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Volumn 14, Issue , 2008, Pages 1872-1885

Isolation and characterization of βA3-crystallin associated proteinase from α-crystallin fraction of human lenses

Author keywords

[No Author keywords available]

Indexed keywords

3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 1 PROPANESULFONIC ACID; ALPHA CRYSTALLIN; ALPHAA CRYSTALLIN; ALPHAB CRYSTALLIN; ARGININE; BETA CRYSTALLIN; BETAA3 CRYSTALLIN; BETAB1 CRYSTALLIN; BETAB2 CRYSTALLIN; CRYSTALLIN; DEOXYCHOLATE SODIUM; GAMMA CRYSTALLIN; GAMMAB CRYSTALLIN; GAMMAC CRYSTALLIN; GAMMAD CRYSTALLIN; OCTYL GLUCOSIDE; PROTEINASE; SERINE; TRITON X 100; UNCLASSIFIED DRUG; DEOXYCHOLIC ACID; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN;

EID: 55349144541     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (45)
  • 1
    • 0021240896 scopus 로고
    • A synthetic endopeptidase substrate hydrolyzed by bovine lens neutral proteinase preparation
    • Wagner BJ, Fu SCJ, Margolis JW, Fleshman KR. A synthetic endopeptidase substrate hydrolyzed by bovine lens neutral proteinase preparation. Exp Eye Res 1984; 38:477-83.
    • (1984) Exp Eye Res , vol.38 , pp. 477-483
    • Wagner, B.J.1    Fu, S.C.J.2    Margolis, J.W.3    Fleshman, K.R.4
  • 2
    • 0347796615 scopus 로고
    • Purification neutral lens endopeptidase: Close similarity to a neutral proteinase in pituitary
    • Ray K, Harris H. Purification neutral lens endopeptidase: Close similarity to a neutral proteinase in pituitary. Proc Natl Acad Sci USA 1985; 82:7545-9.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7545-7549
    • Ray, K.1    Harris, H.2
  • 3
    • 0021081033 scopus 로고
    • Isolation and characterization of a 25 K serine proteinase from bovine lens cortex
    • Srivastava OP, Ortwerth BJ. Isolation and characterization of a 25 K serine proteinase from bovine lens cortex. Exp Eye Res 1983; 37:597-612.
    • (1983) Exp Eye Res , vol.37 , pp. 597-612
    • Srivastava, O.P.1    Ortwerth, B.J.2
  • 6
    • 0023920931 scopus 로고
    • Characterization of a highly purified membrane proteinase from bovine lens
    • Srivastava OP. Characterization of a highly purified membrane proteinase from bovine lens. Exp Eye Res 1988; 46:269-83.
    • (1988) Exp Eye Res , vol.46 , pp. 269-283
    • Srivastava, O.P.1
  • 7
    • 0024600743 scopus 로고
    • Human lens membrane proteinase: Purification and age-related distributional changes in water soluble and insoluble fractions
    • Srivastava OP, Srivastava K. Human lens membrane proteinase: Purification and age-related distributional changes in water soluble and insoluble fractions. Exp Eye Res 1989; 48:161-75.
    • (1989) Exp Eye Res , vol.48 , pp. 161-175
    • Srivastava, O.P.1    Srivastava, K.2
  • 8
    • 0035166263 scopus 로고    scopus 로고
    • Role of calcium-dependent protease (s) in globalization of isolated rat lens cortical fiber cells
    • Wang L, Christensen BN, Bhatanagar A, Srivastava SK. Role of calcium-dependent protease (s) in globalization of isolated rat lens cortical fiber cells. Invest Ophthalmol Vis Sci 2001; 42:194-9.
    • (2001) Invest Ophthalmol Vis Sci , vol.42 , pp. 194-199
    • Wang, L.1    Christensen, B.N.2    Bhatanagar, A.3    Srivastava, S.K.4
  • 9
    • 0037331388 scopus 로고    scopus 로고
    • Decreased caspase-3 activity in human lens epithelium from posterior subcapsular cataracts
    • Andersson M, Honarvar A, Sjostrand J, Peterson A, Karlsson JO. Decreased caspase-3 activity in human lens epithelium from posterior subcapsular cataracts. Exp Eye Res 2003; 76:175-82.
