메뉴 건너뛰기




Volumn 64, Issue 3, 1997, Pages 437-445

Changes in calpain II mRNA in young rat lens during maturation and cataract formation

Author keywords

Calpain II; Cataract; Lens; Maturation; mRNA; Northern blot; Quantitative PCR; Rat

Indexed keywords

CALPAIN II; MESSENGER RNA; SODIUM SELENITE; UNCLASSIFIED DRUG;

EID: 0031106297     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1996.0229     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 0026775178 scopus 로고
    • Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I
    • Adachi, Y., Kitahara-Ozawa, A., Sugamura, K., Lee, W. J., Yodoi, J., Maki, M., Murachi, T. and Hatanaka, M. (1992). Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I. J. Biol. Chem. 267, 19373-8.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19373-19378
    • Adachi, Y.1    Kitahara-Ozawa, A.2    Sugamura, K.3    Lee, W.J.4    Yodoi, J.5    Maki, M.6    Murachi, T.7    Hatanaka, M.8
  • 2
    • 0030069596 scopus 로고    scopus 로고
    • Calcium ionophore induced proteolysis and cataract: Inhibition by cell permeable calpain antagonists
    • Anderson, J., Marcantonio, J. M. and Duncan, G. (1996). Calcium ionophore induced proteolysis and cataract: inhibition by cell permeable calpain antagonists. Biochem. Biophys. Res. Commun. 218, 893-901.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 893-901
    • Anderson, J.1    Marcantonio, J.M.2    Duncan, G.3
  • 3
    • 0025837971 scopus 로고
    • Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni
    • Anderson, K., Tom, T. D. and Strand, M. (1991). Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni. J. Biol. Chem. 266, 15085-90.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15085-15090
    • Anderson, K.1    Tom, T.D.2    Strand, M.3
  • 4
    • 0026579054 scopus 로고
    • Review of selenite cataract
    • Anderson, R. S. and Shearer, T. R. (1992). Review of selenite cataract Curr. Eye Res. 11, 1147-60.
    • (1992) Curr. Eye Res. , vol.11 , pp. 1147-1160
    • Anderson, R.S.1    Shearer, T.R.2
  • 5
    • 0026632965 scopus 로고
    • Involvement of calpain in diamide-induced cataract in cultured lenses
    • Azuma, M. and Shearer, T. R. (1992). Involvement of calpain in diamide-induced cataract in cultured lenses. FEBS Lett. 307, 313-7.
    • (1992) FEBS Lett. , vol.307 , pp. 313-317
    • Azuma, M.1    Shearer, T.R.2
  • 6
    • 0024956788 scopus 로고
    • Relative abundance of aldose reductase mRNA in rat lens undergoing development of osmotic cataracts
    • Bekhor, I., Songtao, S., Carper, D., Nishimura, C. and Unakar, N. J. (1989). Relative abundance of aldose reductase mRNA in rat lens undergoing development of osmotic cataracts. Curr. Eye Res. 8, 1299-308.
    • (1989) Curr. Eye Res. , vol.8 , pp. 1299-1308
    • Bekhor, I.1    Songtao, S.2    Carper, D.3    Nishimura, C.4    Unakar, N.J.5
  • 8
    • 0029124147 scopus 로고
    • Role of transcription, translation, and protein turnover in controlling the distribution of 3-hydroxy-3-methylglutaryl coenzyme a reductase in the lens
    • Cenedella, R. J. (1995). Role of transcription, translation, and protein turnover in controlling the distribution of 3-hydroxy-3-methylglutaryl coenzyme A reductase in the lens. Invest. Ophthalmol. Vis. Sci. 36, 2133-41.
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 2133-2141
    • Cenedella, R.J.1
  • 9
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall, D. E. and DeMartino, G. N. (1991). Calcium-activated neutral protease (calpain) system: structure, function, and regulation. [Review]. Physiol. Rev. 71, 813-47.
    • (1991) Physiol. Rev. , vol.71 , pp. 813-847
    • Croall, D.E.1    DeMartino, G.N.2
  • 10
    • 0028223362 scopus 로고
    • Cataract and the acceleration of calpain-induced β-crystallin insolubilization occurring during normal maturation of rat lens
