In vivo carbamylation and acetylation of water-soluble human lens αB-crystallin lysine 92

Protein Science

Volumn 10, Issue 6, 2001, Pages 1130-1136

  Lapko, Veniamin N ^a   Smith, David L ^a   Smith, Jean B ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

Acetylation; Carbamylation; Lens crystallins; Mass spectrometry; Post translational modifications

Indexed keywords

ALPHA B CRYSTALLIN LYSINE; ALPHA CRYSTALLIN; LENS PROTEIN; LYSINE; TRYPSIN; UNCLASSIFIED DRUG;

ACETYLATION; ARTICLE; CATARACTOGENESIS; CONTROLLED STUDY; HUMAN; HUMAN CELL; IN VIVO STUDY; LENS; MASS SPECTROMETRY; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MODIFICATION; PROTEIN PROCESSING;

ACETYLATION; CARBAMATES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CRYSTALLINS; HUMANS; LENS, CRYSTALLINE; LYSINE; MASS SPECTROMETRY; PEPTIDES; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TIME FACTORS; TRYPSIN; WATER;

EID: 0035008831     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.40901     Document Type: Article

References (40)

1. Beswick, H.T. and Harding, J.J. 1984. Conformational changes induced in bovine lens α-crystallin by carbamylation. Biochem. J. 223: 221-227.
2. Beswick, H.T. and Harding, J.J. 1987. High-molecular-weight crystallin aggregate formation resulting from non-enzymic carbamylalion of lens crystallins: Relevance to cataract formation. Exp. Eye Res. 45: 569-578.
3. Cherian, M. and Abraham, E.C. 1995. Decreased molecular chaperone property of α-crystallins due to posttranslational modifications. Biochem. Biophys. Res. Commun. 208: 675-679.
4. Crompton, M., Rixon, K.C., and Harding, J.J. 1985. Aspirin prevents carbamylation of soluble lens proteins and prevents cyanate-induced phase separation opacities in vitro: A possible mechanism by which aspirin could prevent cataract. Exp. Eye Res. 40: 297-311.
5. Derham, B.K. and Harding, J.J. 1999. α-Crystallin as a molecular chaperone. Prog. Retin. Eye Res. 18: 463-509.
6. Fujii, N., Ishibashi, Y., Satoh, K., Fujino, M., and Harada, K. 1994. Simultaneous racemization and isomerization at specific aspartic acid residues in αB-crystallin from the aged human lens. Biochim. Biophys. Acta 1204: 157-163.
7. Groenen, P.J.T.A., van Dongen, M.J.P., Voorter, C.E.M., Bloemendal, H., and de Jong, W.W. 1993. Age-dependent deamidation of αB-crystallin. FEBS Lett. 322: 69-72.
8. Groenen, P.J.T.A., Merck, K.B., de Jong, W.W., and Bloemendal, H. 1994. Structure and modifications of the junior chaperone α-crystallin: From lens transparency to molecular pathology. Eur. J. Biochem. 225: 1-19.
9. Harding, J.J. and Crabbe, M.J.C. 1984. The lens: Development, proteins, metabolism and cataract. In The eye. (ed. H. Davson), pp. 207-192. Academic Press, Orlando, FL.
10. Harding, J.J. and Rixon, K.C. 1980. Carbamylation of lens proteins: A possible factor in cataractogenesis in some tropical countries. Exp. Eye Res. 31: 567-571.
11. Hasan, A., Smith, J.B., Qin, W., and Smith, D.L. 1993. The reaction of bovine lens αA-crystallin with aspirin. Exp. Eye Res. 57: 29-35.
12. He, S., Pan, S., Wu, K., Amster, J., and Orlando, R. 1995. Analysis of normal human fetal eye lens crystallins by high-performance liquid chromatography/mass spectrometry. J. Mass Spectrom. 30: 424-431.
13. Horwitz, J. 1992. α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. 89: 10449-10453.
14. Jimenez-Asensio, J., Colvis, C.M., Kowalak, J.A., Duglas-Tabor, Y., Datiles, M.B., Moroni, M., Mura, U., Rao, C.M., Balasubramanian, D., Janjani, A., et al. 1999. An atypical form of αB-crystallin is present in high concentration in some human cataractous lenses. J. Biol. Chem. 274: 32287-32294.
15. Kleiman, N.J., Chiesa, R., Gawinowicz-Kolks, M.A., and Spector, A. 1988. Phosphorylation of β-crystallin B2 (βBp) in the bovine lens. J. Biol. Chem. 263: 14978-14983.
16. Kouzarides, T. 2000. Acetylation: A regulatory modification to rival phosphorylation? EMBO J. 19: 1176-1179.
17. Kraus, L.M. and Kraus, A.P. 1998. The search for the uremic toxin: The case for carbamoylation of amino acids and proteins. Wien. Klin. Wochenschr. 110: 521-530.