    • (2003) Exp Eye Res , vol.76 , pp. 175-182
    • Andersson, M.1    Honarvar, A.2    Sjostrand, J.3    Peterson, A.4    Karlsson, J.O.5
  • 10
    • 33846931622 scopus 로고    scopus 로고
    • Proteolytic mechanisms underlying mitochondrial degradation in ocular lens
    • Zandy AJ, Bassnett S. Proteolytic mechanisms underlying mitochondrial degradation in ocular lens. Invest Ophthalmol Vis Sci 2007; 48:293-302.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 293-302
    • Zandy, A.J.1    Bassnett, S.2
  • 11
    • 3543046713 scopus 로고    scopus 로고
    • Temporal regulation of VEID-7 amino-trimethyl coumarin cleavage activity and caspase-6 correlate with organelle loss during lens development
    • Foley JD, Rosenbaum H, Griep AE. Temporal regulation of VEID-7 amino-trimethyl coumarin cleavage activity and caspase-6 correlate with organelle loss during lens development. J Biol Chem 2004; 279:32142-50.
    • (2004) J Biol Chem , vol.279 , pp. 32142-32150
    • Foley, J.D.1    Rosenbaum, H.2    Griep, A.E.3
  • 12
    • 33745675537 scopus 로고    scopus 로고
    • Ubiquitin-proteosome pathway function is required for lens cell proliferation and differentiation
    • Guo W, Shang F, Liu Q, Urim L, Zhang M, Taylor A. Ubiquitin-proteosome pathway function is required for lens cell proliferation and differentiation. Invest Ophthalmol Vis Sci 2006; 47:2569-75.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 2569-2575
    • Guo, W.1    Shang, F.2    Liu, Q.3    Urim, L.4    Zhang, M.5    Taylor, A.6
  • 13
    • 0013770209 scopus 로고
    • Metabolism of amino acids in lens
    • Waley SG. Metabolism of amino acids in lens. Biochem J 1964; 91:576-83.
    • (1964) Biochem J , vol.91 , pp. 576-583
    • Waley, S.G.1
  • 14
    • 0023813177 scopus 로고
    • Age-related increase in concentration and aggregation of degraded polypeptides in human lenses
    • Srivastava OP. Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Exp Eye Res 1988; 47:525-43.
    • (1988) Exp Eye Res , vol.47 , pp. 525-543
    • Srivastava, O.P.1
  • 16
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by HPLC and mass spectrometry
    • Ma Z, Hanson SR, Lampi KJ, David LL, Smith DL, Smith JB. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp Eye Res 1998; 67:21-30.
    • (1998) Exp Eye Res , vol.67 , pp. 21-30
    • Ma, Z.1    Hanson, S.R.2    Lampi, K.J.3    David, L.L.4    Smith, D.L.5    Smith, J.B.6
  • 17
    • 4043127599 scopus 로고    scopus 로고
    • Characterization of crystallin species present in water soluble-high molecular weight- and water insoluble-protein fractions of aging and cataractous human lenses
    • Harrington V, McCall S, Huynh S, Srivastava OP. Characterization of crystallin species present in water soluble-high molecular weight- and water insoluble-protein fractions of aging and cataractous human lenses. Mol Vis 2004; 10:476-89.
    • (2004) Mol Vis , vol.10 , pp. 476-489
    • Harrington, V.1    McCall, S.2    Huynh, S.3    Srivastava, O.P.4
  • 18
    • 34748888365 scopus 로고    scopus 로고
    • Proteomics of crystallin species present in water insoluble proteins of normal and cataractous human lenses
    • Harrington V, Srivastava OP, Kirk M. Proteomics of crystallin species present in water insoluble proteins of normal and cataractous human lenses. Mol Vis 2007; 13:1680-95.
    • (2007) Mol Vis , vol.13 , pp. 1680-1695
    • Harrington, V.1    Srivastava, O.P.2    Kirk, M.3
  • 20
    • 0032876386 scopus 로고    scopus 로고
    • Characterization of a sodium deoxycholate-activatable proteinase activity associated with betaA3/ A1-crystallin of human lenses
    • Srivastava OP, Srivastava K. Characterization of a sodium deoxycholate-activatable proteinase activity associated with betaA3/ A1-crystallin of human lenses. Biochim Biophys Acta 1999; 1434:33146.
    • (1999) Biochim Biophys Acta , vol.1434 , pp. 33146
    • Srivastava, O.P.1    Srivastava, K.2
  • 21
    • 0020520115 scopus 로고
    • Age-related and distributional changes in trypsin inhibitor activity of bovine lens
    • Srivastava OP, Ortwerth BJ. Age-related and distributional changes in trypsin inhibitor activity of bovine lens. Exp Eye Res 1983; 36:695-706.
