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Volumn 67, Issue 3, 1998, Pages 301-312

Deamidation and disulfide bonding in human lens γ-crystallins

Author keywords

Deamidation; Disulfide bonding; Human lens; Mass spectrometry; crystallins

Indexed keywords

COMPLEMENTARY DNA; GAMMA CRYSTALLIN; LENS PROTEIN;

EID: 0032170644     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1998.0530     Document Type: Article
Times cited : (81)

References (65)
  • 1
    • 0010352954 scopus 로고
    • Characterization of low molecular mass γ-crystallin fragments from human lenses
    • Abbasi A., Smith D. L., Smith J. B. Characterization of low molecular mass γ-crystallin fragments from human lenses. Exp. Eye Res. 1988.
    • (1988) Exp. Eye Res.
    • Abbasi, A.1    Smith, D.L.2    Smith, J.B.3
  • 2
    • 0030893023 scopus 로고    scopus 로고
    • Size of human lens β-crystallin aggregates are distinguished byN
    • Ajaz M. S., Ma Z., Smith D. L., Smith J. B. Size of human lens β-crystallin aggregates are distinguished byN. J. Biol. Chem. 272:1997;11250-11255.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11250-11255
    • Ajaz, M.S.1    Ma, Z.2    Smith, D.L.3    Smith, J.B.4
  • 4
    • 0029770039 scopus 로고    scopus 로고
    • Cloning, expression, and chaperone-like activity of human αA-crystallin
    • Andley U. P., Mathur S., Griest T. A., Petrash J. M. Cloning, expression, and chaperone-like activity of human αA-crystallin. J. Biol. Chem. 271:1996;31973-31980.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31973-31980
    • Andley, U.P.1    Mathur, S.2    Griest, T.A.3    Petrash, J.M.4
  • 7
    • 0023888625 scopus 로고
    • Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin
    • Chiesa R., Gawinowicz-Kolks M. A., Kleiman N. J., Spector A. Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin. Exp. Eye Res. 46:1988;199-208.
    • (1988) Exp. Eye Res. , vol.46 , pp. 199-208
    • Chiesa, R.1    Gawinowicz-Kolks, M.A.2    Kleiman, N.J.3    Spector, A.4
  • 10
    • 0029664615 scopus 로고    scopus 로고
    • The sequence of human βB1-crystallin cDNA allows mass spectrometric detection of βB1 protein missing portions of itsN
    • David L. L., Lampi K. J., Lund A. L., Smith J. B. The sequence of human βB1-crystallin cDNA allows mass spectrometric detection of βB1 protein missing portions of itsN. J. Biol. Chem. 271:1996;4273-4279.
    • (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
  • 11
  • 15
    • 0015715696 scopus 로고
    • Disulphide cross-linked protein of high molecular weight in human cataractous lens
    • Harding J. J. Disulphide cross-linked protein of high molecular weight in human cataractous lens. Exp. Eye Res. 17:1973;377-383.
    • (1973) Exp. Eye Res. , vol.17 , pp. 377-383
    • Harding, J.J.1
  • 16
    • 0017129555 scopus 로고
    • Structural proteins of the mammalian lens: A review with emphasis on changes in development, aging and cataract
    • Harding J. J., Dilley K. J. Structural proteins of the mammalian lens: a review with emphasis on changes in development, aging and cataract. Exp. Eye Res. 22:1976;1-73.
    • (1976) Exp. Eye Res. , vol.22 , pp. 1-73
    • Harding, J.J.1    Dilley, K.J.2
  • 17
    • 0000145042 scopus 로고
    • The lens: Development, proteins, metabolism and cataract
    • Academic Press
    • Harding J. J., Crabbe M. J C. The lens: development, proteins, metabolism and cataract. The Eye. 1984;Academic Press. p. 207-492.
    • (1984) The Eye , pp. 207-492
    • Harding, J.J.1    Crabbe, M.J.C.2
  • 19
    • 0026667939 scopus 로고
    • Formation of hydrogen peroxide by lens proteins: Protein-derived hydrogen peroxide as a potential mechanism of oxidative insult to the lens
    • Hunt J. V., Jiang Z. Y., Wolff S. P. Formation of hydrogen peroxide by lens proteins: protein-derived hydrogen peroxide as a potential mechanism of oxidative insult to the lens. Free Radic. Biol. Med. 13:1992;319-323.
    • (1992) Free Radic. Biol. Med. , vol.13 , pp. 319-323
    • Hunt, J.V.1    Jiang, Z.Y.2    Wolff, S.P.3
  • 21
    • 0027485396 scopus 로고
