Multi-crystallin complexes exist in the water-soluble high molecular weight protein fractions of aging normal and cataractous human lenses

Experimental Eye Research

Volumn 87, Issue 4, 2008, Pages 356-366

  Srivastava, K ^a   Chaves, J M ^a   Srivastava, O P ^a   Kirk, M ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

aging; blue native polyacrylamide gel electrophoresis; cataract; crystallins; lens; post translational modifications

Indexed keywords

AGAROSE; ALDEHYDE DEHYDROGENASE; ALPHA CRYSTALLIN; BETA CRYSTALLIN; DODECYL SULFATE SODIUM; FILENSIN; GAMMA CRYSTALLIN; LENS PROTEIN; PHAKININ; TRYPSIN; UNCLASSIFIED DRUG; WATER SOLUBLE HIGH MOLECULAR WEIGHT PROTEIN;

ADULT; AGED; AGING; ARTICLE; BLUE-NATIVE POLYACRYLAMIDE GEL ELECTROPHORESIS; CATARACT; ELECTRON MICROSCOPY; ELECTROSPRAY MASS SPECTROMETRY; GEL PERMEATION CHROMATOGRAPHY; HUMAN; HUMAN TISSUE; LENS; LIGHT SCATTERING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS;

ADULT; AGED; AGING; CATARACT; CRYSTALLINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; LENS, CRYSTALLINE; MIDDLE AGED; MOLECULAR WEIGHT; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; SOLUBILITY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 52049097263     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2008.07.001     Document Type: Article

References (59)

