Lp82 calpain during rat lens maturation and cataract formation

Current Eye Research

Volumn 17, Issue 11, 1998, Pages 1037-1043

  Shearer, T R ^a   Ma, H ^a   Shih, M ^a   Hata, I ^a   Fukiage, C ^b   Nakamura, Y ^b   Azuma, M ^b  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b SENJU PHARMACEUTICAL CO LTD   (Japan)

Author keywords

Casein zymography; Immunoblot; Lens maturation; Lp82; m calpain; mRNA; Rat lens selenite cataract

Indexed keywords

CALPAIN; CYSTEINE PROTEINASE; ISOENZYME; LENS PROTEIN; MESSENGER RNA; SELENITE;

ANIMAL TISSUE; ARTICLE; CATARACTOGENESIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME LINKED IMMUNOSORBENT ASSAY; EYE DEVELOPMENT; IMMUNOBLOTTING; LENS; NEWBORN; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

AGING; ANIMALS; CALPAIN; CASEINS; CATARACT; CHROMATOGRAPHY, DEAE-CELLULOSE; ENZYME-LINKED IMMUNOSORBENT ASSAY; IMMUNOBLOTTING; ISOENZYMES; LENS, CRYSTALLINE; RATS; RATS, SPRAGUE-DAWLEY; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; SODIUM SELENITE;

EID: 0031767798     PISSN: 02713683     EISSN: None     Source Type: Journal    
DOI: 10.1076/ceyr.17.11.1037.5232     Document Type: Article

References (18)

1. Ma H, Fukiage C, Azuma M, Shearer TR. Cloning and expression of mRNA for calpain Lp82 from rat lens: splice variant of p94. Invest Ophthalmol Vis Sci. 1998;39(2):454-461.
2. Ma H, Shih M, Hata I, Fukiage C, Azuma M, Shearer TR. Lens-specific calpain, Lp82, is expressed and enzymatically active in young rat lens. Exp Eye Res. In press.
3. Croall DE, DeMartino GN. Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol Rev. 1991;71(3):813-847.
4. Dear N, Matena K, Vingron M, Boehm T. A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution. Genomics. 1997;45(1):175-184.
5. Sorimachi H, Ishiura S, Suzuki K. Structure and physiological function of calpains. Biochem J. 1997;328(pt 3): 721-732.
6. Shearer TR, Ma H, Fukiage C, Azuma M. Selenite nuclear cataract: review of the model. Molec Vision. 1997;3:8.
7. David LL, Azuma M, Shearer TR. Cataract and the acceleration of calpain-induced beta-crystallin insolubilization occurring during normal maturation of rat lens. Invest Ophthalmol Vis Sci. 1994;35(3):785-793.
8. David LL, Shearer TR. Calcium-activated proteolysis in the lens nucleus during selenite cataractogenesis. Invest Ophthalmol Vis Sci. 1984;25(11):1275-1283.
9. Richard I, Broux O, Allamand V, et al. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 1995;81(1):27-40.
10. Ma H, Shih M, Throneberg DB, David LL, Shearer TR. Changes in calpain II mRNA in young rat lens during maturation and cataract formation. Exp Eye Res. 1997;64(3): 437-445.
11. Fukiage C, Azuma M, Nakamura Y, Tamada Y, Shearer TR. Calpain-induced light scattering by crystalline from three rodent species. Exp Eye Res. 1997;65(6):757-770.
12. Raser KJ, Posner A, Wang KK. Casein zymography: a method to study μ-calpain, m-calpain, and their inhibitory agents. Arch Biochem Biophys. 1995;319(1):211-216.
13. David LL, Varnum MD, Lampi KJ, Shearer TR. Calpain II in human lens. Invest Ophthalmol Vis Sci. 1989;30(2): 269-275.
14. Varnum MD, David LL, Shearer TR. Age-related changes in calpain II and calpastatin in rat lens. Exp Eye Res. 1989;49(6):1053-1065.
15. Reidy M, Timm E Jr, Stewart C. Quantitative RT-PCR for measuring gene expression. Biotechniques. 1995;18:70-76.
16. Azuma M, Fukiage C, David LL, Shearer TR. Activation of calpain in lens: a review and proposed mechanism. Exp Eye Res. 1997;64(4):529-538.
17. Molinari M, Carafoli E. Calpain: a cytosolic proteinase active at the membranes. J Memb Biol. 1997;156(1):1-8.
18. Sorimachi H, Kinbara K, Kimura S, et al. Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J Biol Chem. 1995;270(52):31158-31162.