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Volumn 76, Issue 4, 1998, Pages 665-671

Characterization of a novel group of basic small heat shock proteins in Xenopus laevis A6 kidney epithelial cells

Author keywords

Basic small heat shock proteins; Heat shock protein; Herbimycin A; hsp30; NEPHGE; Sodium arsenite; Xenopus laevis

Indexed keywords

ARSENITE SODIUM; DACTINOMYCIN; HERBIMYCIN A;

EID: 0032460390     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o98-076     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 0027225560 scopus 로고
    • Expression of endogenous and microinjected hsp 30 genes in early Xenopus laevis embryos
    • Ali, A., Krone, P.H., and Heikkila, J.J. 1993. Expression of endogenous and microinjected hsp 30 genes in early Xenopus laevis embryos. Dev. Genet. 14: 42-50.
    • (1993) Dev. Genet. , vol.14 , pp. 42-50
    • Ali, A.1    Krone, P.H.2    Heikkila, J.J.3
  • 2
    • 0002241311 scopus 로고
    • Expression and function of the low-molecular-weight heat shock proteins
    • Edited by R.I. Morimoto, A. Tissieres, and C. Georgopoulos. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
    • Arrigo, A.-P., and Landry, J. 1994. Expression and function of the low-molecular-weight heat shock proteins. In The biology of heat shock proteins and molecular chaperones. Edited by R.I. Morimoto, A. Tissieres, and C. Georgopoulos. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. pp. 335-373.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.-P.1    Landry, J.2
  • 3
    • 0026271750 scopus 로고
    • Expression of heat shock proteins during development in Drosophila
    • Edited by L. Hightower and L. Nover. Springer-Verlag, Berlin
    • Arrigo, A.-P., and Tanguay, R. M. 1991. Expression of heat shock proteins during development in Drosophila. In Heat shock and development. Edited by L. Hightower and L. Nover. Springer-Verlag, Berlin, pp. 106-119.
    • (1991) Heat Shock and Development , pp. 106-119
    • Arrigo, A.-P.1    Tanguay, R.M.2
  • 5
    • 0021436060 scopus 로고
    • Developmental control of the heat shock response in Xenopus
    • Bienz, M. 1984a. Developmental control of the heat shock response in Xenopus. Proc. Natl. Acad. Sci. U.S.A. 81: 3138-3142.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3138-3142
    • Bienz, M.1
  • 6
    • 0021526790 scopus 로고
    • Xenopus hsp70 genes are constitutively expressed in injected oocytes
    • Bienz, M. 1984b. Xenopus hsp70 genes are constitutively expressed in injected oocytes. EMBO J. 3: 2477-2483.
    • (1984) EMBO J. , vol.3 , pp. 2477-2483
    • Bienz, M.1
  • 7
    • 0028873849 scopus 로고
    • Alpha-crystallins, versatile stress-proteins
    • Boelens, W., and de Jong, W. 1995. Alpha-crystallins, versatile stress-proteins. Mol. Biol. Rep. 21: 75-78.
    • (1995) Mol. Biol. Rep. , vol.21 , pp. 75-78
    • Boelens, W.1    De Jong, W.2
  • 8
    • 0031328320 scopus 로고    scopus 로고
    • Effect of herbimycin A on hsp30 and hsp70 heat shock protein gene expression in Xenopus cultured cells
    • Briant, N., Ohan, N., and Heikkila, J.J. 1997. Effect of herbimycin A on hsp30 and hsp70 heat shock protein gene expression in Xenopus cultured cells. Biochem. Cell Biol. 75: 777-782.
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 777-782
    • Briant, N.1    Ohan, N.2    Heikkila, J.J.3
  • 9
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J., Przbyla, A., MacDonald, R., and Rutter, W. 1979. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry, 18: 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.1    Przbyla, A.2    MacDonald, R.3    Rutter, W.4
  • 10
    • 0023792172 scopus 로고
    • Heat shock gene expression in Xenopus laevis A6 cells in response to heat shock and sodium arsenite treatments
    • Darasch, S., Mosser, D.D., Bols, N.C., and Heikkila, J.J. 1988. Heat shock gene expression in Xenopus laevis A6 cells in response to heat shock and sodium arsenite treatments. Biochem. Cell Biol. 66: 862-868.