18. Kraus, L.M., Elberger, A.J., Handorf, C.R., Pabst, M.J., and Kraus, A.P. 1994. Urea-derived cyanate forms ∈-amino-carbainoyl-lysine (homocitrulline) in leukocyte proteins in patients with end-stage renal disease on peritoneal dialysis. J. Lab. Clin. Med. 123: 882-891.
19. Lapko, V.N., Smith, D.L., and Smith, J.B. 2000. Identification of an artifact in the mass spectrometry of proteins derivatized with iodoacetamide. J. Mass Spectrom. 35: 572-575.
20. Lin, P., Smith, D.L., and Smith, J.B. 1997. In vivo modification of the C-terminal lysine of human lens αB-crystallin. Exp. Eye Res. 65: 673-680.
21. Lin, P.P., Barry, R.C., Smith, D.L., and Smith, J.B. 1998. In vivo acetylation identified at Lysine 70 of human lens αA-crystallin. Protein Sci. 1: 1452-1457.
22. Lund, A.L., Smith, J.B., and Smith, D.L. 1996. Modifications of the water-insoluble human lens α-crystallins. Exp. Eye Res. 63: 661-672.
23. Ma, Z., Hanson, S.R., Lampi, K., David, L., Smith, D.L., and Smith, J.B. 1998. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp. Eye Res. 67: 21-30.
24. Magnaghi-Jaulin, L., Ait-Si-Ali, S., and Harel-Bellan, A. 2000. Histone acelylation and the control of the cell cycle. Prog. Cell Cycle Res. 4: 41-47.
25. Miesbauer, L.R., Zhou, X., Yang, Z., Yang, Z., Sun, Y., Smith, D.L., and Smith, J.B. 1994. Post-translational modifications of the water soluble human lens crystallins from young adults. J. Biol. Chem. 269: 12494-12502.
26. Ortwerth, B.J., Slight, S.H., Prabhakaram, M., Sun, Y., and Smith, J.B. 1992. Site-specific glycation of lens crystallins by ascorbic acid. Biochim. Biophys. Acta 1117: 207-215.
27. Plater, M.L., Boode, D., and Crabbe, M.J. 1997. Ibuprofen protects α-crystallin against posttranslational modification by preventing protein cross-linking. Ophthalmic Res. 29: 421-428.
28. Qin, W., Smith, J.B., and Smith, D.L. 1992. Rates of carbamylation of specific lysyl residues in bovine α-crystallins. J. Biol. Chem. 267: 26128-26133.
29. _. 1993. Reaction of aspirin with cysteinyl residues of lens γ-crystallins: A mechanism for the proposed anti-cataract effect of aspirin. Biochim. Biophys. Acta 1181: 103-110.
30. Rao, G.N. and Cotlier, E. 1988. Aspirin prevents the nonenzymatic glycosylation and carbamylation of the human eye lens crystallins in vitro. Biochem. Biophys. Res. Commun. 151: 991-996.
31. Rao, G.N., Lardis, M.P., and Cotlier, E. 1985. Acetylation of lens crystallins: A possible mechanism by which aspirin could prevent cataract formation. Biochem. Biophys. Res. Commun. 128: 1125-1132.
32. Schey, K.L., Fowler, J.G., Schwartz, J.C., Busman, M., Dillon, J., and Crouch, R.K. 1997. Complete map and identification of the phosphorylation site of bovine lens major intrinsic protein. Invest. Ophthalmol. Vis. Sci. 38: 2508-2515.
33. Sen, A.C. and Chakrabarti, B. 1990. Effect of acetylation by aspirin on the thermodynamic stability of lens crystallins. Exp. Eye Res. 51: 701-709.
34. Smith, J.B., Shun-Shin, G.A., Sun, Y., Miesbauer, L.R., Yang, Z., Yang, Z., Zhou, X., Schwedler, J., and Smith, D.L. 1995. Glutathione adducts, not carbamylated lysines are the major modification of lens α-crystallins from renal failure patients. J. Protein Chem. 14: 179-188.
35. Sterner, D.E. and Berger, S.L. 2000. Acetylation of histones and transcriptionrelated factors. Microbiol. Mol. Biol. Rev. 64: 435-459.
36. Sun, T.X., Akhtar, N., and Liang, J.J. 1998. Conformational change of human lens insoluble α-crystallin. J. Protein Chem. 17: 679-684.
37. Trepanier, D.J., Thibert, R.J., Draisey, T.F., and Caines, P.S. 1996. Carbamylation of erythrocyte membrane proteins: An in vitro and in vivo study. Clin. Biochem. 29: 347-355.
38. van Boekel, M.A.M., Hoogakker, S.E.A., Harding, J.J., and de Jong, W.W. 1996. The influence of some post-translational modifications on the chaperone-like activity of α-crystallin. Ophthalmic Res. (Suppl. 1) 28: 32-38.
39. van Heyningen, R. and Harding, J.J. 1988. A case-control study of cataract in Oxfordshire: Some risk factors. Br. J. Ophthalmol. 72: 804-808.
40. Voorter, C.E.M., de Haard-Hoekman, W.A., van den Oetelaar, P.J.M., Bloemendal, H., and de Jong, W.W. 1988. Spontaneous peptide bond cleavage in aging α-crystallin through a succinimide intermediate. J. Biol. Chem. 263: 19020-19023.