]. American Journal of Physiology Cell Physiol, 1997, 272: C1007-C1016.
Bailey P, Tamara H, Andrew B L, The origin of skeletal muscle stem cells in the embryo and the adult[J]. Current Opinion of Cell Biology, 2001, 13: 679-689.
Ballard F J, Francis G L. Effects of anabolic agents on protein breakdown in L6 myoblasts[J]. Biochemical Journal, 1983, 210: 243-249.
Ballard F J, Johnson R J, Owens P C, Francis G L, Upton F M, McMurtry J P, Wallace J C. Chicken insulin-like growth factor-I: Amino acid sequence, radioimmunoassay, and plasma levels between strains and during growth[J]. General Comparative Endocrinology, 1990, 79: 459-468.
Baldwin K M, Herrick R E, Ilyina-Kakueva E, Oganov V S. Effects of zero gravity on myofibril content and isomyosin distribution in rodent skeletal muscle[J]. The FASEB Journal, 1990, 4: 79-83.
Bartov I. Effects of dietary protein concentration and corticosterone injections on energy and nitrogen balances and fat deposition in broiler chicks[J]. British Poultry Science, 1985, 26: 311-324.
Bodine S C, Latres E, Baumhueter S, Lai V K, Nunez L, Clarke B A, Poueymirou W T, Panaro F J, Na E, Dharmarajan K, Pan Z Q, Valenzuela D M, Dechiara T M, Stitt T N, Yancopoulos G D, Glass D J. Identification of ubiquitin ligases required for skeletal muscle atrophy[J]. Science, 2001, 294: 1704-1708.
Bodine S. C, Stitt T N, Gonzalez M, Kline W O, Stover G L, Bauerlein R, Zlotchenko E, Scrimgrour A, Lawrence J C, Glass D J, Yancopoulos G D. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo[J]. Nature Cell Biology, 2001, 3: 1014-1019.
Boushy A R EL. Vitamin E affects viability, immune response of poultry[J]. Feedstuffs, 1988, 60(44): 20-26.
Bowes S B, Jackson N C, Papachristodoulou D, Umpleby A M, Sonksen P H. Effect of corticosterone on protein degradation in isolated rat soleus and extensor digitorum longus muscles[J]. Journal of Endocrinology, 1996, 148: 501-507.
Braun T, Rudnicki M A, Arnold H H, Jaenisch R. Targeted inactivation of the muscle regulatory gene Myf-5 results in abnormal rib development and perinatal death[J]. Cell, 1992, 71: 369-382.
Broer S, Adaptation of plasma membrane amino acid transport mechanisms to physiological demands[J]. European Journal of Physiology. 2002, 444, 457-466.
Butler A A, LeRoith D. Minireview: tissue-specific versus generalized gene targeting of the igf1 and igf1r genes and their roles in insulin-like growth factor physiology[J]. Endocrinology, 2001, 142:1685-1688.
Carlson C J, Booth F W, Gordon S E. Skeletal muscle myostatin mRNA expression is fiber-type specific and increases during hindlimb unloading[J]. American Journal of Physiology: Regulatory, Integrative and Comparative Physiology, 1999, 277: R601-R606.
Centner T, Yano J, Kimura E, McElhinny A S, Pelin K, Witt C C, Bang M L, Trombitas K, Granzier H, Gregorio C C, Sorimachi H, Labeit S. Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain[J]. Molecular Biology, 2001, 306: 717-726.
Clarke B A, Drujan D, willis M S, Murphy L O, Corpina R A, Stitt T N, Patterson C, Latres E, Glass D J. The E3 ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle[J]. Cell Metabolism, 2007, 6: 376-385.
Dardevet D, Sornet C, Taillandier D, Savary I, Attaix D, Grizard J. Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and oldrats. Lack of regulation of the ubiquitin-proteasome proteolytic pathway in aging[J]. Journal of Clinical Investigation, 1995, 96: 2113-2119.
Dehoux M, Van Beneden R, Pasko N, Lause P, Verniers J, Underwood L, Ketelslegers J M, Thissen J P. Role of the insulin-like growth factor I ecline in the induction of Atrogin-1/MAFbx during fasting and diabetes[J]. Endocrinology, 2004, 145: 4806-4812.
Desler M M, Jones S J, Smith C W, Woods T L. Effects of dexamethasone and anabolic agents on proliferation and protein synthesis and degradation in C2C12 myogenic cells[J]. Journal of Animal Science, 1996, 74: 1265-1273.
Deves R, Boyd C A, Transporters for cationic amino acids in animal cells: discovery, structure, and function[J]. Physiological Reviews, 1998, 78: 487-545.
Dodson M V, Allen R E, Hossner K L. Ovine somatomedin, multiplication-stimulating activity, and insulin promote skeletal muscle satellite cell proliferation in vitro[J]. Endocrinology, 1985, 117: 2357-2363.
McFarland D C, Velleman S G, Pesall J E, Liu C, The role of myostatin in chicken (Gallus domesticus) myogenic satellite cell proliferation and differentiation[J]. General and Comparative Endocrinology, 2007, 151: 351-357.
Duclos M J, Wilkie R S, Goddard C. Stimulation of DNA synthesis in chicken muscle satellite cells by insulin and insulin-like growth factors: Evidence for exclusive mediation by a type-I insulin-like growth factor receptor[J]. Journal of Endocrinology, 1991, 128: 35-42.
El-Habbak M M, Abou-El-Soud S B, Ebeid T A. Effect of induced stress by dexamethasone administration on performance, egg quality and some blood parameters of laying hens[J]. Egyptian Poultry Science, 2005, 25: 89-105.
Falconer J, Harvey S, Forbes J M, Scanes C G. Changes in somatomedin-like activity and growth hormone concentrations in the plasma of the domestic fowl (Callus domesticus) [J]. AJEBAK, 1981, 59: 529-639.
Fan J, Molina P E, Gelato M C, Lang C H. Differential tissue regulation of insulin-like growth factor-1 content and binding protein after endotoxin[J]. Endocrinology, 1994, 134(4): 1685-1692.
Fawcett D H, Bulfied G. Molecular cloning, sequence analysis and expression of putativechicken insulin-like growth factor-I cDNAs[J]. Journal of Molecular Endocrinology, 1990, 4: 201-211.
Florini J R, Ewton D Z, Coolican S A. Growth hormone and the insulin-like growth factor system in myogenesis[J]. Endocrine Reviews 1996, 17: 481-517.
Fournier M, Huang Z S, Li H, Da X, Cercek B, Lewis M I. Insulin-like growth factor-I prevents corticosteroid-induced diaphragm muscle atrophy in emphysematous hamsters[J]. American Journal of Physiology, Regulatory, Integrative and Comparative Physiology, 2003, 285: R34-R43.
Frost R A, Lang C H. Regulation of insulin-like growth factor-I in skeletal muscle and muscle cells[J]. Minerva Endocrinologica, 2003, 28: 53-73.
Furukawa-Hibi Y, Yoshida-Araki K, Ohta T, Ikeda K, Motoyama N. FOXO forkhead transcription factors induce G2-M checkpoint in response to oxidative stress[J]. Journal of Biological Chemistry, 2002, 277: 26729-26732.
Gayan-Ramirez G., Vanderhoydonc F, Verhoeven G., Decramer M. Acute treatment with corticosteroids decreases IGF-1 and IGF-2 expression in the rat diaphragm and gastrocnemius[J]. American Journal of Respiratory and Critical Care Medicine, 1999, 159: 283-289.
Glass D J. Skeletal muscle hypertrophy and atrophy signaling patyway[J]. Biochemistry and Cell Biology, 2005, 37: 1974-1984.
Gomes M D, Lecker S H, Jagoe R T, Navon A, Goldberg A L. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy[J]. National Academy of Sciences Proc, 2001, 98: 14440-14445.
Gomes-Marcondes M C, Tisdale M J. Induction of protein catabolism and the ubiquitin-proteasome pathway by mild oxidative stress[J]. Cancer Lett, 2002, 180: 69-74.
Gonzalez-Cadavid N F, Taylor W E, Yarasheski K. Organization of the human MSTN gene and expression in healthy men and HIV-infected men with muscle wasting[J]. American Journal of Physiology, Regulatory, Integrative and Comparative Physiology, 1998, 95(25): 14938-43.
Gould N R, Siegel H S. Serum lipoproteins in chickens after administration ofadrenocorticotropin or exposure to high temperature[J]. Poultry Science, 1985, 64: 567-574.
Grizard J, Dardevet D, Papet I, Mosoni L, Mirand P P. Nutrient regulation of skeletal muscle protein metabolism in animals, the involvement of hormines and substrates[J]. Nutrition Research Reviews, 1995, 8: 67-91.