    • 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.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 785-793
    • David, L.L.1    Azuma, M.2    Shearer, T.R.3
  • 11
    • 0027937773 scopus 로고
    • Buthionine sulfoximine induced cataracts in mice contain insolubilized crystallins with calpain II cleavage sites
    • David, L. L., Calvin, H. I. and Fu, S.-C. J. (1994). Buthionine sulfoximine induced cataracts in mice contain insolubilized crystallins with calpain II cleavage sites. Invest. Ophthalmol. Vis. Sci. 59, 501-4.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.59 , pp. 501-504
    • David, L.L.1    Calvin, H.I.2    Fu, S.-C.J.3
  • 12
    • 0027468977 scopus 로고
    • Sequence analysis of lens β-crystallins suggests involvement of calpain in cataract formation
    • David, L. L., Shearer, T. R. and Shih, M. (1993). Sequence analysis of lens β-crystallins suggests involvement of calpain in cataract formation. J. Biol. Chem. 268, 1937-40.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1937-1940
    • David, L.L.1    Shearer, T.R.2    Shih, M.3
  • 14
    • 0027424161 scopus 로고
    • Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit
    • DeLuca, C. I., Davies, P. L., Samis, J. A. and Elce, J. S. (1993). Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit. Biochim. Biophys. Acta 1216, 81-93.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 81-93
    • DeLuca, C.I.1    Davies, P.L.2    Samis, J.A.3    Elce, J.S.4
  • 15
    • 0028816606 scopus 로고
    • Calpain expression in lymphoid cells. Increased mRNA and protein levels after cell activation
    • Deshpande, R. V., Goust, J. M., Chakrabarti, A. K., Barbosa, E., Hogan, E. L. and Banik, N. L. (1995). Calpain expression in lymphoid cells. Increased mRNA and protein levels after cell activation. J. Biol. Chem. 270, 2497-505.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2497-2505
    • Deshpande, R.V.1    Goust, J.M.2    Chakrabarti, A.K.3    Barbosa, E.4    Hogan, E.L.5    Banik, N.L.6
  • 16
    • 0028880896 scopus 로고
    • Recombinant calpain II: Improved expression systems and production of a C105A active-site mutant for crystallography
    • Elce, J. C., Hegadorn, C., Gauthier, S., Vince, J. W. and Davies, P. L. (1995). Recombinant calpain II: improved expression systems and production of a C105A active-site mutant for crystallography. Protein Engineering 8, 843-8.
    • (1995) Protein Engineering , vol.8 , pp. 843-848
    • Elce, J.C.1    Hegadorn, C.2    Gauthier, S.3    Vince, J.W.4    Davies, P.L.5
  • 17
    • 0026911137 scopus 로고
    • Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?
    • Goll, D. E., Thompson, V. F., Taylor, R. G. and Zalewska, T. (1992). Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? [Review]. BioEssays 14, 549-56.
    • (1992) BioEssays , vol.14 , pp. 549-556
    • Goll, D.E.1    Thompson, V.F.2    Taylor, R.G.3    Zalewska, T.4
  • 18
    • 0028899142 scopus 로고
    • Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures
    • Hong, D. H. and Forsberg, N. E. (1995). Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures. Mol. Cell. Endocrin. 108, 199-209.
    • (1995) Mol. Cell. Endocrin. , vol.108 , pp. 199-209
    • Hong, D.H.1    Forsberg, N.E.2
  • 19
    • 0026801930 scopus 로고
    • Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits
    • Ilian, M. A. and Forsberg, N. E. (1992). Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits. Biochem J. 287, 163-71.
    • (1992) Biochem J. , vol.287 , pp. 163-171
    • Ilian, M.A.1    Forsberg, N.E.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (London) 227, 680-5.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0007357905 scopus 로고
    • 2+ protease and its inhibitor protein: Calpain and calpastatin