    • (1988) Biochem. Cell Biol. , vol.66 , pp. 862-868
    • Darasch, S.1    Mosser, D.D.2    Bols, N.C.3    Heikkila, J.J.4
  • 11
    • 0027472047 scopus 로고
    • Evolution of the alpha-crystallin/small heat-shock protein family
    • De Jong, W., Leunissen, J., and Voorter, C. 1993. Evolution of the alpha-crystallin/small heat-shock protein family. Mol. Biol. Evol. 10: 103-126.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 103-126
    • De Jong, W.1    Leunissen, J.2    Voorter, C.3
  • 14
    • 0027158545 scopus 로고
    • Structure and organization of a murine gene encoding small heat-shock protein hsp25
    • Gaestel, M., Gotthardt, R., and Muller, T. 1993. Structure and organization of a murine gene encoding small heat-shock protein hsp25. Gene, 128: 279-283.
    • (1993) Gene , vol.128 , pp. 279-283
    • Gaestel, M.1    Gotthardt, R.2    Muller, T.3
  • 16
    • 0028847062 scopus 로고
    • Short circuiting stress protein expression via a tyrosine kinase inhibitor, herbimycin A
    • Hedge, R.S., Zuo, Z., Voellmy, R., and Welch, W.J. 1995. Short circuiting stress protein expression via a tyrosine kinase inhibitor, herbimycin A. J. Cell. Physiol. 165: 186-200.
    • (1995) J. Cell. Physiol. , vol.165 , pp. 186-200
    • Hedge, R.S.1    Zuo, Z.2    Voellmy, R.3    Welch, W.J.4
  • 17
    • 0020440738 scopus 로고
    • Expression of a set of fish genes following heat or metal ion exposure
    • Heikkila, J.J., Schultz, G.A., Iatrou, K., and Gedamu. L. 1982. Expression of a set of fish genes following heat or metal ion exposure. J. Biol. Chem. 257: 12 000-12 005.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12000-12005
    • Heikkila, J.J.1    Schultz, G.A.2    Iatrou, K.3    Gedamu, L.4
  • 18
    • 0023278120 scopus 로고
    • Heat and sodium arsenite act synergistically on heat shock gene expression in Xenopus laevis A6 cells
    • Heikkila, J.J., Darasch, S., Mosser, D.D., and Bols, N. 1987a. Heat and sodium arsenite act synergistically on heat shock gene expression in Xenopus laevis A6 cells. Biochem. Cell Biol. 65: 310-316.
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 310-316
    • Heikkila, J.J.1    Darasch, S.2    Mosser, D.D.3    Bols, N.4
  • 19
    • 0023243914 scopus 로고
    • Examination of heat shock protein mRNA accumulation in early Xenopus laevis embryos
    • Heikkila, J.J., Ovsenek, N., and Krone, P. 1987b. Examination of heat shock protein mRNA accumulation in early Xenopus laevis embryos. Biochem. Cell Biol. 65: 87-94.
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 87-94
    • Heikkila, J.J.1    Ovsenek, N.2    Krone, P.3
  • 20
    • 0030766710 scopus 로고    scopus 로고
    • Heat shock protein gene expression during Xenopus development
    • Heikkila, J.J., Ohan, N., Tam, Y., and Ali, A. 1997. Heat shock protein gene expression during Xenopus development. Cell. Mol. Life Sci. 53: 114-121.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 114-121
    • Heikkila, J.J.1    Ohan, N.2    Tam, Y.3    Ali, A.4
  • 21
    • 0026081094 scopus 로고
    • Studies of the small heat shock proteins of Caenorhabditis elegans using anti-peptide antibodies
    • Hockertz, M.K., Clark-Lewis, I., and Candido, E.P.M. 1991. Studies of the small heat shock proteins of Caenorhabditis elegans using anti-peptide antibodies. FEBS Lett. 280: 375-378.
