Immunohistochemical study of calpain-mediated α-crystallin proteolysis in the UPL rat hereditary cataract

Japanese Journal of Ophthalmology

Volumn 41, Issue 3, 1997, Pages 121-129

  Tomohiro, Masayuki ^a,f   Aida, Yoshitaka ^a   Inomata, Mitsushi ^b   Ito, Yoshimasa ^c   Mizuno, Aritake ^d   Sakuma, Sadashige ^e  

^a Tsukuba Research Laboratories   (Japan)

^b TOKYO METROPOLITAN INSTITUTE OF GERONTOLOGY   (Japan)

^c KINKI UNIVERSITY   (Japan)

^d IBARAKI UNIVERSITY   (Japan)

^e Osaka Prefecture University   (Japan)

^f Upjohn Research Laboratories   (Japan)

Author keywords

crystallin; Calpain; Cataract; Immunohistochemistry; Lens; UPL rat

Indexed keywords

ALPHA CRYSTALLIN; ANTIBODY; CALPAIN;

ANIMAL TISSUE; ARTICLE; CATARACT; CATARACTOGENESIS; CONTROLLED STUDY; FETUS; HETEROZYGOTE; HOMOZYGOTE; IMMUNOHISTOCHEMISTRY; IMMUNOREACTIVITY; LENS FIBER; NEWBORN; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; RAT;

ANIMALS; CALPAIN; CATARACT; CRYSTALLINS; FEMALE; IMMUNOENZYME TECHNIQUES; LENS, CRYSTALLINE; MALE; RATS; RATS, MUTANT STRAINS;

EID: 0030837684     PISSN: 00215155     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0021-5155(97)00029-4     Document Type: Article

References (25)

1. Tomohiro M, Maruyama Y, Mizuno A. Hereditary cataract rat derived from the Sprague-Dawley colony. Anim Eye Res 1993;12:37-44.
2. Tomohiro M, Maruyama Y, Yazawa K, et al. The UPL rat: A new model for hereditary cataracts with two cataract formation types. Exp Eye Res 1993;57:507-10.
3. Tomohiro M, Murata S, Yazawa K, et al. Lens development and crystallin distribution of the early onset hereditary cataract in the UPL rat. Jpn J Ophthalmol 1996;40:42-52.
4. Tomohiro M, Shinzawa S, Yazawa K, et al. Late onset hereditary cataracts in the UPL rat. J Toxicol Pathol 1996;9:73-84.
5. Croall DE, Demartino ON. Calcium-activated neutral protease (calpain) system: Structure, function, and regulation. Physiol Rev 1991;71:813-47.
6. David LL, Shearer TR. Purification of calpain II from rat lens and determination of endogenous substrates. Exp Eye Res 1986;42:227-38.
7. Yoshida H, Murachi T, Tsukahara I. Distribution of calpain I, and calpain II, and calpastatin in bovine lens. Invest Ophthalmol Vis Sei 1985;26:953-56.
8. David LL, Shearer TR. Role of proteolysis in lenses: A review. Lens Eye Toxicol Res 1989;6:725-47.
9. Yoshida H, Yumoto N, Tsukahara I, Murachi T. The degradation of α-crystallin at its carboxyl-terminal portion by calpain in bovine lens. Invest Ophthalmol Vis Sei 1986;27:1269-73.
10. Azuma M, David LL, Shearer TR. Cysteine protease inhibitor E64 reduces the rat of formation of selenite cataract in the whole animal. Curr Eye Res 1991;10:657-66.
11. Hightower KR, David LL, Shearer TR. Regional distribution of free calcium in selenite cataract, relation to calpain II. Invest Ophthalmol Vis Sei 1987;28:1702-6.
12. Iwasaki N, David LL, Shearer TR. Crystallin degradation and insolubilization in regions of young rat lens with calcium ionophore cataract. Invest Ophthalmol Vis Sei 1995;36:502-9.
13. Azuma M, Shearer TR. Involvement of calpain in diamideinduced cataract in cultured lenses. FEBS Letters 1992;307: 313-17.
14. Azuma M, David LL, Shearer TR. Hydration and elevated calcium alone do not produce xylose nuclear cataract, role of proteolysis by calpain. Ophthal Res 1992;24:8-14.
15. Kadoya K, Azuma M, David LL, Shearer TR. Role of calpain in hydrogen peroxide induced cataract. Curr Eye Res 1993; 12:341-46.
16. David LL, Calvin HI, Fu S-CJ. Buthione sulfoximine induced cataracts in mice contain insolubilized crystallins with calpain II cleavage sites. Exp Eye Res 1994;59:501-4.
17. Humason GL. Animal tissue technique. 2nd ed. San Francisco: W.H. Freeman and Company, 1967:432.
18. Inomata M, Hayashi M, Ohno-Iwashita Y, Tsubuki S, Saido TC, Kawashima S. Involvement of calpain in integrin-mediated signal transduction. Arch Biochem Biophys 1996;328: 129-34.
19. de Jong WW, van der Ouderra FJ, Versteeg M, et al. Primary structures of the α-crystallin A chains of seven mammalian species. Eur J Biochem 1975;53:237-42.
20. van der Ouderra FJ, de Jong WW, Bloemendal H. The amino acid sequence of αA2 chain of bovine α-crystallin. Eur J Biochem 1973;39:207-2.
21. van der Ouderra FJ, de Jong WW, Hilderink A, Bloemendal H. The amino-acid sequence of aB2 chain of bovine α-crystallin. Eur J Biochem 1974;49:157-68.
22. Honvits J. α-Crystallin can function as a molecular chaperone. Proc Natl Acad Sei USA 1992;89:10449-53.
23. Kelly MJ, David LL, Iwasaki N, et al. α-crystallin chaperone activity is reduced by calpain II in vitro and selenite cataract. J Biol Chem 1993;268:18844-49.
24. Takemoto L, Emmons T, Honvitz J. The C-terminal region of α-crystallin, involvement in protection against heat-induced denaturation. Biochem J 1993;294:435-38.
25. Takemoto L. Release of αA-crystallin sequence 158-173 correlates with a decrease in the molecular chaperone properties of native α-crystallin. Exp Eye Res 1994,9:239-42.