Grobet L, Royo L J, Poncelet D, Pirottin D, Brouwers B, Riquet J, Schoeberlein A, Dunner S, Menissier F, Massabanda J, Fries R., Hanset R, Georges. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle[J]. Nature Genetics, 1997, 17: 71-74.
Hasselgren P O. Burns and metabolism[J]. Journal of the American College of Surgeons, 1999, 188: 98-103.
Hasty P, Bradley A, Morris J H, Edmondson D G, Venuti J M, Olson E N, Klein W H. Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene[J]. Nature, 1993, 364: 501-506.
Hershko A, Ciechanover A. The ubiquitin system[J]. Annual Review of Biochemistry, 1998, 67: 425-479.
Hogan B L. Bone morphogenetic proteins in development[J]. Current Opinion in Genetics and Development, 1996, 10: 1580-1594.
Hong D H, Forsberg N E. Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures[J]. Molecular Cell Endocrinology, 1995, 108: 199-209.
Hoshino S, Wakita M, Suzuki M, Yamamoto K. Changes in somatomedin-like factor and immunoassayable growth hormone during growth of normal and dwarf pullets and cockerels[J]. Poultry Science, 1982, 61: 777-784.
Humphrey B D, Stephensen C B, Calvert C C, Klasing K C. Glucose and cationic amino acid transporter expression in growing chickens (Gallus gallus domesticus) [J].Comparative Biochemistry and Physiology, 2004, A 138: 515-525.
Humphrey B D, Kirk C K. The acute phase response alters cationic amino acid transporter expression in growing chickens (Gallus gallus domesticus) [J], Comparative Biochemistry and Physiology, 2005, Part A 142: 485-494.
Humphrey B D, Stephensen C B, Calvert C C, Klasing K C. Lysine deficiency and feed restriction independently alter cationic amino acid transporter expression in chickens (Gallus gallus domesticus) [J]. Comparative Biochemistry and Physiology, 2006, Part A 143: 218-227.
Jackman R W, Kandarian S C. The molecular basis of skeletal muscle atrophy[J]. American Journal of Physiology, 2004, 287: C834-C843.
Jagoe R T, Goldberg A L. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy[J]? Current Opinion in Clinical Nutrition and Metabolism Care, 2001, 4: 183-190.
Jagoe R T, Lecker S H, Gomes M, Goldberg A L. Patterns of gene expression in atrophying skeletal muscles: Response to food deprivation[J]. The FASEB Journal, 2002, 16: 1697-1712.
Jeanplong F, Bass J J, Smith H K, Kirk S P, Kambadur R, Sharma M, Oldham J M. Prolonged underfeeding of sheep increases myostatin and myogenic regulatory factor Myf-5 in skeletal muscle while IGF-I and myogenin are repressed[J]. Journal of Endocrinology, 2003, 176: 425-437.
Ji S, Losinski R L, Cornelius S G., Frank G. R, Willis G. M, Gerrard D E, Depreux F F, Spurlock M E. Myostatin expression in porcine tissues: tissue specificity and developmental and postnatal regulation[J]. American Journal of Physiology, 1998, 275: R1265-R1273.
Kajimoto Y, Rotwein P. Structure and expression of a chicken insulin-like growth factor I precursor[J]. Molecular Endocrinology, 1989, 3: 1907-1913.
Kajimoto Y, Rotwein P. Structure of the chicken insulin-like growth factor I gene reveals conserved promoter elements[J]. Journal of Biological Chemistry, 1991, 266: 9724-9731.
Kallincos N C, Wallace J C, Francis G L, Ballard F J. Chemical and biological characterization of chicken insulin-like growth factor-II[J]. Journal of Endocrinology, 1990, 124: 89-97.
Kambadur R, Sharma M, Smith TPL, Bass J J. Mutations in myostatin (GDF-8) in double-muscled Belgian Blue and Piedmontese cattle[J]. Genome Research, 1997, 7:910-915.
Kanda F, Takatani K, Okuda S, Matsushita T, Chihara K, Preventive effects of insulin-like growth factor-I on steroid-induced muscle atrophy[J]. Muscle and Nerve, 1999, 22: 213-217.
Karim L, Coppieters W, Grobet L, Valentini A, Georges M. Convenient genotyping of six myostatin mutations causing double-muscling in cattle using a multiplex oligonucleotide ligation assay[J]. Animal Genetics, 2000, 31: 396-399.
Kayali A G, Goodman M N, Lin J, Young V R. Insulin- and thyroid hormone-independent adaptation of myofibrillar proteolysis to glucocorticoids[J]. American Journal of Physiology, 1990, 259: E699-E705.
Kayali A G, Young V R, Goodman M N. Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis[J]. American Journal of Physiology Endocrinology and Metabolism, 1987, 252: E621-E626.
Kenneth J L, Thomas D S. Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2-△△Ct Method[J]. METHODS, 2001, 25: 402-408.
Kettelhut I C, Wing S S, Goldberg A J. Endocrine regulation of protein breakdown in skeletal muscle[J]. Diabetes/Metabolism Reviews, 1988, 4: 751-772.
Kikuchi K, Buonomo F C, Kajimoto Y, Rotwein P. Expression of insulin-like growth factor-I during chicken development[J]. Endocrinology, 1991, 128: 1323-1328.
Kimball S R, Vary T C, Jefferson L S. Regulation of protein synthesis by insulin[J]. Annual Review of Physiology, 1994, 56: 321-348.
Kocamis H, McFarland D. C, Killefer J. Temporal expression of growth factor genes during myogenesis of satellite cells derived from the biceps femoris and pectoralis major muscles of the chicken[J]. Cell Physiology, 2001, 186: 146-152.
Kuhn E R, Darras V M, Gysemans C, Decuypere E, Berghman L R, Buyse J. The use of intermittent lighting in broiler raising. II. Effects on the somatotropic and thyroid axes and on plasma testosterone levels[J]. Poultry Science, 1996, 75: 595-600.
Kulik G, Klippel A, Weber M J. Anti-apoptotic signaling by the insulin like growth factor-I receptor, phosphatidylinositol 3-kinase, and Akt[J]. Molecular Cell Endocrinology, 1997, 17: 1595-1606.
Lalani R, Bhasin S, Byhower F, Tarnuzzer R, Grant M, Shen R, Asa S, Ezzat S, Gonzalez-Cadavid N F. Myostatin and insulin-like growth factor-I and-II expression in the muscle of rats exposed to the microgravity environment of the Neuro Lab space shuttle ?ight[J]. Journal of Endocrinology, 2000, 167: 417-428.
Lang C H, Silvis C, Nystrom G., Frost R A. Regulation of myostatin by glucocorticoids after thermal injury[J]. The FASEB Journal, 2001, 15: 1807-1809.
Latres E, Amini A R, Amini A A, Grifiths J, Martin F J, Wei Y, Lin H C, Yancopoulos G. D, Glass D J. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-Kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway[J]. Biological Chemistry, 2005, 280: 2737-2744.
Lazar M A. Steroid and thyroid hormone receptors[J]. Endocrinology and Metabolism Clinics of North America, 1991, 20(4): 681-695.
Lee S J, McPherron A C. Regulation of MSTN activity and muscle growth[J]. Proceedings of the National Academy of Sciences of the United States of America, 2001, 98: 9306-9311.
Li B G, Hasselgren P O, Fang C H, Warden G D. Insulin-like growth factor-I blocks dexamethasone-induced protein degradation in cultured myotubes by inhibiting multiple proteolytic pathways: ABA paper[J]. Journal of Burn Care and Rehabilitation, 2002, 25: 112-118.
Li Y P, Schwartz R J, Waddell I D, Holloway B R, Reid M B. Skeletal muscle myocytes undergo protein loss and reactive oxygenmediated NF-kB activation in response to tumor necrosis factorα[J]. The FASEB Journal, 1998, 12: 871-880.
Li Z F, Shelton G D, Engvall E. Elimination of myostatin does not combat muscular dystrophy in dy mice but increases postnatal lethality[J]. American Journal of Pathology, 2005, 166: 491-497.
Lin H, Decuypere E, Buyse J. Oxidative stress induced by corticosterone administration in broiler chickens (Gallus gallus domesticus): 1. chronic exposure[J]. Biochemistry and Molecular Biology, 2004, 139: 737-744.
Lin H, Sui S J, Jiao H C, Buyse J, Decuypere E. Impaired development of broiler chickens by stress mimicked by corticosterone exposure[J]. Comparative Biochemistry andMolecular Biology, 2006, 143: 400-405.
Lin H, Sui S J, Jiao H C, Jiang K J, Zhao J P, Dong H. Effects of diet and stress mimicked by corticosterone administration on early postmortem muscle metabolism of broiler chickens[J]. Poultry Science, 2007, 86: 545-554.
