Antigenically dominant proteins within the human liver mitochondrial proteome identified by monoclonal antibodies

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• 作者：YanFang Ju (1)
  JinJu Yang (2)
  Rong Liu (2)
  XiaoLan Liu (2)
  XueMei Du (2)
  Li Liu (2)
  ZhiCheng Chen (2)
  Jun Chi (2)
  ShuEr Liu (2)
  Yuan Gao (2)
  JianEn Gao (2)
  ShunChang Jiao (1)
  FuChu He (2)
  QiHong Sun (2)
  
• 关键词：mitochondria ; monoclonal antibodies ; cDNA library screening ; antigenically dominant proteins ; liver
• 刊名：Science China Life Sciences
• 出版年：2011
• 出版时间：January 2011
• 年：2011
• 卷：54
• 期：1
• 页码：16-24
• 全文大小：875KB
• 参考文献：1. Darley-Usmar V M, Rickwood D, Wilson M T. Mitochondria: a Practical Approach. Oxford: IRL Press, 1987
  2. Cordwell S J, Wilkins M R, Cerpa-Poljak A, / et al. Cross-species identification of proteins separated by two-dimensional gel electrophoresis using matrix-assisted laser desorption ionisation/time-of-flight mass spectrometry and amino acid composition. Electrophoresis, 1995, 16: 438鈥?43 CrossRef
  3. Taylor S W, Fahy D, Zhang B, / et al. Characterization of the human heart mitochondrial proteome. Nat Biotechnol, 2003, 21: 281鈥?86 CrossRef
  4. Kusnezow W, Hoheisel J D. Antibody microarrays: promises and problems. Biotechniques, 2002, Suppl: 14鈥?3
  5. Lemasters J J, Qian T, Bradham C A, / et al. Mitochondrial dysfunction in the pathogenesis of necrotic and apoptotic cell death. J Bio energ Biomembr, 1999, 31: 305鈥?19 CrossRef
  6. Beal M F. Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci, 2000, 23: 298鈥?04 CrossRef
  7. Chinnery P F, Howell N, Andrews R M, / et al. Mitochondrial DNA analysis: polymorphisms and pathogenicity. J Med Genet, 1999, 36: 505鈥?10
  8. Parrella P, Xiao Y, Fliss M, / et al. Detection of mitochondrial DNA mutations in primary breast cancer and fine-needle aspirates. Cancer Res, 2001, 61: 7623鈥?626
  9. Hibi K, Nakayama H, Yamazaki T, / et al. Mitochondrial DNA alteration in esophageal cancer. Int J Cancer, 2001, 92: 319鈥?21 CrossRef
  10. Simonnet H, Alazard N, Pfeiffer K, / et al. Low mitochondrial respiratory chain content correlates with tumor aggressiveness in renal cell carcinoma. Carcinogenesis, 2002, 23: 759鈥?68 CrossRef
  11. Copeland W C, Wachsman J T, Johnson F M, / et al. Mitochondrial DNA alterations in cancer. Cancer Invest, 2002, 20: 557鈥?69 CrossRef
  12. Modica-Napolitano J S, Singh K K. Mitochondrial dysfunction in cancer. Mitochondron, 2004, 4: 755鈥?62 CrossRef
  13. Leonard J V, Schapira A H. Mitochondrial respiratory chain disorders II: eurodegenerative disorders and nuclear gene defects. Lancet, 2000, 355: 389鈥?94 CrossRef
  14. Leonard J V, Schapira A H. Mitochondrial respiratory chain disorders I: mitochondrial DNA defects. Lancet, 2000, 355: 299鈥?04 CrossRef
  15. DiMauro S, Bonilla E, Davidson M, / et al. Mitochondria in neuromuscular disorders. Biochim Biophys Acta, 1998, 1366: 199鈥?10 CrossRef
  16. Zeviani M, Spinazzola A, Carelli V. Nuclear genes in mitochondrial disorders. Curr Opin Genet Dev, 2003, 13: 262鈥?70 CrossRef
  17. Mizuno Y, Ohta S, Tanaka M, / et al. Deficiencies in Complex I subunits of the respiratory chain in Parkinson鈥檚 disease. Biochem Biophys Res Commun, 1989, 163: 1450鈥?455 CrossRef
  18. Schapira A H, Cooper J M, Dexter D, / et al. Mitochondrial complex I deficiency in Parkinson鈥檚 disease. J Neurochem 1990, 54: 823鈥?27 CrossRef
  19. Betarbet R, Sherer T B, MacKenzie G, / et al. Chronic systemic pesticide exposure reproduces features of Parkinson鈥檚 disease. Nat Neurosci, 2000, 3: 1301鈥?306 CrossRef
  20. Kim S H, Vlkolinsky R, Cairns N, / et al. The reduction of NADH: Ubiquinone oxidoreductase 24- and 75-kD subunits in brains of patients with Down syndrome and Alzheimer鈥檚 disease. Life Sci, 2001, 68: 2741鈥?750 CrossRef
  21. Arenas J, Campos Y, Ribacoba R, / et al. Complex I defect in muscle from patients with Huntington鈥檚 disease. Ann Neurol, 1998, 43: 397鈥?00 CrossRef
  22. Vielhaber S, Kunz D, Winkler K, / et al. Mitochondrial DNA abnormalities in skeletal muscle of patients with sporadic amyotrophic lateral sclerosis. Brain, 2000, 123: 1339鈥?348 CrossRef
  23. Vielhaber S, Schroder R, Winkler K, / et al. Defective mitochondrial oxidative phosphorylation in myopathies with tubular aggregates originating from sarcoplasmic reticulum. J Neuropathol Exp Neurol, 2001, 60: 1032鈥?040
  24. Dror N, Klein E, Karry R, / et al. State-dependent alterations in mitochondrial complex I activity in platelets: A potential peripheral marker for schizophrenia. Mol Psychiatry, 2002, 7: 995鈥?001 CrossRef
  25. Lenaz G, D鈥橝urelio M, Merlo Pich M, / et al. Mitochondrial bioenergetics in aging. Biochim Biophys Acta, 2000, 1459: 397鈥?04 CrossRef