    • Glutathione levels of the human crystalline lens in aging and its antioxidant effect against the oxidation of lens proteins
    • Kamei A. Glutathione levels of the human crystalline lens in aging and its antioxidant effect against the oxidation of lens proteins. Biol. Pharm. Bull. 16:1993;870-875.
    • (1993) Biol. Pharm. Bull. , vol.16 , pp. 870-875
    • Kamei, A.1
  • 24
    • 0030614501 scopus 로고    scopus 로고
    • Sequence analysis of βB3, βA1, βA3 and βA4-crystallins completes the identification of the major proteins of the young human lens
    • Lampi K. J., Ma Z., Shih M., Shearer T. R., Smith J. B., Smith D. L., David L. L. Sequence analysis of βB3, βA1, βA3 and βA4-crystallins completes the identification of the major proteins of the young human lens. J. Biol. Chem. 272:1997;2268-2275.
    • (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
  • 25
    • 0025685391 scopus 로고
    • Mechanisms of photochemically produced turbidity in lens protein solutions
    • Li D.-Y., Borkman R. F., Wang R.-H., Dillon J. Mechanisms of photochemically produced turbidity in lens protein solutions. Exp. Eye Res. 51:1990;663-669.
    • (1990) Exp. Eye Res. , vol.51 , pp. 663-669
    • Li, D.-Y.1    Borkman, R.F.2    Wang, R.-H.3    Dillon, J.4
  • 26
    • 0031745913 scopus 로고    scopus 로고
    • In vivo acetylation identified at Lysine 70 of human lens αA-crystallin
    • Lin P. P., Barry R. C., Smith D. L., Smith J. B. In vivo acetylation identified at Lysine 70 of human lens αA-crystallin. Protein Sci. 7 (6):1998;1451-1457.
    • (1998) Protein Sci. , vol.76 , pp. 1451-1457
    • Lin, P.P.1    Barry, R.C.2    Smith, D.L.3    Smith, J.B.4
  • 27
    • 0030702940 scopus 로고    scopus 로고
    • In vivo modification of the C-terminal lysine of human lens αB-crystallin
    • Lin P., Smith D. L., Smith J. B. In vivo modification of the C-terminal lysine of human lens αB-crystallin. Exp. Eye Res. 65:1997;673-680.
    • (1997) Exp. Eye Res. , vol.65 , pp. 673-680
    • Lin, P.1    Smith, D.L.2    Smith, J.B.3
  • 28
    • 0027087293 scopus 로고
    • Protein-thiol mixed disulfides in human lens
    • Lou M. F., Dickerson J. E., Jr. Protein-thiol mixed disulfides in human lens. Exp. Eye Res. 55:1992;889-896.
    • (1992) Exp. Eye Res. , vol.55 , pp. 889-896
    • Lou, M.F.1    Dickerson J.E., Jr.2
  • 29
    • 0025353464 scopus 로고
    • The role of protein-thiol mixed disulfides in cataractogenesis
    • Lou M. F., Dickerson J. E., Jr, Garadi R. The role of protein-thiol mixed disulfides in cataractogenesis. Exp. Eye Res. 50:1990;819-826.
    • (1990) Exp. Eye Res. , vol.50 , pp. 819-826
    • Lou, M.F.1    Dickerson J.E., Jr.2    Garadi, R.3
  • 30
    • 0030475908 scopus 로고    scopus 로고
    • Modifications of the water-insoluble human lens α-crystallins
    • Lund A. L., Smith J. B., Smith D. L. Modifications of the water-insoluble human lens α-crystallins. Exp. Eye Res. 63:1996;661-672.
    • (1996) Exp. Eye Res. , vol.63 , pp. 661-672
    • Lund, A.L.1    Smith, J.B.2    Smith, D.L.3
  • 31
    • 0027317391 scopus 로고
    • Nonenzymatic glycation alters protein structure and stability
    • Luthra M., Balasubramanian D. Nonenzymatic glycation alters protein structure and stability. J. Biol. Chem. 268:1993;18119-18127.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18119-18127
    • Luthra, M.1    Balasubramanian, D.2
  • 32
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by HPLC and mass spectrometry
    • Ma Z., Hanson S. R., Lampi K., David L., Smith D. L., Smith J. B. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp. Eye Res. 67 (1):1998;21-30.
    • (1998) Exp. Eye Res. , vol.671 , pp. 21-30
    • Ma, Z.1    Hanson, S.R.2    Lampi, K.3    David, L.4    Smith, D.L.5    Smith, J.B.6
  • 33
    • 0027454119 scopus 로고
    • Stability of normal and aging lens gamma crystallins
    • Mandal K., Lerman S. Stability of normal and aging lens gamma crystallins. Ophthalmic, Res. 25:1993;295-301.
    • (1993) Ophthalmic, Res. , vol.25 , pp. 295-301
    • Mandal, K.1    Lerman, S.2
  • 34
    • 0021957560 scopus 로고
    • Structural and evolutionary relationships among five members of the human γ-crystallin gene family