Liu W, Chen B, Deng D, Xu F, Cui L, Cao Y L. Repair of tendon defect with dermal fibroblast engineered tendon in a porcine model[J]. Tissue Engineering, 2006, 12(4): 775-788.
Long W, Wei L P, Barrett E J. Dexamethasone inhibits the stimulation of muscle protein synthesis and PHAS-I and p70S6-kinase phosphorylation[J]. American Journal of Physiology Endocrinology and Metabolism, 2000, 280: 570-575.
Ma K, Mallidis C, Artaza J, Taylor W, Gonzalez-Cadavid N, Bhasin S. Characterization of 5’-regulatory region of human myostatin gene: regulation by dexamethasone in vitro[J]. American Journal of Physiology Endocrinology and Metabolism, 2001, 281: E1128-E1136.
Ma K, Mallidis C, Bhasin S, Mahabadi V, Artaza J, Gonzalez-Cadavid N, Arias, Salehian B. Glucocorticoid-induced skeletal muscle atrophy is associated with upregulation of myostatin gene expression[J]. American Journal of Physiology Endocrinology and Metabolism, 2003, 285: E363-E371.
Malheiros R D, Moraes V M, Collin A, Decuypere E, Buyse J. Free diet selection by broilers as influenced by dietary macronutient ratio and corticosterone supplementation. 1. Diet selection, organ weight, and plasma metabolites[J]. Poultry Science, 2003, 82: 123-131.
Matsumura Y, Domeki M, Sugahara K, Kubo T, Roberts C T Jr, LeRoith D, Kato H. Nutritional regulation of insulin-like growth factor-I receptor mRNA levels in growing chickens[J]. Bioscience Biotech Biochem, 1996, 60: 979-982.
Matteri R L, Carroll J A, Dyer C J. Neuroendocrine responses to stress[J]. Biology of Animal Stress, 2000, 43-76.
McMurtry J P, Francis G L, Upton F Z, Rosselot G, Brocht D M. Developmental changes in chicken and turkey insulin-like growth factor-I (IGF-I) studied with a homologous radioimmunoassay for chicken IGF-I[J]. Journal of Endocrinology, 1994, 142: 225-234.
McPherron A C, Lawler A M, Lee S J. Regulation of skeletal muscle mass in mice by a newTGF-βsuperfamily member[J]. Nature, 1997, 387: 83-90.
McPherron A C, Lee S J. Double muscling in cattle due to mutations in the myostatin gene[J]. Proceedings of the National Academy of Science of the USA, 1997, 94: 12457-12461.
Mitch W E, Goldberg A L. Mechanisms of muscle wasting: The role of the ubiquitin-proteasome pathway[J]. New England Journal of Medicine, 1996, 335: 1897-1905.
Montagne J, Stewart M J, Stocker H, Hafen E, Kozma S C, Thomas G. Drosophila S6 kinase: a regulator of cell size[J]. Science, 1999, 285: 2126-2129.
Morishita D, Wakita M, Hoshino S. Effect of hypophysectomy on insulin-like growth factor (IGF)-I binding activity of serum in chickens[J]. Comparative Biochemistry and Physiology, 1993, 104 A: 261-265.
Munoz K A, Satarug S, Tischler M E. Time course of the response of myofibrillar and sarcoplasmic protein metabolism to unweighting of the soleus muscle[J]. Metabolism, 1993, 42: 1006-1012.
Musaro A, Rosenthal N. Attenuating muscle wasting: cell and gene therapy approaches[J]. Current Genomics, 2003, 4: 575-585.
Nabeshima Y, Hanaoka K, Hayasaka M, Esumi E, Li S, Nonaka I. Myogenin gene disruption results in perinatal lethality because of severe muscle defect[J]. Nature, 1993, 364: 532-535.
Okumura J, Kita K. Recent advance in the relationship between endocrine status and nutrition on chickens[J]. Asian-Australasian Journal of Animal Sciences, 1999, 12 (7): 135-141. Oldham S, Montagne J, Radimerski T, Thomas G, Hafen E. Genetic and biochemical
characterization of dTOR, the Drosophila homolog of the target of rapamycin. Genes Development, 2000, 14: 2689-2694.
Palacin M, Estevez R, Bertran J, Zorzano A. Molecular biology of mammalian plasma membrane amino acid transporters[J]. Physiological Reviews, 1998, 78: 969-1038.
Patel K, Amthor H. The function of myostatin and strategies of myostatin blockade-new hope for therapies aimed at promoting growth of skeletal muscle[J]. Neuromuscular Disorders, 2005, 1: 117-126.
Polak P, Hall M, N. mTOR and the control of whole body metabolism[J]. Current Opinion inCell Biology, 2009, 21: 209-218.
Puvadolpirod S. Model of physiological stress in Chickens.2. dosimetry of adrenocorticotropin[J]. Poultry Science, 2000, 79: 370-376.
Rios R, Carneiro I, Arce V M. Devesa J. Myostatin regulates cell survival during C2C12 myogenesis[J]. Biochemical and Biophysical Research Communications, 2001, 19: 561-566.
Rios R, Carneiro I, Arce V M, Devesa J. Myostatin is an inhibitor of myogenic differentiation[J]. American Journal of Physiology Cell Physiology, 2002, 282: 993-999.
Roeder R A, Thorpe S D, Byers F M, Schelling G T, Gunn J M. Influence of anabolic agents on protein synthesis and degradation in muscle cells grown in culture[J]. Growth, 1986, 50: 485-495.
Rommel C, Bodine S C, Clarke B A, Rossman R, Nunez L, Stitt T N, Yancopoulos G D, Glass D J. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI (3)K/Akt/mTOR and PI(3)K/Akt/ GSK3 pathways[J]. Nature Cell Biology, 2001, 3(11): 1009-1013.
Rosselot G, McMurtry J P, Vasilatos-Younken R, Czerwinski S. Effect of exogenous chicken growth hormone (cGH) administration on insulin-like growth factor-I (IGF-I) gene expression in domestic fowl[J]. Molecular and Cellular Endocrinology, 1995, 114: 157-166.
Roy R R, Gardiner P F, Simpson D R, Edgerton V R. Glucocorticoid-induced atrophy in different fiber types of selected rat jaw and hind-limb muscles[J]. Archives of Oral Biology, 1983, 28: 639-643.
Rudnicki M A, Braun T, Hinuma S, Jaenisch R. Inactivation of MyoD in mice leads to up-regulation of the myogenic HLH gene Myf-5 and results in apparently normal muscle development[J]. Cell, 1992, 71: 383-390.
Rudnicki M A, Schnegelsberg P N, Stead R H, Braun T, Arnold H H, Jaenisch R. MyoD or Myf-5 is required for the formation of skeletal muscle[J]. Cell, 1993, 75: 1351-1359.
Sacheck J M. Expression of muscle-specific ubiquitin-protein ligases (E3s) during muscle atrophy [J]. The FASEB Journal, 2003, 17: A9578.
Sacheck J M, Ohtsuka A, McLary C, Goldberg A L. IGF-1 stimulates muscle growth bysuppressing protein breakdown and expression of atrophy-related ubiquitin-ligases, atrogin-1 and MuRF1[J]. American Journal of Physiology Endocrinology and Metabolism, 2004, 287: 591-601.
Saier M H. Genome archeology leading to the characterization and classification of transport proteins[J]. Current Opinion Microbiology, 1999, 2: 555-561.
Samani A A, Brodt P. The receptor for the type 1 insulin-like growth factor and its ligands regulate multiple cellular functions that impact on metastasis[J]. Journal of Surgical Oncology Clinics of North America, 2001, 10 (2): 289-312.
Sandri M, Sandri C, Gilbert A, Skurk C, Calabria, E, Picard A, Walsh K, Schiaffino S, Lecker S H, Goldberg A L. Foxo transcription factors induce the atrophy-related ubiquitin ligase Atrogin-1 and cause skeletal muscle atrophy[J]. Cell, 2004, 117: 399-412.
Sarbassov D D, Ali S M, Sabatini D M. Growing roles for the mTOR pathway[J]. Current Opinion in Cell Biology, 2005, 17: 596-603.
Scanes C G, Duyka D R, Lauterio T J, Bowen S J, Huybrechts L M, Bacon W L, King D B. Effect of chicken growth hormone, triiodothyronine and hypophysectomy in growing domestic fowl[J]. Growth, 1986, 50: 12-31.
Schakman O, Gilson H de C V, Lause P, Verniers J, Havaux X, Ketelslegers J M, Thissen J P. Insulin-like growth factor-I gene transfer by electroporation prevents skeletal muscle atrophy in glucocorticoid treated rats[J]. Endocrinology, 2005, 146: 1789-1797.