    • (1983) Exp Eye Res , vol.36 , pp. 695-706
    • Srivastava, O.P.1    Ortwerth, B.J.2
  • 22
    • 0020535622 scopus 로고
    • Purification and properties of a protein from bovine lens which inhibits trypsin and two endogenous proteinases
    • Srivastava OP, Ortwerth BJ. Purification and properties of a protein from bovine lens which inhibits trypsin and two endogenous proteinases. Exp Eye Res 1983; 36:363-79.
    • (1983) Exp Eye Res , vol.36 , pp. 363-379
    • Srivastava, O.P.1    Ortwerth, B.J.2
  • 23
    • 0024585808 scopus 로고
    • The effect of aging and cataract formation on the trypsin inhibitor activity of human lens
    • Srivastava OP, Ortwerth BJ. The effect of aging and cataract formation on the trypsin inhibitor activity of human lens. Exp Eye Res 1989; 48:25-36.
    • (1989) Exp Eye Res , vol.48 , pp. 25-36
    • Srivastava, O.P.1    Ortwerth, B.J.2
  • 25
    • 0020055879 scopus 로고
    • Activation of a trypsin-like proteinase from bovine lens alpha crystallin
    • Tse SS, Ortwerth BJ. Activation of a trypsin-like proteinase from bovine lens alpha crystallin. Exp Eye Res 1982; 34:659-74.
    • (1982) Exp Eye Res , vol.34 , pp. 659-674
    • Tse, S.S.1    Ortwerth, B.J.2
  • 26
    • 0026527490 scopus 로고
    • Characterization of elastase inhibitor properties of alpha crystallin and water insoluble fraction from bovine lens
    • Ortwerth BJ, Oleson PR. Characterization of elastase inhibitor properties of alpha crystallin and water insoluble fraction from bovine lens. Exp Eye Res 1992; 54:103-11.
    • (1992) Exp Eye Res , vol.54 , pp. 103-111
    • Ortwerth, B.J.1    Oleson, P.R.2
  • 27
    • 0019516739 scopus 로고
    • Activation of proteinases with trypsin-like specificity from bovine and human lenses
    • Tse SS, Ortwerth BJ. Activation of proteinases with trypsin-like specificity from bovine and human lenses. Exp Eye Res 1981; 32:605-15.
    • (1981) Exp Eye Res , vol.32 , pp. 605-615
    • Tse, S.S.1    Ortwerth, B.J.2
  • 28
    • 0036978853 scopus 로고    scopus 로고
    • Comparison of ultraviolet induced photo-kinetics for lens-derived and recombinant β-crystaillins
    • Ostrovsky MA, Sergeev YV, Atkinson DB, Soustov LV, Hejtmancik JF. Comparison of ultraviolet induced photo-kinetics for lens-derived and recombinant β-crystaillins. Mol Vis 2002; 8:72-8.
    • (2002) Mol Vis , vol.8 , pp. 72-78
    • Ostrovsky, M.A.1    Sergeev, Y.V.2    Atkinson, D.B.3    Soustov, L.V.4    Hejtmancik, J.F.5
  • 29
    • 0029664615 scopus 로고    scopus 로고
    • The sequence of human βB1-crystallin cDNA allows mass spectrometric detection of βB1 protein missing portions of its N-terminal extension
    • David LL, Lampi KJ, Lund AL, Smith JB. The sequence of human βB1-crystallin cDNA allows mass spectrometric detection of βB1 protein missing portions of its N-terminal extension. J Biol Chem 1996; 271:4273-9.
    • (1996) J Biol Chem , vol.271 , pp. 4273-4279
    • David, L.L.1    Lampi, K.J.2    Lund, A.L.3    Smith, J.B.4
  • 30
    • 0030614501 scopus 로고    scopus 로고
    • Sequence analysis of βA3, βB3 and βA4 crystallins completes the identification of the major proteins in young human lens
    • Lampi KJ, Ma Z, Shih M, Shearer TR, Smith JB, Smith DL, David LL. Sequence analysis of βA3, βB3 and βA4 crystallins completes the identification of the major proteins in young human lens. J Biol Chem 1997; 272:2268-75.
    • (1997) J Biol Chem , vol.272 , pp. 2268-2275
    • Lampi, K.J.1    Ma, Z.2    Shih, M.3    Shearer, T.R.4    Smith, J.B.5    Smith, D.L.6    David, L.L.7
  • 31
    • 33747493858 scopus 로고    scopus 로고
    • Truncation of motifs III and IV in human lens βA3-crysatllin destabilizes the structure
    • Gupta R, Srivastava K, Srivastava OP. Truncation of motifs III and IV in human lens βA3-crysatllin destabilizes the structure. Biochemistry 2006; 45:9964-78.
