Truncation of βA3/A1-crystallin during aging of the bovine lens; possible implications for lens optical quality

Experimental Eye Research

Volumn 68, Issue 1, 1999, Pages 99-103

  Werten, Paul J L ^a   Vos, Erwin ^a   De Jong, Wilfried W ^a  

^a RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

Aging; Bovine; Cataract; Cleavage; Eye lens; Proteolysis; Truncation; crystallin; A1; A3

Indexed keywords

BETA CRYSTALLIN; CRYSTALLIN; EYE PROTEIN;

AGING; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CATTLE; LENS; NONHUMAN; OPTICS; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; ANIMAL; BIOSYNTHESIS; CATARACT; EYE REFRACTION; METABOLISM; MOLECULAR GENETICS; PATHOPHYSIOLOGY; PHYSIOLOGY; VISUAL ACUITY;

AGING; AMINO ACID SEQUENCE; ANIMALS; CATARACT; CATTLE; CRYSTALLINS; EYE PROTEINS; LENS, CRYSTALLINE; MOLECULAR SEQUENCE DATA; REFRACTION, OCULAR; VISUAL ACUITY;

EID: 0032587683     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1998.0584     Document Type: Article

References (25)

1. Bax, B., Lapatto, R., Nalini, V., Driessen, H., Lindley, P. F., Mahadevan, D., Blundell, T. L. and Slingsby, C. (1990). X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins. Nature 347, 776-80.
2. Benedek, G. B. (1971). Theory of transparency of the eye. Appl. Opt. 10, 459-73.
3. Berbers, G. A., Brans, A. M., Hoekman, W. A., Slingsby, C., Bloemendal, H. and de Jong, W. W. (1983). Aggregation behavior of the bovine β-crystallin Bp chain studied by limited proteolysis. Biochim. Biophys. Acta 748, 213-19.
4. Blundell, T., Lindley, P., Miller, L., Moss, D., Slingsby, C., Tickle, I., Turnell, B. and Wistow, G. (1981). The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II. Nature 289, 771-7.
5. Bours, J., Doepfmer, K. and Hockwin, O. (1976). Isoelectric focusing of crystallins from different parts of the bovine and dog lens in dependence of age. Doc. Ophthalmol. Proc. Ser. 8, 75-98.
6. David, L. L., Azuma, M. and Shearer, T. R. (1994). Cataract and the acceleration of calpain-induced β-crystallin insolubilization occurring during normal maturation of rat lens. Invest. Ophthalmol. Vis. Sci. 35, 785-93.
7. Delaye, M. and Tardieu, A. (1983). Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302, 415-17.
8. Driessen, H. P. C., Herbrink, P., Bloemendal, H. and de Jong, W. W. (1981). Primary structure of the bovine β-crystallin Bp chain. Internal duplication and homology with γ-crystallin. Eur. J. Biochem. 121, 83-91.
9. Gorin, B. and Horwitz, J. (1984). Cloning and characterization of a cow beta crystallin cDNA. Curr. Eye Res. 3, 939-48.
10. Harding, J. (1991). Common pathways to cataract. In: Cataract Biochemistry Epidemiology and Pharmacology. Pp. 191. Chapman & Hall: London, U.K.
11. Hejtmancik, J. F., Wingfield, P. T., Chambers, C., Russell, P., Chen, H. C., Sergeev, Y. V. and Hope, J. N. (1997). Association properties of βB2- and βA3-crystallin: Ability to form dimers. Protein Eng. 10, 1347-52.
12. Hogg, D., Tsui, L. C., Gorin, M. and Breitman, M. L. (1986). Characterization of the human β-crystallin gene HuβA3/A1 reveals ancestral relationships among the βγ-crystallin superfamily. J. Biol. Chem. 261, 12420-7.
13. Hope, J. N., Chen, H. C. and Hejtmancik, J. F. (1994). βa3/a1-crystallin association: Role of the N-terminal arm. Protein Eng. 7, 445-51.
14. Inana, G., Shinohara, T., Maizel, J. V. J. and Piatigorsky, J. (1982). Evolution and diversity of the crystallins. Nucleotide sequence of a β-crystallin mRNA from the mouse lens. J. Biol. Chem. 257, 9064-71.
15. Kozak, M. (1989). The scanning model for translation: An update. J. Cell Biol. 108, 229-41.
16. Kozak, M. (1991). An analysis of vertebrate mRNA sequences: Intimations of translational control. J. Cell. Biol. 115, 887-903.
17. Peterson, C. A. and Piatigorsky, J. (1986). Preferential conservation of the globular domains of the βA3/A1-crystallin polypeptide of the chicken eye lens. Gene 45, 139-47.
18. Pierscionek, B. and Augusteyn, R. C. (1988). Protein distribution patterns in concentric layers from single bovine lenses: Changes with development and ageing. Curr. Eye Res. 7, 11-23.
19. Quax-Jeuken, Y., Janssen, C., Quax, W., van Den Heuvel, R. and Bloemendal, H. (1984). Bovine β-crystallin complementary DNA clones. Alternating proline/alanine sequence of βB1 subunit originates from a repetitive DNA sequence. J. Mol. Biol. 180, 457-72.
20. Sergeev, Y., Wingfield, P., Hope, J. and Hejtmancik, J. F. (1997). The role of C-terminal extension in βB2-crystallin oligomerization. Invest. Ophthalmol. Vis. Sci. 38, S206.
21. Shih, M., Lampi, K. J., Shearer, T. R. and David, L. L. (1998). Cleavage of β-crystallins during maturation of bovine lens. Mol. Vis. 4, 4 < http://www.emory.edu/ molvis/v4/p4 >.
22. Slingsby, C. and Bateman, O. A. (1994). Formation and crystallization of the eye lens heterodimer βB2-βB3-crystallin. Exp. Eye Res. 58, 761-4.
23. Trinkl, S., Glockshuber, R. and Jaenicke, R. (1994). Dimerization of βB2-crystallin: The role of the linker peptide and the N- and C-terminal extensions. Protein Sci. 3, 1392-400.
24. Werten, P. J. L., Carver, J. A., Jaenicke, R. and de Jong, W. W. (1996). The elusive role of the N-terminal extension of βA3- and βA1-crystallin. Protein Eng. 9, 1021-8.
25. Wistow, G., Turnell, B., Summers, L., Slingsby, C., Moss, D., Miller, L., Lindley, P. and Blundell, T. (1983). X-ray analysis of the eye lens protein γII-crystallin at 1·9 Å resolution. J. Mol. Biol. 170, 175-202.