Scheuermann G. N, Bilgili S F, Hess J B, Mulvaney D R. Brest muscle development in commercial broiler chickens[J]. Poultry Science, 2003, 82: 1648-1658.
Schuelke M , Kathryn R, Wagner M D, Leslie E, Stolz L E, Hubner C, Riebel T, Komen W, Braun T, Tobin J F, Lee S J. Myostatin mutation associated with gross muscle hypertrophy in a child[J]. The New England Journal Medicine, 2004, 350: 2682-2688.
Seene T. Turnover of skeletal muscle contractile proteins in glucocorticoid myopathy[J]. The Journal of Steroid Biochemistry and Molecular Biology, 1994, 50: 1-4.
Shah O J, Anthony J C, Kimball S R, Jefferson L S. Glucocorticoids oppose translational control by leucine in skeletal muscle[J]. American Journal of Physiology Endocrinology and Metabolism, 2000, 279: E1185–E1190.
Shoji S. Myofibrillar protein catabolism in rat steroid myopathy measured by 3-methylhistidine excretion in the urine[J]. Journal of Neurological Sciences, 1989, 93: 333-340.
Shogi S, Pennington R J. The effect of cortisone on protein breakdown and synthesis in rat skeletal muscle[J]. Molecular and Cellular Endocrinology, 1977, 6: 159-169.
Sjogren K, Liu J L, Blad K, Skrtic S, Vidal O, Wallenius V, Leroith D, Tornell J, Isalsson O P, Jansson J O, Ohlsson, C. Liver derived insulin-like growth factor I (IGF-I) is the principal source of IGF-I in blood but is not required for postnatal body growth in mice[J]. Proceedings of the National Acadamy of Science of USA, 1999, 96: 7088-7092.
Sloan J L, Mager S. Cloning and functional expression of a human Na (+) and Cl(-)-dependent neutral and cationic amino acid transporter B(0+)[J]. Journal of Biological Chemistry, 1999, 274: 23740-23745.
Smith I J, Aversa Z, Alamdari N, Petkova V, Hasselgren P O. Sepsis downregulates myostatin mRNA levels without altering myostatin protein levels in skeletal muscle[J]. Journal of Cell Biochemistry, 2010, 11: 1059-1073.
Southorn B G, Palmer R M, Garlick P J. Acute effects of corticosterone on tissue protein synthesis and insulin sensitivity in rats in vivo[J]. Biochemical Journal, 1990, 272: 187-191.
Spencer E M,Liu C C. In vivo actions of Insulin like growth factor-1 on bone formation and resorption in rats[J]. Bone, 1991, 12(4): 21-26.
Steele R. Influences of corticosteroids on protein and carbohydrate metabolism[J]. Handbook of Physiology, 1975, 6: 135-168.
Szabo G, Dallmann G, Muller G, Patthy L, Soller M, Varga L. A deletion in the myostatin gene causes the compact (Cmpt) hypermuscular mutation in mice[J]. Mammalian Genome, 1998, 9: 671-672.
Tanaka M, Hayashida Y, Sakaguchi K, Ohkubo T, Wakita M, Hoshino S, Nakashima K. Growth hormone-independent expression of insulin-like growth factor I messenger ribonucleic acid in extrahepatic tissues of the chicken[J]. Endocrinology, 1996, 137: 30-34.
Taylor W E, Bhasin S, Artaza J, Byhower F, Azam M, Willard D H Jr, Kull F C Jr,Gonzalez-Cadavid N. Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells[J]. American Journal of Physiology Endocrinology and Metabolism, 2001, 280: E221-E228.
te Pas M F, de Jong P R, Verburg F J. Glucocorticoid inhibition of C2C12 proliferation rate and differentiation capacity in relation to mRNA levels of the MRF gene family[J]. Molecular Biology Reports, 2000, 27: 87-98.
te Pas M F, de Jong P R, Verburg F J, Duin M., Henning R H. Gender related and dexamethasone induced differences in the mRNA levels of the MRF genes in rat anterior tibial skeletal muscle[J]. Molecular Biology Reports, 1999, 26: 277-284.
Thomas M, Langley B, Berry C, Sharma M, Kirk S, Bass J, Kambadur R. Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation[J]. Biochemistry and Molecular Biology, 2000, 275: 40235-40243.
Tomas F N, Munro H N, Young V R. Effect of glucocorticoid administration on the rate of muscle protein breakdown in vivo in rats, as measured by urinary excretion of N-methylhistidine[J]. Biochemical Journal, 1979, 178: 139-146.
Tomas F M, Pym R A, Johnson I L. Muscle protein turnover in chickens selected for increased growth rate, food consumption or efficiency of food utilization: effects of genotype and relationship to plasma IGF-I and growth hormone[J]. British Poultry Science, 1991, 32: 363-376.
Vandenburgh H H, Karlisch P, Shansky J, Feldstein R. Insulin and IGF-I induce pronounced hypertrophy of skeletal myofibers in tissue culture[J]. Americian Journal of Physiology, 1991, 260: C475-C484.
Whittemore La, Song K N, Li X P, Aghajanian J, Davies M, Girgenrath S, Hill J J, Kelley P, Knight A, Maylor R, O’Hara D, Quazi A, Ryerson S, Tan X Y, Tomkison K N, Veldman G M, Windom A, Wright J F, Wudyka S, Zhao L, Wolfman N M. Inhibition of myostatin in adult mice increases skeletal muscle mass and strength[J]. Biochemical and Biophysical Research Communications, 2003, 300: 965-971.
Wang L, Luo G. J, Wang J J, Hasselgren P O. Dexamethasone stimulates proteasome- and calcium-dependent proteolysis in cultured L6 myotubes[J]. Shock, 1998, 10: 298-306.
Wing S S, Goldberg A L. Glucocorticoids activate the ATP-ubiquitin-dependent proteolyticsystem in skeletal muscle during fasting[J]. American Journal of Physiology, 1993, 264: 668-676.
Wozney J M. The bone morphogenetic protein family: multifunctional cellular regulators in the embryo and adult[J]. European Journal of Oral Sciences, 1998, 106: 160-166.
Wullschleger S, Loewith R, Hall M N. TOR signaling in growth and metabolism[J]. Cell, 2006, 124: 471-484.
Yakar S, Liu J L, Stannard B, Butler A, Accili D, Sauer B, Leroith D. Normal growth and development in the absence of hepatic insulin-like growth factor I[J]. Proceedings of National Acadamy Sciences of USA, 1999, 96: 7324-7329.
Yan Q. Membrane transporters: methods and protocols[M]. Humana Press, Totowa, New Jersey. 2003.
Yuan L, Lin H, Jiang K J, Jiao H C, Song Z G.. Corticosterone administration and high-energy feed results in enhanced fat accumulation and insulin resistance in broiler chickens[J]. British Poultry Science, 2008, 49: 487-495.
Zhang H, Stallock J P, Ng J C, Reinhard C, Neufeld T P. Regulation of cellular growth by the Drosophila target of rapamycin dTOR[J]. Genes Development, 2000, 14: 2712-2724.
Zhu J, Hadhazy M, Wehling M, Tidball G, McNally E M. Dominant negative myostatin produces hypertrophy without hyperplasia in muscle[J]. FEBS Letters, 2000, 474: 71-75.
郭旭明,陈家伦.糖皮质激素受体拮抗剂-RU486的作用机制及临床研究[J].《国外医学》内分泌学分册,1993, 13(2): 64-67.
黄祯祥,洪涛,刘崇柏.医学病毒学基础及实验技术[M].科学出版社,1990:149-162.
刘丑生,赵兴波,李宁,赵有璋.动物肌肉生长发育调控的功能基因研究进展[J].中国畜牧杂志,2003,39(5):48-49.
刘立斌,周红雨.成肌细胞的临床应用现状及前景[J].中国修复重建外科杂志,2007,21(7): 767-770.
刘欣春,朱悦.胰岛素样生长因子-1对骨骼肌源性干细胞的促增殖效应[J].解剖学报,2008,39(1): 79-82.
龙定彪,张克英,陈代文,李建文,余冰.肌肉生长抑制素的研究进展[J].动物营养学报,2007,19: 498-502.
王兵,刘贻运,郑介柏,袁士翔.骨延长术中的骨钙素和胰岛素样因子-I的含量变化[J].中国矫形外科杂志,2002,9(3): 267-269.
王明若,王兴龙,韩文瑜.现代动物免疫学[M].吉林科技出版社,1996: 400-405.
王志钢,吴应积,旭日干. mTOR信号通路与细胞生长调控[J].生物物理学报,2007,23(5): 333-342.
魏宗友,徐柏林,郝志敏,王曙.氨基酸转运载体的研究进展[J].中国饲料,2010,13: 19-25.
薛慧良.胰岛素样生长因子系统的研究进展[J].生物学教学,2007,32(11):4-6.