    • (1991) FEBS Lett. , vol.280 , pp. 375-378
    • Hockertz, M.K.1    Clark-Lewis, I.2    Candido, E.P.M.3
  • 22
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small hsps as molecular chaperones
    • Jakob, U., and Buchner, J. 1994. Assisting spontaneity: the role of Hsp90 and small hsps as molecular chaperones. Trends Biochem. Sci. 19: 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 23
    • 0025877859 scopus 로고
    • Tissue distribution and developmental profiles of immunoreactive alphaB crystallin in the rat determined with a sensitive immunoassay system
    • Kato, K.H., Shinohara, H., Kurobe, N., Inaguma, Y., Shimizu, K., and Ohshima, K. 1991. Tissue distribution and developmental profiles of immunoreactive alphaB crystallin in the rat determined with a sensitive immunoassay system. Biochim. Biophys. Acta, 1074: 201-208.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 201-208
    • Kato, K.H.1    Shinohara, H.2    Kurobe, N.3    Inaguma, Y.4    Shimizu, K.5    Ohshima, K.6
  • 24
    • 0027495153 scopus 로고
    • Coinduction of two low-molecular-weight stress proteins, alphaB crystallin and hsp28, by heat or arsenite stress in human glioma cells
    • Kato, K.H., Goto, S., Hasegawa, K., and Inaguma, Y. 1993a. Coinduction of two low-molecular-weight stress proteins, alphaB crystallin and hsp28, by heat or arsenite stress in human glioma cells. J. Biochem. (Tokyo), 114: 640-647.
    • (1993) J. Biochem. (Tokyo) , vol.114 , pp. 640-647
    • Kato, K.H.1    Goto, S.2    Hasegawa, K.3    Inaguma, Y.4
  • 25
    • 0027392709 scopus 로고
    • Responses to heat shock of alphaB crystallin and hsp28 in U373 MG human glioma cells
    • Kato, K.H., Goto, S., Hasegawa, K., Shinohara, H., and Inaguma, Y. 1993b. Responses to heat shock of alphaB crystallin and hsp28 in U373 MG human glioma cells. Biochim. Biophys. Acta, 1175: 257-262.
    • (1993) Biochim. Biophys. Acta , vol.1175 , pp. 257-262
    • Kato, K.H.1    Goto, S.2    Hasegawa, K.3    Shinohara, H.4    Inaguma, Y.5
  • 26
    • 0023911049 scopus 로고
    • Analysis of hsp 30, hsp 70, and ubiquitin gene expression in Xenopus laevis tadpoles
    • Krone, P.H., and Heikkila, J.J. 1988. Analysis of hsp 30, hsp 70, and ubiquitin gene expression in Xenopus laevis tadpoles. Development (Cambridge), 103: 59-67.
    • (1988) Development (Cambridge) , vol.103 , pp. 59-67
    • Krone, P.H.1    Heikkila, J.J.2
  • 27
    • 0024411412 scopus 로고
    • Expression of microinjected hsp70/CAT and hsp30/CAT chimeric genes in developing Xenopus laevis embryos
    • Krone, P.H., and Heikkila, J.J. 1989. Expression of microinjected hsp70/CAT and hsp30/CAT chimeric genes in developing Xenopus laevis embryos. Development (Cambridge), 106: 271-281.
    • (1989) Development (Cambridge) , vol.106 , pp. 271-281
    • Krone, P.H.1    Heikkila, J.J.2
  • 28
    • 0026537572 scopus 로고
    • Comparison of the regulatory regions of the Xenopus laevis small heat-shock protein encoding gene family
    • Krone, P.H., Snow, A., Ali, A., Pasternak, J.J., and Heikkila, J.J. 1992. Comparison of the regulatory regions of the Xenopus laevis small heat-shock protein encoding gene family. Gene, 110: 159-166.
    • (1992) Gene , vol.110 , pp. 159-166
    • Krone, P.H.1    Snow, A.2    Ali, A.3    Pasternak, J.J.4    Heikkila, J.J.5
  • 29
    • 0028036390 scopus 로고
    • Purification and immunological characterization of color carp (Cyprinus carpio) fibroblast heat shock proteins
    • Ku, C.C., Lu, C.H., Kou, G.H., and Chen, S.N. 1994. Purification and immunological characterization of color carp (Cyprinus carpio) fibroblast heat shock proteins. Comp. Biochem. Physiol. B, 107: 147-159.
    • (1994) Comp. Biochem. Physiol. B , vol.107 , pp. 147-159
    • Ku, C.C.1    Lu, C.H.2    Kou, G.H.3    Chen, S.N.4
  • 30
    • 0022462428 scopus 로고
    • An ancient developmental induction: Heat-shock protein induced in sporulation and oogenesis
    • Kurtz, S., Rossi, J., Petko, L., and Lindquist, S. 1986. An ancient developmental induction: heat-shock protein induced in sporulation and oogenesis. Science (Washington, D.C.), 231: 1154-1157.