  26. Ling Y H, Lin R, Perez-Soler R. Erlotinib induces mitochondrial-mediated apoptosis in human H3255 non-small-cell lung cancer cells with epidermal growth factor receptorL858R mutation through mitochondrial oxidative phosphorylation-dependent activation of BAX and BAK. Mol Pharmacol, 2008, 74: 793鈥?06 CrossRef
  27. Murray J, Zhang B, Taylor S W, / et al. The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Bio Chem, 2003, 278: 13619鈥?3622 CrossRef
  28. Sercarz E E, Lehmann P V, Ametani A, / et al. Dominance and crypticity of T cell antigenic determinants. Annu Rev Immunol, 1993, 11: 729鈥?66 CrossRef
  29. Wienhold W, Malcherek G, Jung C, / et al. An example of immunodominance: engagement of synonymous TCR by invariant CDR3尾. Int Immunol, 2000, 12: 747鈥?56 CrossRef
  30. Gao J, Gao Y, Ju Y, / et al. Proteomics-based generation and characterization of monoclonal antibodies against human liver mitochondrial proteins. Proteomics, 2006, 6: 427鈥?37 CrossRef
  31. Mootha V K, Bunkenborg J, Olsen J V, / et al. Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell, 2003, 115: 629鈥?40 CrossRef
  32. Lusty C J. Carbamoylphosphate synthetase I of rat liver mitochondria: Purification, properties, and polypeptide molecular weight. Eur J Biochem, 1978, 85: 373鈥?83 CrossRef
  33. Raymond Y, Shore G C. Biogenesis of the mitochondrial enzyme, carbamyl phosphate synthetase: Appearance during fetal development of rat liver and rapid repression in freshly dispersed hepatocytes. Biochim Biophys Acta, 1981, 656: 111鈥?19
  34. Saarelainen S, Zeiler T, Rautiainen J, / et al. Lipocalin allergen Bos d 2 is a weak immunogen. Int Immunol, 2002, 14: 401鈥?09 CrossRef
  35. Nagata N, Matsuda I, Qyanagi K. Estimated frequency of urea cycle enzymopathies in Japan. Am J Med Genet, 1991, 39: 228鈥?29 CrossRef
  36. Cardona D M, Zhang X, Liu C. Loss of carbamoyl phosphate synthetase I in small-intestinal adenocarcinoma. Am J Clin Pathol, 2009, 132: 877鈥?82 CrossRef
  37. Head R A, Brown R M, Zolkipli Z, / et al. Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: Dihydrolipoamide acetyltransferase (E2) deficiency. Ann Neurol, 2005, 58: 234鈥?41 CrossRef
  38. Haselbeck R J, Hoffmann I, Duester G. Distinct functions for Aldh1 and Raldh2 in the control of ligand production for embryonic retinoid signaling pathways. Dev Genet, 1999, 25: 353鈥?64 CrossRef
  39. Molotkov A, Duester G. Genetic evidence that retinaldehyde dehydrogenase Raldh1 (Aldh1a1) functions downstream of alcohol dehydrogenase Adh1 in metabolism of retinol to retinoic acid. J Biol Chem, 2003, 278: 36085鈥?6090 CrossRef
  40. Moreb J S, Baker H V, Chang L J, / et al. ALDH isozymes downregulation affects cell growth, cell motility and gene expression in lung cancer cells. Mol Cancer, 2008, 7: 87 CrossRef
  41. Levi B P, Yilmaz O H, Duester G, / et al. Aldehyde dehydrogenase 1a1 is dispensable for stem cell function in the mouse hematopoietic and nervous systems. Blood, 2009, 113: 1670鈥?680 CrossRef
  42. Moreb J S, Mohuczy D, Ostmark B, / et al. RNAi-mediated knockdown of aldehyde dehydrogenase class-1A1 and class-3A1 is specific and reveals that each contributes equally to the resistance against 4-hydroperoxycyclophosphamide. Cancer Chemother Pharmaco, 2007, 59: 127鈥?36 CrossRef
  43. Ekhart C, Rodenhuis S, Smits P H, / et al. Relations between polymorphisms in drug-metabolising enzymes and toxicity of chemotherapy with cyclophosphamide, thiotepa and carboplatin. Pharmacogenet Genom, 2008, 18: 1009鈥?015 CrossRef
  44. Jackson S, Kler R S, Bartlett K, / et al. Combined enzyme defect of mitochondrial fatty acid oxidation. J Clin Invest, 1992, 90: 1219鈥?225 CrossRef
  45. Cao W, Liu N, Tang S, / et al. Acetyl-Coenzyme A acyltransferase 2 attenuates the apoptotic effects of BNIP3 in two human cell lines. Biochim Biophys Acta, 2008, 1780: 873鈥?80
  46. Vallat L, Magdel茅nat H, Merle-B茅ral H, / et al. The resistance of B-CLL cells to DNA damage-induced apoptosis defined by DNA microarrays. Blood, 2003, 101: 4598鈥?606 CrossRef
  47. Stegk J P, Ebert B, Martin H J, / et al. Expression profiles of human 11beta-hydroxysteroid dehydrogenases type 1 and type 2 in inflammatory bowel diseases. Mol Cell Endocrinol, 2009, 301: 104鈥?08 CrossRef
  48. Hale C, Wang M. Development of 11beta-HSD1 inhibitors for the treatment of type 2 diabetes. Mini Rev Med Chem, 2008, 8: 702鈥?10 CrossRef
  49. Hwang J Y, Lee S H, Kim G S, / et al. HSD11B1 polymorphisms predicted bone mineral density and fracture risk in postmenopausal women without a clinically apparent hypercortisolemia. Bone, 2009, 45: 1098鈥?103 CrossRef
  50. Tashjian R Z, Lin C, Aswad B, / et al. 11beta-hydroxysteroid dehydrogenase type 1 expression in periprosthetic osteolysis. Orthopedics, 2008, 31: 545 CrossRef
  51. Ahmed A, Saksena S, Sherlock M, / et al. Induction of hepatic 11beta-hydroxysteroid dehydrogenase type 1 in patients with alcoholic liver disease. Clin Endocrinol (Oxf), 2008, 68: 898鈥?03 CrossRef
  