张鹏,陈世益.成肌细胞在肌肉骨骼系统疾病基因治疗中的应用研究进展[J].中国运动医学杂志, 2003, 22 (5) : 483-486, 489.
朱伦,陈增良. mTOR的结构与功能[J].国际病理科学与临床杂志,2006,26: 31-34.
Anker S D, Clark A L, Kemp M, Salsbury C, Teixeira M M, Hellewell P G, Coats A J. Tumor necrosis factor and steroid metabolism in chronic heart failure: possible relation to muscle wasting[J]. Journal of the American College of Cardiology, 1997, 30: 997-1001.
Anthony G, Bernadette C, Michel J D. Nutrient supply enhances both IGF-I and MSTN mRNA levels in chicken skeletal muscle[J]. Domestic Animal Endocrinology, 2004, 26: 143-154.
Armstrong D G, Hogg C O. Type-I insulin-like growth factor receptor gene expression in the chick. Developmental changes and the effect of selection for increased growth on the amount of receptor mRNA[J]. Journal of Endocrinology, 1994, 12: 3-12.
Artaza J N, Bhasin S, Mallidis C, Taylo R W, Ma K, Gonzalez-Cadavid N F. Endogenous expression and localization of myostatin and its relation to myosin heavy chain distribution in C2C12 skeletal muscle cells[J]. Cellular Physiology, 2002, 190: 170-179.
Auclair D, Garrel D R, Chaouki Z A, Ferland L H. Activation of the ubiquitin pathway in rat skeletal muscle by catabolic doses of glucocorticoids[J]. American Journal of Physiology Cell Physiol, 1997, 272: C1007-C1016.
Bailey P, Tamara H, Andrew B L, The origin of skeletal muscle stem cells in the embryo and the adult[J]. Current Opinion of Cell Biology, 2001, 13: 679-689.
Ballard F J, Francis G L. Effects of anabolic agents on protein breakdown in L6 myoblasts[J]. Biochemical Journal, 1983, 210: 243-249.
Ballard F J, Johnson R J, Owens P C, Francis G L, Upton F M, McMurtry J P, Wallace J C. Chicken insulin-like growth factor-I: Amino acid sequence, radioimmunoassay, and plasma levels between strains and during growth[J]. General Comparative Endocrinology, 1990, 79: 459-468.
Baldwin K M, Herrick R E, Ilyina-Kakueva E, Oganov V S. Effects of zero gravity on myofibril content and isomyosin distribution in rodent skeletal muscle[J]. The FASEB Journal, 1990, 4: 79-83.
Bartov I. Effects of dietary protein concentration and corticosterone injections on energy and nitrogen balances and fat deposition in broiler chicks[J]. British Poultry Science, 1985, 26: 311-324.
Bodine S C, Latres E, Baumhueter S, Lai V K, Nunez L, Clarke B A, Poueymirou W T, Panaro F J, Na E, Dharmarajan K, Pan Z Q, Valenzuela D M, Dechiara T M, Stitt T N, Yancopoulos G D, Glass D J. Identification of ubiquitin ligases required for skeletal muscle atrophy[J]. Science, 2001, 294: 1704-1708.
Bodine S. C, Stitt T N, Gonzalez M, Kline W O, Stover G L, Bauerlein R, Zlotchenko E, Scrimgrour A, Lawrence J C, Glass D J, Yancopoulos G D. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo[J]. Nature Cell Biology, 2001, 3: 1014-1019.
Boushy A R EL. Vitamin E affects viability, immune response of poultry[J]. Feedstuffs, 1988, 60(44): 20-26.
Bowes S B, Jackson N C, Papachristodoulou D, Umpleby A M, Sonksen P H. Effect of corticosterone on protein degradation in isolated rat soleus and extensor digitorum longus muscles[J]. Journal of Endocrinology, 1996, 148: 501-507.
Braun T, Rudnicki M A, Arnold H H, Jaenisch R. Targeted inactivation of the muscle regulatory gene Myf-5 results in abnormal rib development and perinatal death[J]. Cell, 1992, 71: 369-382.
Broer S, Adaptation of plasma membrane amino acid transport mechanisms to physiological demands[J]. European Journal of Physiology. 2002, 444, 457-466.
Butler A A, LeRoith D. Minireview: tissue-specific versus generalized gene targeting of the igf1 and igf1r genes and their roles in insulin-like growth factor physiology[J]. Endocrinology, 2001, 142:1685-1688.
Carlson C J, Booth F W, Gordon S E. Skeletal muscle myostatin mRNA expression is fiber-type specific and increases during hindlimb unloading[J]. American Journal of Physiology: Regulatory, Integrative and Comparative Physiology, 1999, 277: R601-R606.
Centner T, Yano J, Kimura E, McElhinny A S, Pelin K, Witt C C, Bang M L, Trombitas K, Granzier H, Gregorio C C, Sorimachi H, Labeit S. Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain[J]. Molecular Biology, 2001, 306: 717-726.
Clarke B A, Drujan D, willis M S, Murphy L O, Corpina R A, Stitt T N, Patterson C, Latres E, Glass D J. The E3 ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle[J]. Cell Metabolism, 2007, 6: 376-385.
Dardevet D, Sornet C, Taillandier D, Savary I, Attaix D, Grizard J. Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and oldrats. Lack of regulation of the ubiquitin-proteasome proteolytic pathway in aging[J]. Journal of Clinical Investigation, 1995, 96: 2113-2119.
Dehoux M, Van Beneden R, Pasko N, Lause P, Verniers J, Underwood L, Ketelslegers J M, Thissen J P. Role of the insulin-like growth factor I ecline in the induction of Atrogin-1/MAFbx during fasting and diabetes[J]. Endocrinology, 2004, 145: 4806-4812.
Desler M M, Jones S J, Smith C W, Woods T L. Effects of dexamethasone and anabolic agents on proliferation and protein synthesis and degradation in C2C12 myogenic cells[J]. Journal of Animal Science, 1996, 74: 1265-1273.
Deves R, Boyd C A, Transporters for cationic amino acids in animal cells: discovery, structure, and function[J]. Physiological Reviews, 1998, 78: 487-545.
Dodson M V, Allen R E, Hossner K L. Ovine somatomedin, multiplication-stimulating activity, and insulin promote skeletal muscle satellite cell proliferation in vitro[J]. Endocrinology, 1985, 117: 2357-2363.
McFarland D C, Velleman S G, Pesall J E, Liu C, The role of myostatin in chicken (Gallus domesticus) myogenic satellite cell proliferation and differentiation[J]. General and Comparative Endocrinology, 2007, 151: 351-357.
Duclos M J, Wilkie R S, Goddard C. Stimulation of DNA synthesis in chicken muscle satellite cells by insulin and insulin-like growth factors: Evidence for exclusive mediation by a type-I insulin-like growth factor receptor[J]. Journal of Endocrinology, 1991, 128: 35-42.
El-Habbak M M, Abou-El-Soud S B, Ebeid T A. Effect of induced stress by dexamethasone administration on performance, egg quality and some blood parameters of laying hens[J]. Egyptian Poultry Science, 2005, 25: 89-105.
Falconer J, Harvey S, Forbes J M, Scanes C G. Changes in somatomedin-like activity and growth hormone concentrations in the plasma of the domestic fowl (Callus domesticus) [J]. AJEBAK, 1981, 59: 529-639.
Fan J, Molina P E, Gelato M C, Lang C H. Differential tissue regulation of insulin-like growth factor-1 content and binding protein after endotoxin[J]. Endocrinology, 1994, 134(4): 1685-1692.
Fawcett D H, Bulfied G. Molecular cloning, sequence analysis and expression of putativechicken insulin-like growth factor-I cDNAs[J]. Journal of Molecular Endocrinology, 1990, 4: 201-211.
Florini J R, Ewton D Z, Coolican S A. Growth hormone and the insulin-like growth factor system in myogenesis[J]. Endocrine Reviews 1996, 17: 481-517.
Fournier M, Huang Z S, Li H, Da X, Cercek B, Lewis M I. Insulin-like growth factor-I prevents corticosteroid-induced diaphragm muscle atrophy in emphysematous hamsters[J]. American Journal of Physiology, Regulatory, Integrative and Comparative Physiology, 2003, 285: R34-R43.
Frost R A, Lang C H. Regulation of insulin-like growth factor-I in skeletal muscle and muscle cells[J]. Minerva Endocrinologica, 2003, 28: 53-73.
Furukawa-Hibi Y, Yoshida-Araki K, Ohta T, Ikeda K, Motoyama N. FOXO forkhead transcription factors induce G2-M checkpoint in response to oxidative stress[J]. Journal of Biological Chemistry, 2002, 277: 26729-26732.
