Quantitative proteomics analysis by iTRAQ in human nuclear cataracts of different ages and normal lens nuclei

Proteomics - Clinical Applications

Volumn 9, Issue 7-8, 2015, Pages 776-786

  Zhou, Hai Yan ^a,b   Yan, Hong ^a   Wang, Li Li ^b   Yan, Wei Jia ^c   Shui, Ying Bo ^d   Beebe, David C ^d  

^a FOURTH MILITARY MEDICAL UNIVERSITY   (China)

^b Xi'an Central Hospital   (China)

^c XI'AN MEDICAL UNIVERSITY   (China)

^d WASHINGTON UNIVERSITY   (United States)

Author keywords

Alpha crystallin B chain; GSH synthetase; Human; ITRAQ Nuclear cataract

Indexed keywords

ALPHA CRYSTALLIN; BETAINE HOMOCYSTEINE METHYLTRANSFERASE; BETAINE HOMOCYSTEINE METHYLTRANSFERASE 1; FATTY ACID BINDING PROTEIN; GAMMA CRYSTALLIN; GAMMA CRYSTALLIN C; GLUTATHIONE SYNTHASE; PHAKININ; PHOSPHOGLYCERATE KINASE; PHOSPHOGLYCERATE KINASE 1; PROTEIN; PTERIN 4 ALPHA CARBINOLAMINE DEHYDRATASE; SPECTRIN; SPECTRIN BETA CHAIN; UNCLASSIFIED DRUG; CRYAB PROTEIN, HUMAN; EYE PROTEIN; PEPTIDE;

ADULT; AGE RELATED NUCLEAR CATARACT; AGED; ARTICLE; CONTROLLED STUDY; DOWN REGULATION; FEMALE; HUMAN; HUMAN TISSUE; ISOBARIC TAGS FOR RELATIVE AND ABSOLUTE QUANTITATION; LENS NUCLEUS; LIQUID CHROMATOGRAPHY; MALE; MASS SPECTROMETRY; OXIDATIVE STRESS; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DATABASE; PROTEIN EXPRESSION; PROTEOMICS; QUANTITATIVE ANALYSIS; SENILE CATARACT; UPREGULATION; AGING; AMINO ACID SEQUENCE; CATARACT; CHEMISTRY; ISOTOPE LABELING; METABOLISM; MIDDLE AGED; MOLECULAR GENETICS; PATHOLOGY; PROCEDURES; VERY ELDERLY; WESTERN BLOTTING;

AGED; AGED, 80 AND OVER; AGING; ALPHA-CRYSTALLIN B CHAIN; AMINO ACID SEQUENCE; BLOTTING, WESTERN; CATARACT; EYE PROTEINS; FEMALE; GLUTATHIONE SYNTHASE; HUMANS; ISOTOPE LABELING; LENS NUCLEUS, CRYSTALLINE; MALE; MASS SPECTROMETRY; MIDDLE AGED; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEOMICS;

EID: 84949107455     PISSN: 18628346     EISSN: 18628354     Source Type: Journal    
DOI: 10.1002/prca.201400061     Document Type: Article

References (43)