• 作者单位：YanFang Ju (1)
  JinJu Yang (2)
  Rong Liu (2)
  XiaoLan Liu (2)
  XueMei Du (2)
  Li Liu (2)
  ZhiCheng Chen (2)
  Jun Chi (2)
  ShuEr Liu (2)
  Yuan Gao (2)
  JianEn Gao (2)
  ShunChang Jiao (1)
  FuChu He (2)
  QiHong Sun (2)
  
  1. Department of Oncology, General Hospital of PLA, Beijing, 100853, China
  2. State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing, 102206, China
  

文摘

Analysis of the mitochondrial proteome would provide valuable insight into the function of this important organelle, which plays key roles in energy metabolism, apoptosis, free radical production, thermogenesis, and calcium signaling. It could also increase our understanding about the mechanisms that promote mitochondrial disease. To identify proteins that are antigenically dominant in human liver mitochondria, we generated >240 hybridoma cell lines from native mitochondrial proteins after cell fusion, screening, and cloning. Antibodies that recognized mitochondrial proteins were identified by screening human liver cDNA expression libraries. In this study, we identified 6 major antigens that were recognized by at least 2 different monoclonal antibodies (mAbs). The proteins that were antigenically dominant were: acetyl-Coenzyme A acyltransferase 2 (mitochondrial 3-oxoacyl-Coenzyme A thiolase), aldehyde dehydrogenase 1 family member A1, carbamoyl phosphate synthetase 1, dihydrolipoamide S-acetyltransferase (E2 component of pyruvate dehydrogenase complex), enoyl coenzyme A hydratase 1, and hydroxysteroid (11-beta) dehydrogenase 1. We also determined the subcellular localizations of these enzymes within the mitochondria using immunohistocytochemistry. We believe that these well-characterized antibodies will provide a valuable resource for the Human Liver Proteome Project (HLPP), and will make studies aimed at investigating liver mitochondrial function far easier to perform in future. Our results provide strong evidence that, (i) depletion of dominant proteins from liver mitochondrial samples is possible and, (ii) the approaches adopted in this study can be used to explore or validate protein-protein interactions in this important organelle.