1. Andley U.P. Crystallins in the eye: Function and pathology. Prog. Ret. Eye Res. 26 (2007) 78-98
2. Andley U.P., and Clark B.A. Generation of oxidants in the near UV photooxidation of human lens alpha-crystallin. Invest. Ophthalmol. Vis. Sci. 30 (1989) 706-713
3. Bateman O.A., Sarra R., van Genesen S.T., Kappe G., Lubsen N.H., and Slingsby C. The stability of human acidic beta-crystallin oligomers and heterooligomers. Exp. Eye Res. 77 (2003) 409-422
4. Biswas A., and Das K. Role of ATP on the interaction of alpha crystallin with its substrates and its implications for the molecular chaperone function. J. Biol. Chem. 279 (2004) 42648-42657
5. Bloemendal H., deJong W., Jaenicke R., Lubsen N.C., Slingsby C., and Tardieu A. Ageing and vision: structure, stability and function of lens crystallins. Prog. Biophys. Mol. Biol. 86 (2004) 407-485
6. Brrokse P.S., Pinner A., Ramachandran A., Coward L., Barnes S., Kim H., and Darley-Usmar V.M. High throughput two-dimensional blue-native electrophoresis: A tool for functional proteomics of mitochondria and signaling complexes. Proteomics 2 (2002) 969-977
7. Camacho-Carvajal M.M., Wollscheid B., Aebersold R., Steimle V., and Schamel W.A. Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates. Mol. Cell Preoteomics 3 (2004) 176-182
8. Carter J.M., Hutcheson A.M., and Quinlan R.A. In vitro studies on the assembly properties of the lens proteins CP 49, CP 115: Coassembly with alpha crystallin but not with vimentin. Exp. Eye Res. 60 (1995) 181-192
9. Carver J., Aquilina A., Cooper P., Williams G., and Truscott R. Alpha crystallin: molecular chaperone and protein surfactant. Biochem. Biophys. Acta 1204 (1994) 195-206
10. Choudhary S., Xiao T., Vergara L.A., Srivastava S., Nees D., Piatigorsky J., and Ansari N.H. Role of aldehyde dehydrogenase isozymes in the defense of rat lens and human lens epithelial cells against oxidative stress. Invest. Ophthalmol. Vis. Sci. 46 (2005) 259-267
11. Claeys D., Geering K., and Meyer B.J. Two dimensional blue native/sodium dodecyl sulfate gel electrophoresis for analysis of multimeric proteins in platelets. Electrophoresis 26 (2005) 1189-1199
12. Delaye M., and Tardieu A. Short range order of crystallin proteins accounts for eye lens transparency. Nature 302 (1983) 415-417
13. Fu S.-C.J., Su S.W., Wagner B.J., and Hart R. Characterization of lens proteins IV. Analysis of soluble high molecular weight protein aggregates in human lenses. Exp. Eye Res. 38 (1984) 485-495
14. Gilliland K.O., Freel C.D., Lane C.W., Fowler W.C., and Costello M.J. Multilamellar bodies as potential scattering particles in human age-related nuclear cataracts. Mol. Vis. 7 (2001) 120-130
15. Gilliland K.O., Johnsen S., Metlapalty S., Costello M.J., Ramamurthy B., Krishna P.V., and Balasubramanian S. Mile light scattering calculations for an Indian age-related nuclear cataract with a high density of multilamellar bodies. Mol. Vis. 14 (2008) 572-582
16. Groenen P.J.T.A., van Dongen M.J.P., Voorter C.E.M., Bloemendal H., and deJong W.W. Age-dependent deamidation of αB-crystallin. FEBS Lett. 322 (1993) 69-72
17. Hanson S.R.A., Hasan A., Smith D.L., and Smith J.B. The major in vivo modifications of human water insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp. Eye Res. 71 (2000) 195-207
18. Harrington V., and Srivastava O.P. Proteomics of crystallin species present in water insoluble proteins of normal and cataractous human lenses. Mol. Vis. 13 (2007) 1680-1694
19. Harrington V., McCall S., Huynh S., and Srivastava O.P. Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses. Mol Vis. 10 (2004) 476-489
20. Horwitz J. Alpha crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci., U.S.A. 89 (1992) 10449-10453
21. Jedziniak J., Kinoshita J.H., Yates E.M., and Benedek G.B. The concentration and localization of heavy molecular weight aggregates in aging normal and cataractous lenses. Exp. Eye Res. 20 (1975) 367-369
22. Jedziniak J.A., Nicoli D.F., Baram H., and Benedeck G.B. Quantitative verification of the existence of high molecular weight protein aggregates in intact human lens by light scattering spectroscopy. Invest. Ophthalmol. Vis. Sci. 17 (1978) 51-57
23. King G., and Holmes R. Human corneal and lens aldehyde dehydrogenases. Purification and properties of human lens ALDH1 and differential expression as major soluble proteins in human lens (ALDH1) and cornea (ALDH3). Adv. Exp. Med. Biol. 414 (1997) 19-27
24. King G., Hirst L., and Holmes R. Human corneal and lens aldehyde dehydrogenase: localization and function(s) of ocular ALDH1 and ALDH3 isozymes. Adv. Exp. Med. Biol. 463 (1999) 189-198
25. Laemmli U.K. Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 227 (1970) 1680-1685
26. Lampi K.J., Ma Z., Hanson S.R.A., Azuma M., Shih M., Shearer T.R., Smith D.L., and Smith J.B. Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry. Exp. Eye. Res. 67 (1998) 31-43
27. Liang P., and Macrae T.H. Molecular chaperone and the cytoskeleton. J. Cell Sci. 110 (1997) 1431-1440
28. Lorand L. Transglutaminase mediated cross-linking of proteins and cell aging: the erythrocyte and lens models. In: Zappia V. (Ed). Advances in Post-Translational Modifications of Proteins and Aging (1988), Plenum Press, New York 79-94