    • (2006) Biochemistry , vol.45 , pp. 9964-9978
    • Gupta, R.1    Srivastava, K.2    Srivastava, O.P.3
  • 32
    • 1642524490 scopus 로고    scopus 로고
    • Characterization of covalent multimers of crystallins in aging human lenses
    • Srivastava OP, Kirk MC, Srivastava K. Characterization of covalent multimers of crystallins in aging human lenses. J Biol Chem 2004; 279:10901-9.
    • (2004) J Biol Chem , vol.279 , pp. 10901-10909
    • Srivastava, O.P.1    Kirk, M.C.2    Srivastava, K.3
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of number of alpha-helical and beta strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N, Venyaminov SY, Woody RW. Estimation of number of alpha-helical and beta strand segments in proteins using circular dichroism spectroscopy. Protein Sci 1999; 8:370-80.
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 36
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Stahelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76:4350-4.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Stahelin, T.2    Gordon, J.3
  • 37
    • 0029083170 scopus 로고
    • Conversion from oligomers to tetramers enhances autophosphorylation by lens alpha A-crystallin. Specificity between alpha A-and alpha B-crystallin subunits
    • Kantorow M, Horwitz J, van Boekel MA, deJong WW, Piatigorsky J. Conversion from oligomers to tetramers enhances autophosphorylation by lens alpha A-crystallin. Specificity between alpha A-and alpha B-crystallin subunits. J Biol Chem 1995; 270:17215-20.
    • (1995) J Biol Chem , vol.270 , pp. 17215-17220
    • Kantorow, M.1    Horwitz, J.2    van Boekel, M.A.3    deJong, W.W.4    Piatigorsky, J.5
  • 39
    • 0036974373 scopus 로고    scopus 로고
    • Factors influencing α-crystallin association with phospholipids Vesicles
    • Cobb BA, Petrash JM. Factors influencing α-crystallin association with phospholipids Vesicles. Mol Vis 2002; 8:85-93.
    • (2002) Mol Vis , vol.8 , pp. 85-93
    • Cobb, B.A.1    Petrash, J.M.2
  • 40
    • 0034009392 scopus 로고    scopus 로고
    • Characterization of alpha-crystallin-plasma membrane binding
    • Cobb BA, Petrash JM. Characterization of alpha-crystallin-plasma membrane binding. J Biol Chem 2000; 275:6664-72.
    • (2000) J Biol Chem , vol.275 , pp. 6664-6672
    • Cobb, B.A.1    Petrash, J.M.2
  • 42
    • 0032535896 scopus 로고    scopus 로고
    • Studies on the binding of α-crystallin to recombinant prochymosins and chymosin
    • Chitpinityol S, Goode D, Crabbe JC. Studies on the binding of α-crystallin to recombinant prochymosins and chymosin. Mol Vis 1998; 4:1.
    • (1998) Mol Vis , vol.4 , pp. 1
    • Chitpinityol, S.1    Goode, D.2    Crabbe, J.C.3
  • 43
    • 52049097263 scopus 로고    scopus 로고
    • Multi-crystallin complexes exist in the water-soluble high molecular weight protein fractions of aging normal and cataractous human lenses
    • Srivastava K, Chaves JM, Srivastava OP, Kirk M. Multi-crystallin complexes exist in the water-soluble high molecular weight protein fractions of aging normal and cataractous human lenses. Exp Eye Res 2008; 87:356-66.
    • (2008) Exp Eye Res , vol.87 , pp. 356-366
    • Srivastava, K.1    Chaves, J.M.2    Srivastava, O.P.3    Kirk, M.4
  • 44
    • 11144247762 scopus 로고    scopus 로고
    • Lapko VN, Cerny RL, Smith DL. SMITH JB, Modifications of human βA1/ Α3-crystallins include S-methylation, glutathiolation, and truncation. Protein Sci 2005; 14:45-54,
    • Lapko VN, Cerny RL, Smith DL. SMITH JB, Modifications of human βA1/ Α3-crystallins include S-methylation, glutathiolation, and truncation. Protein Sci 2005; 14:45-54,
  • 45
    • 0032587683 scopus 로고    scopus 로고
    • Truncation of βA3/A1-crystallin during aging of the bovine lens: Possible implications for lens optical quality
    • Werten PJL, Vos E, De Jong WW. Truncation of βA3/A1-crystallin during aging of the bovine lens: possible implications for lens optical quality. Exp Eye Res 1999; 68:99-103.
    • (1999) Exp Eye Res , vol.68 , pp. 99-103
    • Werten, P.J.L.1    Vos, E.2    De Jong, W.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.