1. Resnikoff, S., Keys, T. U., Future trends in global blindness. Indian J. Ophthalmol 2012, 60, 387-395.
2. Ono, K., Hiratsuka, Y., Murakami, A., Global inequality in eye health: country-level analysis from the Global Burden of Disease Study. Am. J. Public Health 2010, 100, 1784-1788.
3. Brian, G., Taylor, H., Cataract blindness-challenges for the 21st century. Bull World Health Organ. 2001, 79, 249-256.
4. Harrington, V., Srivastava, O. P., Kirk, M., Proteomic analysis of water insoluble proteins from normal and cataractous human lenses. Mol. Vis. 2007, 13, 1680-1694.
5. Su, S., Liu, P., Zhang, H., Li, Z. et al., Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei. Invest. Ophthalmol. Vis. Sci. 2011, 13, 4182-4191.
6. Grey, A. C., Schey, K. L., Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry. Invest. Ophthalmol. Vis. Sci. 2009, 50, 4319-4329.
7. Zieske, L. R., A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies. J. Exp. Bot. 2006, 57, 1501-1508.
8. Wu, W. W., Wang, G., Baek, S. J., Shen, R. F., Comparative study of three Proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDITOF/TOF. J. Proteome Res. 2006, 5, 651-658.
9. Chylack, L. T Jr., Leske, M. C., McCarthy, D., Khu, P. et al., Lens opacities classification system II (LOCS II). Arch. Ophthalmol. 1989, 107, 991-997.
10. Srivastava, O. P., Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Exp. Eye Res. 1988, 47, 525-543.
11. Zhang, X., Yin, X., Yu, H., Liu, X. et al., Quantitative proteomic analysis of serum proteins in patients with Parkinson's disease using an isobaric tag for relative and absolute quantification labeling, two-dimensional liquid chromatography, and tandem mass spectrometry. Analyst 2012, 137, 490-495.
12. Chen, G., Zhang, Y., Jin, X., Zhang, L. et al., Urinary proteomics analysis for renal injury in hypertensive disorders of pregnancy with iTRAQ labeling and LC-MS/MS. Proteomics Clin. Appl. 2011, 5, 300-310.
13. Wang, W. S., Liu, X. H., Liu, L. X., Jin, D. Y. et al., Identification of proteins implicated in the development of pancreatic cancer-associated diabetes mellitus by iTRAQ-based quantitative proteomics. J. Proteomics 2013, 84, 52-60.
14. Benedek, G. B., Theory of transparency of the eye. Appl. Opt. 1971, 10, 459-473.
15. Graw, J., The crystallins: genes, proteins, and diseases. Biol. Chem. 1997, 378, 1331-1348.
16. Sakthivel, M., Elanchezhian, R., Thomas, P. A., Geraldine, P., Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats. Mol. Vis. 2010, 16, 445-453.
17. Groenen, P. J., Merck, K. B., de Jong, W. W., Bloemendal, H., Structure and modifications of the junior chaperone α-crystallin. Eur. J. Biochem. 1994, 225, 1-19.
18. Han, J., Schey, K., MALDI tissue imaging of ocular lens α-crystallin. Invest. Ophthalmol. Vis. Sci. 2006, 47, 2990-2996.
19. Spector, A., The search of a solution to senile cataract. Invest. Ophthalmol. Vis. Sci. 1984, 25, 130-146.
20. Gan, C. S., Chong, P. K., Pham, T. K., Wright, P. C., Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ). J. Proteome Res. 2007, 6, 821-827.
21. Ye, H., Sun, L., Huang, X., Zhang, P. et al., A proteomic approach for plasma biomarker discovery with 8-plex iTRAQ labeling and SCX-LC-MS/MS. Mol. Cell Biochem. 2010, 343, 91-99.
22. Caubet, C., Lacroix, C., Decramer, S., Drube, J. et al., Advances in urinary proteome analysis and biomarker discovery in pediatric renal disease. Pediatr. Nephrol. 2010, 25, 27-35.
23. Andley, U. P., Effects of alpha-crystallin on lens cell function and cataract pathology. Curr. Mol. Med. 2009, 9, 887-892.