    • Academic Press Inc.: NY, U.S.A.
    • 2+ protease and its inhibitor protein: calpain and calpastatin. In Calcium and Cell Function. Vol. IV, Academic Press Inc.: NY, U.S.A.
    • (1983) Calcium and Cell Function , vol.4
    • Murachi, T.1
  • 23
    • 0029105722 scopus 로고
    • Quantitative RT-PCR for measuring gene expression
    • Reidy, M. C., Timm, E. A. Jr. and Stewart, C. C. (1995). Quantitative RT-PCR for measuring gene expression. BioTechniques 18, 70-6.
    • (1995) BioTechniques , vol.18 , pp. 70-76
    • Reidy, M.C.1    Timm Jr., E.A.2    Stewart, C.C.3
  • 24
    • 0027377973 scopus 로고
    • IGF-1 enhancement of FGF-induced lens fiber differentiation in rats of different ages
    • Richardson, N. A., Chamberlain, C. and McAvoy, J. W. (1993). IGF-1 enhancement of FGF-induced lens fiber differentiation in rats of different ages. Invest. Ophthalmol. Vis. Sci. 34(12), 3303-12.
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , Issue.12 , pp. 3303-3312
    • Richardson, N.A.1    Chamberlain, C.2    McAvoy, J.W.3
  • 25
    • 0020314081 scopus 로고
    • Role of calcium in selenium cataract
    • Shearer, T. R. and David, L. L. (1983). Role of calcium in selenium cataract. Curr. Eye Res. 2, 777-84.
    • (1983) Curr. Eye Res. , vol.2 , pp. 777-784
    • Shearer, T.R.1    David, L.L.2
  • 27
    • 0029050241 scopus 로고
    • Precipitation of crystallins from young rat lens by endogenous calpain
    • Shearer, T. R., Shih, M., Azuma, M. and David, L. L. (1995). Precipitation of crystallins from young rat lens by endogenous calpain. Exp. Eye Res. 61, 141-50.
    • (1995) Exp. Eye Res. , vol.61 , pp. 141-150
    • Shearer, T.R.1    Shih, M.2    Azuma, M.3    David, L.L.4
  • 28
    • 0029790711 scopus 로고    scopus 로고
    • In vitro precipitation of rat lens crystallins by calpain I-a calpain requiring low amounts of calcium for activation
    • Shearer, T. R., Throneberg, D. B. and Shih, M. (1996). In vitro precipitation of rat lens crystallins by calpain I-a calpain requiring low amounts of calcium for activation. Ophthalmol. Res. 28, 109-14.
    • (1996) Ophthalmol. Res. , vol.28 , pp. 109-114
    • Shearer, T.R.1    Throneberg, D.B.2    Shih, M.3
  • 29
    • 0027089685 scopus 로고
    • Modulation of cellular signals by calpain
    • Suzuki, K., Saido, T. C. and Hirai, S. (1992). Modulation of cellular signals by calpain. [Review]. Ann. NY Acad. Sci. 674, 218-27.
    • (1992) Ann. NY Acad. Sci. , vol.674 , pp. 218-227
    • Suzuki, K.1    Saido, T.C.2    Hirai, S.3
  • 31
    • 0024850771 scopus 로고
    • Age related changes in calpain II and calpastatin in rat lens
    • Varnum, M. D., David, L. L. and Shearer, T. R. (1989). Age related changes in calpain II and calpastatin in rat lens. Exp. Eye Res. 49, 1053-65.
    • (1989) Exp. Eye Res. , vol.49 , pp. 1053-1065
    • Varnum, M.D.1    David, L.L.2    Shearer, T.R.3
  • 32
    • 0029054037 scopus 로고
    • Calcimycin-induced lens epithelial cell apoptosis contributes to cataract formation
    • Wang-Cheng, L., Kusak, J. R., Wang, G.-M., Wu, Z.-Q. and Spector, A. (1995). Calcimycin-induced lens epithelial cell apoptosis contributes to cataract formation. Exp. Eye Res. 61, 91-8.
    • (1995) Exp. Eye Res. , vol.61 , pp. 91-98
    • Wang-Cheng, L.1    Kusak, J.R.2    Wang, G.-M.3    Wu, Z.-Q.4    Spector, A.5
  • 33
    • 0021885110 scopus 로고
    • Distribution of calpain I, calpain II, and calpastatin in bovine lens
    • Yoshida, H., Murachi, T. and Tsukahara, I. (1985). Distribution of calpain I, calpain II, and calpastatin in bovine lens. Invest. Ophthalmol. Vis. Sci. 26, 953-6.
    • (1985) Invest. Ophthalmol. Vis. Sci. , vol.26 , pp. 953-956
    • Yoshida, H.1    Murachi, T.2    Tsukahara, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.