    • (1986) Science (Washington, D.C.) , vol.231 , pp. 1154-1157
    • Kurtz, S.1    Rossi, J.2    Petko, L.3    Lindquist, S.4
  • 31
    • 0027325351 scopus 로고
    • Hsp 23 and hsp 26 exhibit distinct spatial and temporal patterns of constitutive expression in Drosophila adults
    • Marin, R., Valet, J.P., and Tanguay, R.M. 1993. Hsp 23 and hsp 26 exhibit distinct spatial and temporal patterns of constitutive expression in Drosophila adults. Dev. Genet. 14: 69-77.
    • (1993) Dev. Genet. , vol.14 , pp. 69-77
    • Marin, R.1    Valet, J.P.2    Tanguay, R.M.3
  • 32
    • 0030889987 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA encoding a Xenopus immunoglobulin binding protein, BiP (Grp78)
    • Miskovic, D., Luisa, S.-C., Ohan, N., Flajnik, M.F., and Heikkila, J.J. 1997. Isolation and characterization of a cDNA encoding a Xenopus immunoglobulin binding protein, BiP (Grp78). Comp. Biochem. Physiol. B, 116: 227-234.
    • (1997) Comp. Biochem. Physiol. B , vol.116 , pp. 227-234
    • Miskovic, D.1    Luisa, S.-C.2    Ohan, N.3    Flajnik, M.F.4    Heikkila, J.J.5
  • 33
    • 0021231377 scopus 로고
    • Cell type-specific activation of actin genes in the early amphibian embryo
    • Mohun, T.J., Brennan, S., Dathan, N., Fairman, S., and Gurdon, J.B. 1983. Cell type-specific activation of actin genes in the early amphibian embryo. Nature (London), 311: 716-721.
    • (1983) Nature (London) , vol.311 , pp. 716-721
    • Mohun, T.J.1    Brennan, S.2    Dathan, N.3    Fairman, S.4    Gurdon, J.B.5
  • 35
    • 0025744556 scopus 로고
    • Induction of Hsp72/73 by herbimycin A, an inhibitor of transformation by tyrosine kinase oncogenes
    • Murakami, Y., Uehara, Y., Yamamoto, C., Fukazawa, H., and Mizuno, S. 1991. Induction of Hsp72/73 by herbimycin A, an inhibitor of transformation by tyrosine kinase oncogenes. Exp. Cell Res. 195: 338-344.
    • (1991) Exp. Cell Res. , vol.195 , pp. 338-344
    • Murakami, Y.1    Uehara, Y.2    Yamamoto, C.3    Fukazawa, H.4    Mizuno, S.5
  • 36
    • 0030929973 scopus 로고    scopus 로고
    • Low molecular weight heat shock proteins in the desert topminnow Poeciliopsis lucida: Homologs of human hsp27 and Xenopus hsp30
    • Norris, C.E., Brown, M.A., Hickey, E., Weber, L.A., and Hightower, L.E. 1997. Low molecular weight heat shock proteins in the desert topminnow Poeciliopsis lucida: homologs of human hsp27 and Xenopus hsp30. Mol. Biol. Evol. 14: 1050-1061.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 1050-1061
    • Norris, C.E.1    Brown, M.A.2    Hickey, E.3    Weber, L.A.4    Hightower, L.E.5
  • 37
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 38
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell, P.Z, Goodman, H., and O'Farrell, P.H. 1977. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell, 12: 1133-1142.
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrell, P.Z.1    Goodman, H.2    O'Farrell, P.H.3
  • 39
    • 0029052774 scopus 로고
    • Involvement of differential gene expression and mRNA stability in the developmental regulation of the hsp30 gene family in heat-shocked Xenopus laevis embryos
    • Ohan, N., and Heikkila, J.J. 1995. Involvement of differential gene expression and mRNA stability in the developmental regulation of the hsp30 gene family in heat-shocked Xenopus laevis embryos. Dev. Genet. 17: 176-184.
