Lp85 calpain is an enzymatically active rodent-specific isozyme of lens Lp82

Current Eye Research

Volumn 20, Issue 3, 2000, Pages 183-189

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

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b SENJU PHARMACEUTICAL CO LTD   (Japan)

Author keywords

Calpain; Lens; Lp82; Lp85; Protease; Rat

Indexed keywords

AMINO ACID; CALPAIN; CASEIN; COMPLEMENTARY DNA; RNA;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; IMMUNOBLOTTING; LENS; MATURATION; MIGRATION; MOLECULAR CLONING; MOLECULAR WEIGHT; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; RAT; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SPECIES DIFFERENCE; ZYMOGRAPHY;

EID: 0034076740     PISSN: 02713683     EISSN: None     Source Type: Journal    
DOI: 10.1076/0271-3683(200003)2031-9FT183     Document Type: Article

References (12)

1. Sorimachi H, Ishihara S, Suzuki K. Structure and physiological function of calpains. BiochemJ. 1997; 328:721-732.
2. 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; 39:454-461.
3. Fukiage C, Ma H, Azuma M, Shearer TR. Molecular cloning and sequence analysis of calpain Rt88 from rat retina/choroid. [ARVO Abstract] Invest Ophthalmol Vis Sci. 1998;39:(4), S43, abstract # 190.
4. Herasse M, Ono Y, Fougerousse F, Kimura E, Stockholm D et al. I. Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional events Mol Cell Biol. 1999;19:4047-4055
5. Ma H, Hata I, Shih M, Fukiage C, Nakamura Y, Azuma M, Shearer TR. Lp82 is the dominant form of calpain in young mouse lens. Exp Eye Res. 1999;68:447-456.
6. Ma H, Shih M, Hata I, Fukiage C, Azuma M, Shearer TR. Protein for Lp82 calpain is expressed and enzymatically active in young rat lens. Exp Eye Res. 1998;67:221-229.
7. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227:680-685.
8. Towbin H, Steahelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci. (USA) 1979;76:4350-4354.
9. Raser KJ, Posner A, Wang KKW. Casein zymography: A method to study mu-calpain, m-calpain, and their inhibitory agents. Arch Biochem Biophys. 1995;319:211-216.
10. David LL, Shearer TR. Purification of calpain II from rat lens and determination of endogenous substrates. Exp Eye Res. 1986;42:227-38.
11. Shearer TR, Ma H, Shin M, Hata I, Fukiage C, Nakamura Y, Azuma M. Lp82 calpain during rat lens maturation and cataract formation. Curr Eye Res. 1998;17:1037-1043.
12. Smolders RH, van Geel IG, Gerards WL, Bloemendal H, de long WW. Reduced chaperone-like activity of alpha A(ins)-crystallin, an alternative splicing product containing a large insert peptide. J Biol Chem. 1995;270:13916-24.