29. Lund A.L., Smith J.B., and Smith D.L. Modification of water-insoluble human lens α-crystallin. Exp. Eye Res. 63 (1996) 661-672
30. Ma Z., Hanson S.R.A., Lampi K.J., David L.L., Smith D.L., and Smith J.B. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp. Eye Res. 67 (1998) 21-30
31. Marin-Vinader L., Onnekink C., van Genesen S.T., Slingsby C., and Lubsen N.H. In vivo heteromers formation. Expression of soluble beta A4-crystallin requires coexpression of a heteromeric partner. FEBS J 273 (2006) 3172-3182
32. Matsushima H., David L.L., Hiraoka T., and Clark J.I. Loss of cytoskeletal proteins and lens cell opacification in the selenite cataract model. Exp. Eye Res. 64 (1997) 387-395
33. McDermott M., Chiesa R., Roberts J.E., and Dillon J. Photooxidation of specific residues in α-crystallin. Biochemistry 30 (1991) 8653-8660
34. Meissier M., and Chakravarti B. High molecular weight protein aggregates of calf and cow lenses: spectroscopic evaluations. Exp. Eye Res. 47 (1988) 173-183
35. Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., and Smith J.B. Post-translational modifications of water-soluble human lens crystallins from young adults. J. Biol. Chem. 269 (1994) 12494-12502
36. Muchowski P.L., Valdez M.M., and Clark J.I. α-B crystallin selectively targets intermediate filament proteins during thermal stress. Invest. Ophthalmol. Vis. Sci. 40 (1999) 951-958
37. Nagaraj R.H., Sell D.R., Prabhakaram M., Ortwerth B.J., and Monnier V.M. High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 10257-10261
38. Nijtmans L.G.J., Henderson N.S., and Holt I.J. Blue native electrophoresis to study mitochondrial and other protein complexes. Methods 26 (2002) 327-334
39. Quinlan R. Cytoskeletal competence requires protein chaperones. Prog. Mol. Subcell. Biol. 28 (2002) 219-233
40. Quinlan R.A., Carter J.M., Hutcheson A.M., and Campbell D.G. The 53 kDa polypeptide component of the bovine fibre cell cytoskeleton is derived from the 115 kDa beaded filament protein: evidence for a fiber cell specific intermediate filament protein. Curr. Eye Res. 9 (1992) 909-921
41. Roy D., and Spector A. High molecular proteins from human lenses. Exp. Eye Res. 22 (1976) 273-279
42. Schagger H., and van Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199 (1991) 223-231
43. Schagger H., Cramer W.A., and von Jagow G. Analysis of molecular masses and oligomer states of protein complexes by two-dimensional native gel electrophoresis. Anal. Biochem. 217 (1994) 220-230
44. Schamel W.W.A., and Reth M. Monomeric and oligomeric complexes of the B cell antigen receptor. Immunity. 13 (2000) 5-14
45. Searle B.C., Dasari S., Wilmarth P.A., Turner M., Reddy A.P., David L.L., and Nagalia S.R. Identification of protein modifications using MS/MS de novo sequencing and the OpenSEa alignment algorithm. J. Proteome Res. 4 (2005) 546-554
46. Spector A. Aging of lens and cataract formation. In: Sekulaer R., Kline D., and Dismukes K. (Eds). Aging and Human Visual Function (1982), Alan R. Liss, New York 27-43
47. Spector A. The search for a solution to senile cataracts. Procter Lecture. Invest. Ophthalmol. Vis. Sci. 25 (1984) 130-145
48. Srivastava O.P. Age-related increase in concentration and aggregation of degraded polypeptide in human lenses. Exp. Eye Res. 47 (1988) 525-543
49. Srivastava O.P., Srivastava K., and Silney C. Levels of crystallin fragments and identification of their origin in water soluble high molecular weight (HMW) proteins of human lenses. Curr. Eye Res. 15 (1996) 511-520
50. Srivastava O.P., Kirk M.C., and Srivastava K. Characterization of covalent multimers of crystallins in aging human lenses. J. Biol. Chem. 279 (2004) 10901-10909
51. Sun T.X., and Liang J.J. Conformational and functional differences between recombinant human alpha A- and alpha B-crystallins. J. Biol. Chem. 272 (1997) 6220-6225
52. Swamy M., Siegers G.M., Minguet S., Wollscheid B., and Schamel W.W.A. Blue native polyacrylamide gel electrophoresis (BN-PAGE) for identification and analysis of multiprotein complexes. Sci. STKE 345 (2006) 14
53. Takemoto L. Increased deamidation of asparagines 101 from alpha-A crystallin in high molecular aggregate of normal human lens. Exp. Eye Res. 68 (1999) 641-645
54. Takemoto L., and Boyle D. Increased deamidation of asparagines during human senile cataractogenesis. Mol. Vis. 6 (2000) 164-168
55. Takemoto L., and Ponce A.A. Decreased association of aged alpha crystallins with gamma crystallins. Exp. Eye Res. 83 (2006) 793-797
56. Ting H.-H., and Crabbe M.J.C. Bovine lens aldehyde dehydrogenase: Purification and preliminary characterization. Biochem. J. 215 (1983) 351-359
57. Ueda Y., Duncan M., and David L.L. Lens proteomics: The accumulation of crystallin modifications in mouse lens with age. Invest. Ophthalmol. Vis. Sci. 43 (2002) 205-215
58. van Kleef F.S.M., Willems-Thijssen W., and Hoenders H.J. Inter degradation and deamidation of α-crystallin subunits. Eur. J. Biochem. 66 (1976) 477-483
59. Yang Z., Chamorro M., Smith D.L., and Smith J.B. Identification of the major component of high molecular crystallins from old human lenses. Exp Eye Res. 13 (1994) 415-421