    • Meakin S. O., Breitman M. L., Tsui L.-C. Structural and evolutionary relationships among five members of the human γ-crystallin gene family. Mol. Cell Biol. 5:1985;1408-1414.
    • (1985) Mol. Cell Biol. , vol.5 , pp. 1408-1414
    • Meakin, S.O.1    Breitman, M.L.2    Tsui, L.-C.3
  • 35
    • 0023389564 scopus 로고
    • γ-crystallins of the human eye lens: Expression analysis of five members of the gene family
    • Meakin S. O., Du R. P., Tsui L.-C., Breitman M. L. γ-crystallins of the human eye lens: expression analysis of five members of the gene family. Mol. Cell. Biol. 7:1987;2671-2679.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2671-2679
    • Meakin, S.O.1    Du, R.P.2    Tsui, L.-C.3    Breitman, M.L.4
  • 36
    • 0028216737 scopus 로고
    • Post-translational modifications of the water soluble human lens crystallins from young adults
    • Miesbauer L. R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D. L., Smith J. B. Post-translational modifications of the water soluble human lens crystallins from young adults. J. Biol. Chem. 269:1994;12494-12502.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12494-12502
    • Miesbauer, L.R.1    Zhou, X.2    Yang, Z.3    Yang, Z.4    Sun, Y.5    Smith, D.L.6    Smith, J.B.7
  • 38
    • 0027081126 scopus 로고
    • Studies on the solubilization of the water-insoluble fraction from human lens and cataract
    • Ortwerth B. J., Olesen P. R. Studies on the solubilization of the water-insoluble fraction from human lens and cataract. Exp. Eye Res. 55:1992;777-783.
    • (1992) Exp. Eye Res. , vol.55 , pp. 777-783
    • Ortwerth, B.J.1    Olesen, P.R.2
  • 39
    • 0023656808 scopus 로고
    • Inter-and intramolecular disulfide bond formation and related structural changes in the lens proteins
    • Ozaki Y., Mizuno A., Itoh K., Iriyama K. Inter-and intramolecular disulfide bond formation and related structural changes in the lens proteins. J. Biol. Chem. 262:1987;15445-15551.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15445-15551
    • Ozaki, Y.1    Mizuno, A.2    Itoh, K.3    Iriyama, K.4
  • 40
    • 0025646639 scopus 로고
    • Effect of acetylation by aspirin on the thermodynamic stability of lens crystallins
    • Sen A. C., Chakrabarti B. Effect of acetylation by aspirin on the thermodynamic stability of lens crystallins. Exp. Eye Res. 51:1990a;701-709.
    • (1990) Exp. Eye Res. , vol.51 , pp. 701-709
    • Sen, A.C.1    Chakrabarti, B.2
  • 41
    • 0025113391 scopus 로고
    • Proximity of sulfhydryl groups in lens proteins: Excimer fluorescence of pyrene-labeled crystallins
    • Sen A. C., Chakrabarti B. Proximity of sulfhydryl groups in lens proteins: excimer fluorescence of pyrene-labeled crystallins. J. Biol. Chem. 265:1990b;14277-14284.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14277-14284
    • Sen, A.C.1    Chakrabarti, B.2
  • 42
    • 0026637369 scopus 로고
    • Ageing and changes in protein conformation in the human lens: A Raman microspectroscopic study
    • Siebinga I., Vrensen G. F. J. M., Otto K., Puppels G. J., de Mul F. F. M., Greve J. Ageing and changes in protein conformation in the human lens: a Raman microspectroscopic study. Exp. Eye Res. 54:1992;759-767.
    • (1992) Exp. Eye Res. , vol.54 , pp. 759-767
    • Siebinga, I.1    Vrensen, G.F.J.M.2    Otto, K.3    Puppels, G.J.4    De Mul, F.F.M.5    Greve, J.6
  • 45
    • 0018194985 scopus 로고
    • Disulfide-linked high molecular weight protein associated with human cataract
    • Spector A., Roy D. Disulfide-linked high molecular weight protein associated with human cataract. Proc. Natl. Acad. Sci. USA. 75:1978;3244-3248.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3244-3248
    • Spector, A.1    Roy, D.2
  • 46
    • 0023813177 scopus 로고
    • Age-related increase in concentration and aggregation of degraded polypeptides in human lenses
    • Srivastava O. M. Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Exp. Eye Res. 47:1988;525-543.
    • (1988) Exp. Eye Res. , vol.47 , pp. 525-543
    • Srivastava, O.M.1
  • 47