24. Zhou, P., Luo, Y., Liu, X., Fan, L. et al., Down-regulation and CpG island hypermethylation of CRYAA in age-related nuclear cataract. FASEB J. 2012, 26, 4897-4902.
25. Liao, J., Su, X., Chen, P., Wang, X. et al., Meta-analysis of genome-wide association studies in multiethnic Asians identifies two loci for age-related nuclear cataract. Hum. Mol. Genet. 2014, 23, 6119-6128.
26. Iwaki, T., Iwaki, A., Goldman, J. E., Alpha B-crystallin in oxidative muscle fibers and its accumulation in ragged-red fibers: a comparative immunohistochemical and histochemical study in human skeletal muscle. Acta Neuropathol. 1993, 85, 475-480.
27. Sun, T. X., Das, B. K., Conformational and functional differences between recombinant human lens alphaA-and alphaB-crystallin. J. Biol. Chem. 1997, 272, 6220-6225.
28. Srivastava, K., Chaves, J. M., Srivastava, O. P., Kirk, M., Multi-crystallin complexes exist in the water-soluble high molecular weight protein fractions of aging normal and cataractous human lenses. Exp. Eye Res. 2008, 87, 356-366.
29. Srivastava, O. P., Srivastava, K., Existence of deamidated alphaB-crystallin fragments in normal and cataractous human lenses. Mol. Vis. 2003, 9, 110-118.
30. Lou, M. F., Redox regulation in the lens. Prog. Retin. Eye Res. 2003, 44, 3262-3271.
31. Lou, M. F., Xu, G. T., Cui, X. L., Further studies on the dynamic changes of glutathione and protein-thiol mixed disulfides in H2O2 induced cataract in rat lenses: distributions and effect of aging. Curr. Eye Res. 1995, 14, 951-958.
32. Obrosova, I. G., Stevens, M. J., Effect of dietary taurine supplementation on GSH and NAD(P)-redox status, lipid peroxidation, and energy metabolism in diabetic precataractous lens. Invest. Ophthalmol. Vis. Sci. 1999, 40, 680-688.
33. Hains, P. G., Truscott, R. J., Proteomic analysis of the oxidation of cysteine residues in human age-related nuclear cataract lenses. Biochim Biophys Acta. 2008, 1784, 1959-1964.
34. Fan, X., Liu, X., Hao, S., Wang, B. et al., The LEGSKO mouse: a mouse model of age-related nuclear cataract based on genetic suppression of lensglutathione synthesis. PLoS One 2012, 7, e50832.
35. Rathbun, W. B., Holleschau, A. M., The effects of age on glutathione synthesis enzymes in lenses of Old World simians and prosimians. Curr. Eye Res. 1992, 11, 601-607.
36. Xie, P. Y., Kanai, A., Nakajima, A., Kitahara, S. et al., Glutathione and glutathione-related enzymes in human cataractous lenses. Ophthalmic Res. 1991, 23, 133-140.
37. Harocopos, G. J., Shui, Y. B., McKinnon, M., Holekamp, N. M. et al., Importance of vitreous Liquefaction in age-related cataract. Invest. Ophthalmol. Vis. Sci. 2004, 45, 77-85.
38. Beebe, D. C., Holekamp, N. M., Siegfried, C., Shui, Y. B., Vitreoretinal influences on lens function and cataract. Philos. Trans. R Soc. Lond B Biol. Sci. 2011, 27, 1293-1300.
39. Rao, P. V., Garrow, T. A., John, F., Garland, D. et al., Betaine-homocysteine methyltransferase is a developmentally regulated enzyme crystallin in rhesus monkeylens. J. Biol. Chem. 1998, 13, 30669-30674.
40. Kinoshita, J. H., Mechanisms initiating cataract formation. Proctor Lecture. Invest. Ophthalmol. 1974, 13, 713-724.
41. Pajares, M. A., Pérez-Sala, D., Betaine homocysteine S-methyltransferase: just a regulator of homocysteine metabolism? Cell. Mol. Life Sci. 2006, 63, 2792-2803.
42. Sandu, C., Nick, P., Hess, D., Schiltz, E. et al., Association of betaine-homocysteine S-methyltransferase with microtubules. Biol. Chem. 2000, 381, 619-622.
43. Ichikawa, A., Ohashi, Y., Terada, S., Natsuka, S. et al., In vitro modification of betaine-homocysteine S-methyltransferase by tissue-type transglutaminase. Int. J. Biochem. Cell. Biol. 2004, 36, 1981-1992.