Gayan-Ramirez G., Vanderhoydonc F, Verhoeven G., Decramer M. Acute treatment with corticosteroids decreases IGF-1 and IGF-2 expression in the rat diaphragm and gastrocnemius[J]. American Journal of Respiratory and Critical Care Medicine, 1999, 159: 283-289.
Glass D J. Skeletal muscle hypertrophy and atrophy signaling patyway[J]. Biochemistry and Cell Biology, 2005, 37: 1974-1984.
Gomes M D, Lecker S H, Jagoe R T, Navon A, Goldberg A L. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy[J]. National Academy of Sciences Proc, 2001, 98: 14440-14445.
Gomes-Marcondes M C, Tisdale M J. Induction of protein catabolism and the ubiquitin-proteasome pathway by mild oxidative stress[J]. Cancer Lett, 2002, 180: 69-74.
Gonzalez-Cadavid N F, Taylor W E, Yarasheski K. Organization of the human MSTN gene and expression in healthy men and HIV-infected men with muscle wasting[J]. American Journal of Physiology, Regulatory, Integrative and Comparative Physiology, 1998, 95(25): 14938-43.
Gould N R, Siegel H S. Serum lipoproteins in chickens after administration ofadrenocorticotropin or exposure to high temperature[J]. Poultry Science, 1985, 64: 567-574.
Grizard J, Dardevet D, Papet I, Mosoni L, Mirand P P. Nutrient regulation of skeletal muscle protein metabolism in animals, the involvement of hormines and substrates[J]. Nutrition Research Reviews, 1995, 8: 67-91.
Grobet L, Royo L J, Poncelet D, Pirottin D, Brouwers B, Riquet J, Schoeberlein A, Dunner S, Menissier F, Massabanda J, Fries R., Hanset R, Georges. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle[J]. Nature Genetics, 1997, 17: 71-74.
Hasselgren P O. Burns and metabolism[J]. Journal of the American College of Surgeons, 1999, 188: 98-103.
Hasty P, Bradley A, Morris J H, Edmondson D G, Venuti J M, Olson E N, Klein W H. Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene[J]. Nature, 1993, 364: 501-506.
Hershko A, Ciechanover A. The ubiquitin system[J]. Annual Review of Biochemistry, 1998, 67: 425-479.
Hogan B L. Bone morphogenetic proteins in development[J]. Current Opinion in Genetics and Development, 1996, 10: 1580-1594.
Hong D H, Forsberg N E. Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures[J]. Molecular Cell Endocrinology, 1995, 108: 199-209.
Hoshino S, Wakita M, Suzuki M, Yamamoto K. Changes in somatomedin-like factor and immunoassayable growth hormone during growth of normal and dwarf pullets and cockerels[J]. Poultry Science, 1982, 61: 777-784.
Humphrey B D, Stephensen C B, Calvert C C, Klasing K C. Glucose and cationic amino acid transporter expression in growing chickens (Gallus gallus domesticus) [J].Comparative Biochemistry and Physiology, 2004, A 138: 515-525.
Humphrey B D, Kirk C K. The acute phase response alters cationic amino acid transporter expression in growing chickens (Gallus gallus domesticus) [J], Comparative Biochemistry and Physiology, 2005, Part A 142: 485-494.
Humphrey B D, Stephensen C B, Calvert C C, Klasing K C. Lysine deficiency and feed restriction independently alter cationic amino acid transporter expression in chickens (Gallus gallus domesticus) [J]. Comparative Biochemistry and Physiology, 2006, Part A 143: 218-227.
Jackman R W, Kandarian S C. The molecular basis of skeletal muscle atrophy[J]. American Journal of Physiology, 2004, 287: C834-C843.
Jagoe R T, Goldberg A L. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy[J]? Current Opinion in Clinical Nutrition and Metabolism Care, 2001, 4: 183-190.
Jagoe R T, Lecker S H, Gomes M, Goldberg A L. Patterns of gene expression in atrophying skeletal muscles: Response to food deprivation[J]. The FASEB Journal, 2002, 16: 1697-1712.
Jeanplong F, Bass J J, Smith H K, Kirk S P, Kambadur R, Sharma M, Oldham J M. Prolonged underfeeding of sheep increases myostatin and myogenic regulatory factor Myf-5 in skeletal muscle while IGF-I and myogenin are repressed[J]. Journal of Endocrinology, 2003, 176: 425-437.
Ji S, Losinski R L, Cornelius S G., Frank G. R, Willis G. M, Gerrard D E, Depreux F F, Spurlock M E. Myostatin expression in porcine tissues: tissue specificity and developmental and postnatal regulation[J]. American Journal of Physiology, 1998, 275: R1265-R1273.
Kajimoto Y, Rotwein P. Structure and expression of a chicken insulin-like growth factor I precursor[J]. Molecular Endocrinology, 1989, 3: 1907-1913.
Kajimoto Y, Rotwein P. Structure of the chicken insulin-like growth factor I gene reveals conserved promoter elements[J]. Journal of Biological Chemistry, 1991, 266: 9724-9731.
Kallincos N C, Wallace J C, Francis G L, Ballard F J. Chemical and biological characterization of chicken insulin-like growth factor-II[J]. Journal of Endocrinology, 1990, 124: 89-97.
Kambadur R, Sharma M, Smith TPL, Bass J J. Mutations in myostatin (GDF-8) in double-muscled Belgian Blue and Piedmontese cattle[J]. Genome Research, 1997, 7:910-915.
Kanda F, Takatani K, Okuda S, Matsushita T, Chihara K, Preventive effects of insulin-like growth factor-I on steroid-induced muscle atrophy[J]. Muscle and Nerve, 1999, 22: 213-217.
Karim L, Coppieters W, Grobet L, Valentini A, Georges M. Convenient genotyping of six myostatin mutations causing double-muscling in cattle using a multiplex oligonucleotide ligation assay[J]. Animal Genetics, 2000, 31: 396-399.
Kayali A G, Goodman M N, Lin J, Young V R. Insulin- and thyroid hormone-independent adaptation of myofibrillar proteolysis to glucocorticoids[J]. American Journal of Physiology, 1990, 259: E699-E705.
Kayali A G, Young V R, Goodman M N. Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis[J]. American Journal of Physiology Endocrinology and Metabolism, 1987, 252: E621-E626.
Kenneth J L, Thomas D S. Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2-△△Ct Method[J]. METHODS, 2001, 25: 402-408.
Kettelhut I C, Wing S S, Goldberg A J. Endocrine regulation of protein breakdown in skeletal muscle[J]. Diabetes/Metabolism Reviews, 1988, 4: 751-772.
Kikuchi K, Buonomo F C, Kajimoto Y, Rotwein P. Expression of insulin-like growth factor-I during chicken development[J]. Endocrinology, 1991, 128: 1323-1328.
Kimball S R, Vary T C, Jefferson L S. Regulation of protein synthesis by insulin[J]. Annual Review of Physiology, 1994, 56: 321-348.
Kocamis H, McFarland D. C, Killefer J. Temporal expression of growth factor genes during myogenesis of satellite cells derived from the biceps femoris and pectoralis major muscles of the chicken[J]. Cell Physiology, 2001, 186: 146-152.
Kuhn E R, Darras V M, Gysemans C, Decuypere E, Berghman L R, Buyse J. The use of intermittent lighting in broiler raising. II. Effects on the somatotropic and thyroid axes and on plasma testosterone levels[J]. Poultry Science, 1996, 75: 595-600.
Kulik G, Klippel A, Weber M J. Anti-apoptotic signaling by the insulin like growth factor-I receptor, phosphatidylinositol 3-kinase, and Akt[J]. Molecular Cell Endocrinology, 1997, 17: 1595-1606.
Lalani R, Bhasin S, Byhower F, Tarnuzzer R, Grant M, Shen R, Asa S, Ezzat S, Gonzalez-Cadavid N F. Myostatin and insulin-like growth factor-I and-II expression in the muscle of rats exposed to the microgravity environment of the Neuro Lab space shuttle ?ight[J]. Journal of Endocrinology, 2000, 167: 417-428.
Lang C H, Silvis C, Nystrom G., Frost R A. Regulation of myostatin by glucocorticoids after thermal injury[J]. The FASEB Journal, 2001, 15: 1807-1809.
Latres E, Amini A R, Amini A A, Grifiths J, Martin F J, Wei Y, Lin H C, Yancopoulos G. D, Glass D J. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-Kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway[J]. Biological Chemistry, 2005, 280: 2737-2744.
Lazar M A. Steroid and thyroid hormone receptors[J]. Endocrinology and Metabolism Clinics of North America, 1991, 20(4): 681-695.
Lee S J, McPherron A C. Regulation of MSTN activity and muscle growth[J]. Proceedings of the National Academy of Sciences of the United States of America, 2001, 98: 9306-9311.
