食源性蛋白酶抑制剂结构与功能
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摘要
食源性蛋白酶抑制剂(foodborne protease inhibitors,FPI)来源广泛,且种类繁多,研究分析这些FPI的特异性结构与其生理功能之间的关系具有十分重要的意义。该文首先综述蛋白酶抑制剂的来源、分类和作用机理;另外详细说明3种FPI(包括:Bowman-Birk型、Kunitz型以及Kazal型蛋白酶抑制剂等)命名的由来和其在结构上的区别,这些种类的FPI不仅可调节控制生物机体的蛋白质水解过程,同时还具有诸如调节机体防御、抗肿瘤、抗炎、抗凝血、预防肥胖等生理作用。
Foodborne protease inhibitors(FPI)can be found from a variety of resources,and can be divided into many groups;furthermore,it is of great significance to understand the relationship between their specific structures and physiological functions. The resource,the classification and the functional mechanism of FPIs were summarized;in addition,three kinds of FPIs,including Bowman-Birk type,Kunitz type and Kazal type FPI,were explicated in detail,which involved the explanation of their resources and structural difference;these mentioned FPIs of three kinds not only regulated the proteolysis process of the biological organism,also had physiological functions such as body defensive regulation,anti-tumor function,anti-inflammation function,anti-coagulation function,and prevention of obesity.
Foodborne protease inhibitors(FPI)can be found from a variety of resources,and can be divided into many groups;furthermore,it is of great significance to understand the relationship between their specific structures and physiological functions. The resource,the classification and the functional mechanism of FPIs were summarized;in addition,three kinds of FPIs,including Bowman-Birk type,Kunitz type and Kazal type FPI,were explicated in detail,which involved the explanation of their resources and structural difference;these mentioned FPIs of three kinds not only regulated the proteolysis process of the biological organism,also had physiological functions such as body defensive regulation,anti-tumor function,anti-inflammation function,anti-coagulation function,and prevention of obesity.
引文
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[41]Meester P D,Brick P,Lloyd L F,et al.Structure of the Kunitz-Type Soybean Trypsin Inhibitor(STI):Implication for the Interactions Between Members of the STI Family and Tissue-Plasminogen Activator[J].Acta Crystallographica,2010,54(4):589-597
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[43]Qian Y Q,Li Y,Yang F,et al.Two Kazal-type protease inhibitors from Macrobrachium nipponense and Eriocheir sinensis:comparative analysis of structure and activities[J].Fish&Shellfish Immunology,2012,32(3):446-58
[44]Rimphanitchayakit V,Tassanakajon A.Structure and function of invertebrate Kazal-type serine proteinase inhibitors[J].Developmental&Comparative Immunology,2010,34(4):377-386
[45]Wang B,Zhao J,Song L,et al.Molecular cloning and expression of a novel Kazal-type serine proteinase inhibitor gene from Zhikong scallop Chlamys farreri,and the inhibitory activity of its recombinant domain[J].Fish&shellfish immunology,2008,24(5):629-637
[46]Lu W,Apostol I,Qasim MA,et al.Binding of amino acid sidechains to S-1 cavities of serine proteinases[J].Journal of Molecular Biology,1997,266(2):441-46
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[48]文方德,傅家瑞.植物种子的蛋白酶抑制剂及其生理功能[J].植物生理学报,1997,33(1):1-9
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[2]Swathi M,Lokya V,Swaroop V,et al.Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan,(cv.ICP 7118)[J].Plant Physiology&Biochemistry,2014,83:77-87
[3]Kaur A P,Sohal S K.Pea protease inhibitor inhibits protease activity and development of Bactrocera cucurbitae[J].Journal of Asia-Pacific Entomology,2016,19(4):1183-1189
[4]Oliva M L,Ferreira R S,Ferreira J G,et al.Structural and functional properties of kunitz proteinase inhibitors from leguminosae:a mini review[J].Current Protein&Peptide Science,2011,12(5):348-357
[5]Dias L P,Oliveira J T A,Rocha-Bezerra L C B,et al.A trypsin inhibitor purified from Cassia leiandra,seeds has insecticidal activity against Aedes aegypti[J].Process Biochemistry,2017,57:228-238
[6]Bezerra C D S,Oliveira C F R D,Machado O L T,et al.Exploiting the biological roles of the trypsin inhibitor from Inga vera,seeds:Amultifunctional Kunitz inhibitor[J].Process Biochemistry,2016,51(6):792-803