    • (1995) Dev. Genet. , vol.17 , pp. 176-184
    • Ohan, N.1    Heikkila, J.J.2
  • 40
    • 0031895813 scopus 로고    scopus 로고
    • Heat shock-induced assembly of hsp30 family members into high molecular weight aggregates in Xenopus cultured cells
    • Ohan, N., Tam, Y., and Heikkila, J.J. 1998. Heat shock-induced assembly of hsp30 family members into high molecular weight aggregates in Xenopus cultured cells. Comp. Biochem. Physiol. B, 119: 381-389.
    • (1998) Comp. Biochem. Physiol. B , vol.119 , pp. 381-389
    • Ohan, N.1    Tam, Y.2    Heikkila, J.J.3
  • 41
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D.A., and Lindquist, S. 1993. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27: 437-496.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 43
    • 0028254544 scopus 로고
    • Expression of the alpha-crystallin/small heat-shock protein/ molecular chaperone genes in the lens and other tissues
    • Sax, C., and Piatigorsky, J. 1994. Expression of the alpha-crystallin/small heat-shock protein/ molecular chaperone genes in the lens and other tissues. Adv. Enzymol. Relat. Areas Mol. Biol. 69: 155-201.
    • (1994) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.69 , pp. 155-201
    • Sax, C.1    Piatigorsky, J.2
  • 44
    • 0020013885 scopus 로고
    • Developmentally regulated transcription from Drosophila melanogaster chromosomal site 67B
    • Sirotkin, K., and Davidson, N. 1982. Developmentally regulated transcription from Drosophila melanogaster chromosomal site 67B. Dev. Biol. 89: 196-210.
    • (1982) Dev. Biol. , vol.89 , pp. 196-210
    • Sirotkin, K.1    Davidson, N.2
  • 45
    • 0029558353 scopus 로고
    • Identification of members of the hsp30 small heat shock protein family and characterization of their developmental regulation in heat shocked Xenopus laevis embryos
    • Tam, Y., and Heikkila, J.J. 1995. Identification of members of the hsp30 small heat shock protein family and characterization of their developmental regulation in heat shocked Xenopus laevis embryos. Dev. Genet. 17: 331-339.
    • (1995) Dev. Genet. , vol.17 , pp. 331-339
    • Tam, Y.1    Heikkila, J.J.2
  • 46
    • 0018734032 scopus 로고
    • Heat-shock induced proteins present in the cell nucleus of Chironomous tentans salivary gland
    • Vincent, M., and Tanguay, R.M 1979. Heat-shock induced proteins present in the cell nucleus of Chironomous tentans salivary gland. Nature (London), 281: 501-503.
    • (1979) Nature (London) , vol.281 , pp. 501-503
    • Vincent, M.1    Tanguay, R.M.2
  • 47
  • 48
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters, E., Lee, G., and Vierling, E. 1996. Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Biol. 47: 325-338.
    • (1996) J. Exp. Biol. , vol.47 , pp. 325-338
    • Waters, E.1    Lee, G.2    Vierling, E.3
  • 49
    • 0027925653 scopus 로고
    • Heat shock proteins functioning as molecular chaperones: Their roles in normal and stressed cells
    • Welch, W.J. 1993. Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells. Philos. Trans. R. Soc. London Ser. B, 339: 327-333.
    • (1993) Philos. Trans. R. Soc. London Ser. B , vol.339 , pp. 327-333
    • Welch, W.J.1
  • 50
    • 0028097732 scopus 로고
    • Variation in heat shock proteins among species of desert fishes (Poeciliidae, Poeciliopsis)
    • White, C.N., Hightower, L.E., and Schultz, J.R. 1994. Variation in heat shock proteins among species of desert fishes (Poeciliidae, Poeciliopsis). Mol. Biol. Evol. 11: 106-119.
    • (1994) Mol. Biol. Evol. , vol.11 , pp. 106-119
    • White, C.N.1    Hightower, L.E.2    Schultz, J.R.3
  • 51
    • 0024369102 scopus 로고
    • Induction of glucose-regulated proteins in Xenopus laevis A6 cells
    • Winning, R.S., Heikkila, J.J., and Bols, N.C. 1989. Induction of glucose-regulated proteins in Xenopus laevis A6 cells. J. Cell. Physiol. 140: 239-245.
    • (1989) J. Cell. Physiol. , vol.140 , pp. 239-245
    • Winning, R.S.1    Heikkila, J.J.2    Bols, N.C.3


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