    • 0029994346 scopus 로고    scopus 로고
    • Characterization of three isoforms of a 9 kDa γD-crystallin fragment isolated from human lenses
    • Srivastava O. P., Srivastava K. Characterization of three isoforms of a 9 kDa γD-crystallin fragment isolated from human lenses. Exp. Eye Res. 62:1996;593-604.
    • (1996) Exp. Eye Res. , vol.62 , pp. 593-604
    • Srivastava, O.P.1    Srivastava, K.2
  • 48
    • 0026650046 scopus 로고
    • Identification of a 9 kDa γ-crystallin fragment in human lenses
    • Srivastava O. P., McEntire J. E., Srivastava K. Identification of a 9 kDa γ-crystallin fragment in human lenses. Exp. Eye Res. 54:1992;893-901.
    • (1992) Exp. Eye Res. , vol.54 , pp. 893-901
    • Srivastava, O.P.1    McEntire, J.E.2    Srivastava, K.3
  • 49
    • 0027404848 scopus 로고
    • Identification of a γs-crystallin fragment in human lenses
    • Srivastava O. P., Srivastava K., Silney C. Identification of a γs-crystallin fragment in human lenses. Exp. Eye Res. 56:1993;367-369.
    • (1993) Exp. Eye Res. , vol.56 , pp. 367-369
    • Srivastava, O.P.1    Srivastava, K.2    Silney, C.3
  • 50
    • 0027984870 scopus 로고
    • Covalent modification at the C-terminal end of a 9 kDa γD-crystallin fragment in human lenses
    • Srivastava O. P., Srivastava K., Silney C. Covalent modification at the C-terminal end of a 9 kDa γD-crystallin fragment in human lenses. Exp. Eye Res. 58:1994;595-604.
    • (1994) Exp. Eye Res. , vol.58 , pp. 595-604
    • Srivastava, O.P.1    Srivastava, K.2    Silney, C.3
  • 51
    • 0027934872 scopus 로고
    • Release of α-A sequence 158-173 correlates with a decrease in the molecular chaperone properties of native α-crystallin
    • Takemoto L. Release of α-A sequence 158-173 correlates with a decrease in the molecular chaperone properties of native α-crystallin. Exp. Eye Res. 59:1994;239-242.
    • (1994) Exp. Eye Res. , vol.59 , pp. 239-242
    • Takemoto, L.1
  • 52
    • 0029319568 scopus 로고
    • Quantitation of C-terminal modification of alpha-A crystallin during aging of the human lens
    • Takemoto L. Quantitation of C-terminal modification of alpha-A crystallin during aging of the human lens. Exp. Eye Res. 60:1995;721-724.
    • (1995) Exp. Eye Res. , vol.60 , pp. 721-724
    • Takemoto, L.1
  • 53
    • 0029992808 scopus 로고    scopus 로고
    • Differential phosphorylation of alpha-A crystallin in human lens of different age
    • Takemoto L. J. Differential phosphorylation of alpha-A crystallin in human lens of different age. Exp. Eye Res. 62:1996a;499-504.
    • (1996) Exp. Eye Res. , vol.62 , pp. 499-504
    • Takemoto, L.J.1
  • 54
    • 0030583143 scopus 로고    scopus 로고
    • Oxidation of cysteine residues from alpha-A during cataractogenesis of the human lens
    • Takemoto L. J. Oxidation of cysteine residues from alpha-A during cataractogenesis of the human lens. Biochem. Biophys. Res. Commun. 223:1996b;216-220.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 216-220
    • Takemoto, L.J.1
  • 55
    • 0031126762 scopus 로고    scopus 로고
    • Disulphide bond formation of cysteine-37 and cysteine-66 of betaB2 crystallin during cataractogenesis of the human lens
    • Takemoto L. J. Disulphide bond formation of cysteine-37 and cysteine-66 of betaB2 crystallin during cataractogenesis of the human lens. Exp. Eye Res. 64:1997;609-614.
    • (1997) Exp. Eye Res. , vol.64 , pp. 609-614
    • Takemoto, L.J.1
  • 56
    • 0026334294 scopus 로고
    • Truncation of αA-crystallin from the human lens
    • Takemoto L., Emmons T. Truncation of αA-crystallin from the human lens. Exp. Eye Res. 53:1991;811-813.
    • (1991) Exp. Eye Res. , vol.53 , pp. 811-813
    • Takemoto, L.1    Emmons, T.2
  • 59
    • 0028171466 scopus 로고
    • Dimerization of βB2-crystallin: The role of the linker peptide and theN-
    • Trinkl S., Glockshuber R., Jaenicke R. Dimerization of βB2-crystallin: the role of the linker peptide and theN-. Protein Sci. 3:1994;1392-1400.
    • (1994) Protein Sci. , vol.3 , pp. 1392-1400
    • Trinkl, S.1    Glockshuber, R.2    Jaenicke, R.3
  • 60


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.