[7]Cruz A C B,Massena F S,Migliolo L,et al.Bioinsecticidal activity of a novel Kunitz trypsin inhibitor from Catanduva(Piptadenia moniliformis)seeds[J].Plant Physiology&Biochemistry Ppb,2013,70(1):61-68
[8]Pandey P K,Jamal F.Bio-potency of a 21 kDa Kunitz-type trypsin inhibitor from Tamarindus indica seeds on the developmental physiology of H.armigera[J].Pesticide Biochemistry&Physiology,2014,116:94-102
[9]Kim S H,Hara S,Hase S,et al.Comparative Study on Amino Acid Sequences of Kunitz-Type Soybean Trypsin Inhibitors,Tia,Tib,and Tic[J].Journal of Biochemistry,1985,98(2):435-448
[10]Srinivasan A,Giri A P,Harsulkar A M,et al.A Kunitz trypsin inhibitor from chickpea(Cicer arietinum L.)that exerts anti-metabolic effect on podborer(Helicoverpa armigera)larvae[J].Plant Molecular Biology,2005,57(3):359-374
[11]Macedo M L,de SáC M,Freire M D,et al.A Kunitz-type inhibitor of coleopteran proteases,isolated from Adenanthera pavonina L.seeds and its effect on Callosobruchus maculatus[J].Journal of A-gricultural&Food Chemistry,2004,52(9):2533-2540
[12]Liao H,Ren W,Kang Z,et al.A trypsin inhibitor from Cassia obtusifolia,seeds:isolation,characterization and activity against Pieris rapae[J].Biotechnology Letters,2007,29(4):653-658
[13]DraméK N,Passaquet C,Repellin A,et al.Cloning,characterization and differential expression of a Bowman-Birk inhibitor during progressive water deficit and subsequent recovery in peanut(Arachishypogaea)leaves[J].Journal of Plant Physiology,2013,170(2):225-229
[14]Xiang M,Zhang X,Deng Y,et al.Comparative transcriptome analysis provides insights of anti-insect molecular mechanism of Cassia obtusifolia trypsin inhibitor against Pieris rapae[J].Archives of Insect Biochemistry&Physiology,2018,97(1):1-21
[15]Batista I F C,Oliva M L V,Araujo M S,et al.Primary structure of a Kunitz-type trypsin inhibitor from Enterolobiumcontortisiliquum,seeds[J].Phytochemistry,1996,41(4):1017-1022
[16]Srikanth S,Chen Z.Plant Protease Inhibitors in Therapeutics-Focus on Cancer Therapy[J].Frontiers in Pharmacology,2016,7:1-19
[17]Laskowski M,Qasim M A.What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?[J].BiochimicaetBiophysicaActa(BBA)-Protein Structure and Molecular Enzymology,2000,1477(1/2):324-337
[18]Rustgi S,Boex-Fontvieille E,Reinbothe C,et al.The complex world of plant protease inhibitors:Insights into a Kunitz-type cysteine protease inhibitor of Arabidopsis thaliana[J].Communicative&Integrative Biology 2018,11:1-8
[19]Brauer A B E,Nievo M,McBride J D,et al.The structural basis of a conserved P2 threonine in canonical serine proteinase inhibitors[J].Journal of Biomolecular Structure and Dynamics,2003,20(5):645-655
[20]Birk Y.The Bowman-Birk inhibitor Trypsin-and chymotrypsin-inhibitor from soybeans[J].International Journal of Peptide&Protein Research,1985,25(2):113-131
[21]Chan Y S,Zhang Y,Ng T B.Brown Kidney Bean Bowman-Birk Trypsin Inhibitor is Heat and pH Stable and Exhibits Anti-proliferative Activity[J].Applied Biochemistry&Biotechnology,2013,169(4):1306-1314
[22]Koepke J,Ermler U,Warkentin E,et al.Crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3覽resolution.Structural basis of Janus-faced protease inhibitor specificity 1[J].Journal of Molecular Biology,2000,298(3):477-491
[23]Ware J H,Wan X S,Rubin H,et al.Soybean Bowman-Birk Protease Inhibitor Is a Highly Effective Inhibitor of Human Mast Cell Chymase[J].Archives of Biochemistry&Biophysics,1997,344(1):133-138
[24]Oliva M L,Silva M C,Sallai R C,et al.A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds.[J].Biochimie,2010,92(11):1667-1673
[25]Araújo C L,Bezerra I W,Oliveira A S,et al.In vivo bioinsecticidal activity toward Ceratitis capitata(fruit fly)and Callosobruchus maculatus(cowpea weevil)and in vitro bioinsecticidal activity toward different orders of insect pests of a trypsin inhibitor purified from tamarind tree(Tamarindus indica)seeds[J].J Agric Food Chem,2005,53(11):4381-4387
[26]Oliveira C F R D,Vasconcelos I M,Aparicio R,et al.Purification and biochemical properties of a Kunitz-type trypsin inhibitor from Entada acaciifolia(Benth.)seeds[J].Process Biochemistry,2012,47(6):929-935
[27]Ma Y,Zhao Q,Lu M Z,et al.Kunitz-type trypsin inhibitor gene family in Arabidopsis,and Populustrichocarpa,and its expression response to wounding and herbivore in Populusnigra[J].Tree Genetics&Genomes,2011,7(2):431-441