Li B G, Hasselgren P O, Fang C H, Warden G D. Insulin-like growth factor-I blocks dexamethasone-induced protein degradation in cultured myotubes by inhibiting multiple proteolytic pathways: ABA paper[J]. Journal of Burn Care and Rehabilitation, 2002, 25: 112-118.
Li Y P, Schwartz R J, Waddell I D, Holloway B R, Reid M B. Skeletal muscle myocytes undergo protein loss and reactive oxygenmediated NF-kB activation in response to tumor necrosis factorα[J]. The FASEB Journal, 1998, 12: 871-880.
Li Z F, Shelton G D, Engvall E. Elimination of myostatin does not combat muscular dystrophy in dy mice but increases postnatal lethality[J]. American Journal of Pathology, 2005, 166: 491-497.
Lin H, Decuypere E, Buyse J. Oxidative stress induced by corticosterone administration in broiler chickens (Gallus gallus domesticus): 1. chronic exposure[J]. Biochemistry and Molecular Biology, 2004, 139: 737-744.
Lin H, Sui S J, Jiao H C, Buyse J, Decuypere E. Impaired development of broiler chickens by stress mimicked by corticosterone exposure[J]. Comparative Biochemistry andMolecular Biology, 2006, 143: 400-405.
Lin H, Sui S J, Jiao H C, Jiang K J, Zhao J P, Dong H. Effects of diet and stress mimicked by corticosterone administration on early postmortem muscle metabolism of broiler chickens[J]. Poultry Science, 2007, 86: 545-554.
Liu W, Chen B, Deng D, Xu F, Cui L, Cao Y L. Repair of tendon defect with dermal fibroblast engineered tendon in a porcine model[J]. Tissue Engineering, 2006, 12(4): 775-788.
Long W, Wei L P, Barrett E J. Dexamethasone inhibits the stimulation of muscle protein synthesis and PHAS-I and p70S6-kinase phosphorylation[J]. American Journal of Physiology Endocrinology and Metabolism, 2000, 280: 570-575.
Ma K, Mallidis C, Artaza J, Taylor W, Gonzalez-Cadavid N, Bhasin S. Characterization of 5’-regulatory region of human myostatin gene: regulation by dexamethasone in vitro[J]. American Journal of Physiology Endocrinology and Metabolism, 2001, 281: E1128-E1136.
Ma K, Mallidis C, Bhasin S, Mahabadi V, Artaza J, Gonzalez-Cadavid N, Arias, Salehian B. Glucocorticoid-induced skeletal muscle atrophy is associated with upregulation of myostatin gene expression[J]. American Journal of Physiology Endocrinology and Metabolism, 2003, 285: E363-E371.
Malheiros R D, Moraes V M, Collin A, Decuypere E, Buyse J. Free diet selection by broilers as influenced by dietary macronutient ratio and corticosterone supplementation. 1. Diet selection, organ weight, and plasma metabolites[J]. Poultry Science, 2003, 82: 123-131.
Matsumura Y, Domeki M, Sugahara K, Kubo T, Roberts C T Jr, LeRoith D, Kato H. Nutritional regulation of insulin-like growth factor-I receptor mRNA levels in growing chickens[J]. Bioscience Biotech Biochem, 1996, 60: 979-982.
Matteri R L, Carroll J A, Dyer C J. Neuroendocrine responses to stress[J]. Biology of Animal Stress, 2000, 43-76.
McMurtry J P, Francis G L, Upton F Z, Rosselot G, Brocht D M. Developmental changes in chicken and turkey insulin-like growth factor-I (IGF-I) studied with a homologous radioimmunoassay for chicken IGF-I[J]. Journal of Endocrinology, 1994, 142: 225-234.
McPherron A C, Lawler A M, Lee S J. Regulation of skeletal muscle mass in mice by a newTGF-βsuperfamily member[J]. Nature, 1997, 387: 83-90.
McPherron A C, Lee S J. Double muscling in cattle due to mutations in the myostatin gene[J]. Proceedings of the National Academy of Science of the USA, 1997, 94: 12457-12461.
Mitch W E, Goldberg A L. Mechanisms of muscle wasting: The role of the ubiquitin-proteasome pathway[J]. New England Journal of Medicine, 1996, 335: 1897-1905.
Montagne J, Stewart M J, Stocker H, Hafen E, Kozma S C, Thomas G. Drosophila S6 kinase: a regulator of cell size[J]. Science, 1999, 285: 2126-2129.
Morishita D, Wakita M, Hoshino S. Effect of hypophysectomy on insulin-like growth factor (IGF)-I binding activity of serum in chickens[J]. Comparative Biochemistry and Physiology, 1993, 104 A: 261-265.
Munoz K A, Satarug S, Tischler M E. Time course of the response of myofibrillar and sarcoplasmic protein metabolism to unweighting of the soleus muscle[J]. Metabolism, 1993, 42: 1006-1012.
Musaro A, Rosenthal N. Attenuating muscle wasting: cell and gene therapy approaches[J]. Current Genomics, 2003, 4: 575-585.
Nabeshima Y, Hanaoka K, Hayasaka M, Esumi E, Li S, Nonaka I. Myogenin gene disruption results in perinatal lethality because of severe muscle defect[J]. Nature, 1993, 364: 532-535.
Okumura J, Kita K. Recent advance in the relationship between endocrine status and nutrition on chickens[J]. Asian-Australasian Journal of Animal Sciences, 1999, 12 (7): 135-141. Oldham S, Montagne J, Radimerski T, Thomas G, Hafen E. Genetic and biochemical
characterization of dTOR, the Drosophila homolog of the target of rapamycin. Genes Development, 2000, 14: 2689-2694.
Palacin M, Estevez R, Bertran J, Zorzano A. Molecular biology of mammalian plasma membrane amino acid transporters[J]. Physiological Reviews, 1998, 78: 969-1038.
Patel K, Amthor H. The function of myostatin and strategies of myostatin blockade-new hope for therapies aimed at promoting growth of skeletal muscle[J]. Neuromuscular Disorders, 2005, 1: 117-126.
Polak P, Hall M, N. mTOR and the control of whole body metabolism[J]. Current Opinion inCell Biology, 2009, 21: 209-218.
Puvadolpirod S. Model of physiological stress in Chickens.2. dosimetry of adrenocorticotropin[J]. Poultry Science, 2000, 79: 370-376.
Rios R, Carneiro I, Arce V M. Devesa J. Myostatin regulates cell survival during C2C12 myogenesis[J]. Biochemical and Biophysical Research Communications, 2001, 19: 561-566.
Rios R, Carneiro I, Arce V M, Devesa J. Myostatin is an inhibitor of myogenic differentiation[J]. American Journal of Physiology Cell Physiology, 2002, 282: 993-999.
Roeder R A, Thorpe S D, Byers F M, Schelling G T, Gunn J M. Influence of anabolic agents on protein synthesis and degradation in muscle cells grown in culture[J]. Growth, 1986, 50: 485-495.
Rommel C, Bodine S C, Clarke B A, Rossman R, Nunez L, Stitt T N, Yancopoulos G D, Glass D J. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI (3)K/Akt/mTOR and PI(3)K/Akt/ GSK3 pathways[J]. Nature Cell Biology, 2001, 3(11): 1009-1013.
Rosselot G, McMurtry J P, Vasilatos-Younken R, Czerwinski S. Effect of exogenous chicken growth hormone (cGH) administration on insulin-like growth factor-I (IGF-I) gene expression in domestic fowl[J]. Molecular and Cellular Endocrinology, 1995, 114: 157-166.
Roy R R, Gardiner P F, Simpson D R, Edgerton V R. Glucocorticoid-induced atrophy in different fiber types of selected rat jaw and hind-limb muscles[J]. Archives of Oral Biology, 1983, 28: 639-643.
Rudnicki M A, Braun T, Hinuma S, Jaenisch R. Inactivation of MyoD in mice leads to up-regulation of the myogenic HLH gene Myf-5 and results in apparently normal muscle development[J]. Cell, 1992, 71: 383-390.
Rudnicki M A, Schnegelsberg P N, Stead R H, Braun T, Arnold H H, Jaenisch R. MyoD or Myf-5 is required for the formation of skeletal muscle[J]. Cell, 1993, 75: 1351-1359.
Sacheck J M. Expression of muscle-specific ubiquitin-protein ligases (E3s) during muscle atrophy [J]. The FASEB Journal, 2003, 17: A9578.
Sacheck J M, Ohtsuka A, McLary C, Goldberg A L. IGF-1 stimulates muscle growth bysuppressing protein breakdown and expression of atrophy-related ubiquitin-ligases, atrogin-1 and MuRF1[J]. American Journal of Physiology Endocrinology and Metabolism, 2004, 287: 591-601.