[28]Otlewski J,Jask觔3Lski M,Buczek O,et al.Structure-function relationship of serine protease-protein inhibitor interaction[J].Acta Biochimica Polonica,2001,48(2):419-428
[29]Laskowski M,Qasim M A.What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?[J].Biochimica Et Biophysica Acta,2000,1477(1/2):324-337
[30]Dattagupta J K,Podder A,Chakrabarti C,et al.Refined crystal structure(2.3魡)of a double-headed winged beanα-chymotrypsin inhibitor and location of its second reactive site[J].Proteins Structure Function&Bioinformatics,1999,35(3):321-331
[31]Kouzuma Y,Suetake M,Kimura M,et al.Isolation and primary structure of proteinase inhibitors from Erythrina variegata(LINN.)var.Orientalis seeds[J].Journal of the Agricultural Chemical Society of Japan,1992,56(11):1819-1824
[32]Macedo M L,Garcia V A,Md F,et al.Characterization of a Kunitz trypsin inhibitor with a single disulfide bridge from seeds of Inga laurina(SW.)Willd[J].Phytochemistry,2007,68(8):1104-1111
[33]Santos E A D,Oliveira A S D,Uch?aL M A,et al.Affinity Chromatography as a Key Tool to Purify Protein Protease Inhibitors from Plants[M].London:UNITED KINGDOM:IntechOpen,2012:211-244
[34]Wu H C,Lin J Y.The complete amino acid sequence of a Kunitz family trypsin inhibitor from seeds of Acacia confusa.[J].Journal of biochemistry,1993,113(2):258-263
[35]De O C,Santana L A,Carmona A K,et al.Structure of cruzipain/cruzain inhibitors isolated from Bauhinia bauhinioides seeds.[J].Biological Chemistry,2001,382(5):847-852
[36]Riffel A,Brandelli A,Bellato,et al.Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp.kr6[J].Journal of Biotechnology,2007,128(3):693-703
[37]Vashisth A,Nagarajan S.Effect on germination and early growth characteristics in sunflower(Helianthus annuus)seeds exposed to static magnetic field[J].Journal of Plant Physiology,2010,167(2):149-156
[38]Guerra Y,Valiente P A,Pons T,et al.Structures of a bi-functional Kunitz-type STI family inhibitor of serine and aspartic proteases:Could the aspartic protease inhibition have evolved from a canonical serine protease-binding loop?[J].Journal of Structural Biology,2016,195(2):259-271
[39]Vagadia B H,Vanga S K,Raghavan V.Inactivation methods of soybean trypsin inhibitor-A review[J].Trends in Food Science&Technology,2017,64(2):115-125
[40]Song H K,Suh S W.Kunitz-type soybean trypsin inhibitor revisited:refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator[J].Journal of Molecular Biology,1998,275(2):347-363
[41]Meester P D,Brick P,Lloyd L F,et al.Structure of the Kunitz-Type Soybean Trypsin Inhibitor(STI):Implication for the Interactions Between Members of the STI Family and Tissue-Plasminogen Activator[J].Acta Crystallographica,2010,54(4):589-597
[42]Kwon H,Yang H,Lee S,et al.Characterization of a Kazal-type serine protease inhibitor from black rockfish Sebastes schlegelii and its possible role in hepatic immune response[J].Fish&shellfish immunology,2018,74:485-490
[43]Qian Y Q,Li Y,Yang F,et al.Two Kazal-type protease inhibitors from Macrobrachium nipponense and Eriocheir sinensis:comparative analysis of structure and activities[J].Fish&Shellfish Immunology,2012,32(3):446-58
[44]Rimphanitchayakit V,Tassanakajon A.Structure and function of invertebrate Kazal-type serine proteinase inhibitors[J].Developmental&Comparative Immunology,2010,34(4):377-386
[45]Wang B,Zhao J,Song L,et al.Molecular cloning and expression of a novel Kazal-type serine proteinase inhibitor gene from Zhikong scallop Chlamys farreri,and the inhibitory activity of its recombinant domain[J].Fish&shellfish immunology,2008,24(5):629-637
[46]Lu W,Apostol I,Qasim MA,et al.Binding of amino acid sidechains to S-1 cavities of serine proteinases[J].Journal of Molecular Biology,1997,266(2):441-46
[47]Krowarsch D,Cierpicki T,Jelen F,et al.Canonical protein inhibitors of serine proteases[J].Cellular and molecular life sciences,2003,60(11):2427-2444
[48]文方德,傅家瑞.植物种子的蛋白酶抑制剂及其生理功能[J].植物生理学报,1997,33(1):1-9
[49]廖海,杜林方,周嘉裕.植物中蛋白类蛋白酶抑制剂的研究进展[J].天然产物研究与开发,2002,14(1):80-84
[50]Birk Y.Plant Protease Inhibitors:Significance in Nutrition,Plant Protection,Cancer Prevention and Genetic Engineering[M].Berlin:Springer Science&Business Media,2003:111-120
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