Saier M H. Genome archeology leading to the characterization and classification of transport proteins[J]. Current Opinion Microbiology, 1999, 2: 555-561.
Samani A A, Brodt P. The receptor for the type 1 insulin-like growth factor and its ligands regulate multiple cellular functions that impact on metastasis[J]. Journal of Surgical Oncology Clinics of North America, 2001, 10 (2): 289-312.
Sandri M, Sandri C, Gilbert A, Skurk C, Calabria, E, Picard A, Walsh K, Schiaffino S, Lecker S H, Goldberg A L. Foxo transcription factors induce the atrophy-related ubiquitin ligase Atrogin-1 and cause skeletal muscle atrophy[J]. Cell, 2004, 117: 399-412.
Sarbassov D D, Ali S M, Sabatini D M. Growing roles for the mTOR pathway[J]. Current Opinion in Cell Biology, 2005, 17: 596-603.
Scanes C G, Duyka D R, Lauterio T J, Bowen S J, Huybrechts L M, Bacon W L, King D B. Effect of chicken growth hormone, triiodothyronine and hypophysectomy in growing domestic fowl[J]. Growth, 1986, 50: 12-31.
Schakman O, Gilson H de C V, Lause P, Verniers J, Havaux X, Ketelslegers J M, Thissen J P. Insulin-like growth factor-I gene transfer by electroporation prevents skeletal muscle atrophy in glucocorticoid treated rats[J]. Endocrinology, 2005, 146: 1789-1797.
Scheuermann G. N, Bilgili S F, Hess J B, Mulvaney D R. Brest muscle development in commercial broiler chickens[J]. Poultry Science, 2003, 82: 1648-1658.
Schuelke M , Kathryn R, Wagner M D, Leslie E, Stolz L E, Hubner C, Riebel T, Komen W, Braun T, Tobin J F, Lee S J. Myostatin mutation associated with gross muscle hypertrophy in a child[J]. The New England Journal Medicine, 2004, 350: 2682-2688.
Seene T. Turnover of skeletal muscle contractile proteins in glucocorticoid myopathy[J]. The Journal of Steroid Biochemistry and Molecular Biology, 1994, 50: 1-4.
Shah O J, Anthony J C, Kimball S R, Jefferson L S. Glucocorticoids oppose translational control by leucine in skeletal muscle[J]. American Journal of Physiology Endocrinology and Metabolism, 2000, 279: E1185–E1190.
Shoji S. Myofibrillar protein catabolism in rat steroid myopathy measured by 3-methylhistidine excretion in the urine[J]. Journal of Neurological Sciences, 1989, 93: 333-340.
Shogi S, Pennington R J. The effect of cortisone on protein breakdown and synthesis in rat skeletal muscle[J]. Molecular and Cellular Endocrinology, 1977, 6: 159-169.
Sjogren K, Liu J L, Blad K, Skrtic S, Vidal O, Wallenius V, Leroith D, Tornell J, Isalsson O P, Jansson J O, Ohlsson, C. Liver derived insulin-like growth factor I (IGF-I) is the principal source of IGF-I in blood but is not required for postnatal body growth in mice[J]. Proceedings of the National Acadamy of Science of USA, 1999, 96: 7088-7092.
Sloan J L, Mager S. Cloning and functional expression of a human Na (+) and Cl(-)-dependent neutral and cationic amino acid transporter B(0+)[J]. Journal of Biological Chemistry, 1999, 274: 23740-23745.
Smith I J, Aversa Z, Alamdari N, Petkova V, Hasselgren P O. Sepsis downregulates myostatin mRNA levels without altering myostatin protein levels in skeletal muscle[J]. Journal of Cell Biochemistry, 2010, 11: 1059-1073.
Southorn B G, Palmer R M, Garlick P J. Acute effects of corticosterone on tissue protein synthesis and insulin sensitivity in rats in vivo[J]. Biochemical Journal, 1990, 272: 187-191.
Spencer E M,Liu C C. In vivo actions of Insulin like growth factor-1 on bone formation and resorption in rats[J]. Bone, 1991, 12(4): 21-26.
Steele R. Influences of corticosteroids on protein and carbohydrate metabolism[J]. Handbook of Physiology, 1975, 6: 135-168.
Szabo G, Dallmann G, Muller G, Patthy L, Soller M, Varga L. A deletion in the myostatin gene causes the compact (Cmpt) hypermuscular mutation in mice[J]. Mammalian Genome, 1998, 9: 671-672.
Tanaka M, Hayashida Y, Sakaguchi K, Ohkubo T, Wakita M, Hoshino S, Nakashima K. Growth hormone-independent expression of insulin-like growth factor I messenger ribonucleic acid in extrahepatic tissues of the chicken[J]. Endocrinology, 1996, 137: 30-34.
Taylor W E, Bhasin S, Artaza J, Byhower F, Azam M, Willard D H Jr, Kull F C Jr,Gonzalez-Cadavid N. Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells[J]. American Journal of Physiology Endocrinology and Metabolism, 2001, 280: E221-E228.
te Pas M F, de Jong P R, Verburg F J. Glucocorticoid inhibition of C2C12 proliferation rate and differentiation capacity in relation to mRNA levels of the MRF gene family[J]. Molecular Biology Reports, 2000, 27: 87-98.
te Pas M F, de Jong P R, Verburg F J, Duin M., Henning R H. Gender related and dexamethasone induced differences in the mRNA levels of the MRF genes in rat anterior tibial skeletal muscle[J]. Molecular Biology Reports, 1999, 26: 277-284.
Thomas M, Langley B, Berry C, Sharma M, Kirk S, Bass J, Kambadur R. Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation[J]. Biochemistry and Molecular Biology, 2000, 275: 40235-40243.
Tomas F N, Munro H N, Young V R. Effect of glucocorticoid administration on the rate of muscle protein breakdown in vivo in rats, as measured by urinary excretion of N-methylhistidine[J]. Biochemical Journal, 1979, 178: 139-146.
Tomas F M, Pym R A, Johnson I L. Muscle protein turnover in chickens selected for increased growth rate, food consumption or efficiency of food utilization: effects of genotype and relationship to plasma IGF-I and growth hormone[J]. British Poultry Science, 1991, 32: 363-376.
Vandenburgh H H, Karlisch P, Shansky J, Feldstein R. Insulin and IGF-I induce pronounced hypertrophy of skeletal myofibers in tissue culture[J]. Americian Journal of Physiology, 1991, 260: C475-C484.
Whittemore La, Song K N, Li X P, Aghajanian J, Davies M, Girgenrath S, Hill J J, Kelley P, Knight A, Maylor R, O’Hara D, Quazi A, Ryerson S, Tan X Y, Tomkison K N, Veldman G M, Windom A, Wright J F, Wudyka S, Zhao L, Wolfman N M. Inhibition of myostatin in adult mice increases skeletal muscle mass and strength[J]. Biochemical and Biophysical Research Communications, 2003, 300: 965-971.
Wang L, Luo G. J, Wang J J, Hasselgren P O. Dexamethasone stimulates proteasome- and calcium-dependent proteolysis in cultured L6 myotubes[J]. Shock, 1998, 10: 298-306.
Wing S S, Goldberg A L. Glucocorticoids activate the ATP-ubiquitin-dependent proteolyticsystem in skeletal muscle during fasting[J]. American Journal of Physiology, 1993, 264: 668-676.
Wozney J M. The bone morphogenetic protein family: multifunctional cellular regulators in the embryo and adult[J]. European Journal of Oral Sciences, 1998, 106: 160-166.
Wullschleger S, Loewith R, Hall M N. TOR signaling in growth and metabolism[J]. Cell, 2006, 124: 471-484.
Yakar S, Liu J L, Stannard B, Butler A, Accili D, Sauer B, Leroith D. Normal growth and development in the absence of hepatic insulin-like growth factor I[J]. Proceedings of National Acadamy Sciences of USA, 1999, 96: 7324-7329.
Yan Q. Membrane transporters: methods and protocols[M]. Humana Press, Totowa, New Jersey. 2003.
Yuan L, Lin H, Jiang K J, Jiao H C, Song Z G.. Corticosterone administration and high-energy feed results in enhanced fat accumulation and insulin resistance in broiler chickens[J]. British Poultry Science, 2008, 49: 487-495.
Zhang H, Stallock J P, Ng J C, Reinhard C, Neufeld T P. Regulation of cellular growth by the Drosophila target of rapamycin dTOR[J]. Genes Development, 2000, 14: 2712-2724.
Zhu J, Hadhazy M, Wehling M, Tidball G, McNally E M. Dominant negative myostatin produces hypertrophy without hyperplasia in muscle[J]. FEBS Letters, 2000, 474: 71-75.