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Volumn 154, Issue , 1997, Pages 261-268

Expression of the potential biomarker heat shock protein 70 and its regulator, the metazoan DnaJ homolog, by temperature stress in the sponge Geodia cydonium

Author keywords

DnaJ like protein; Geodia cydonium; Heat shock protein; hsp70; Sponge

Indexed keywords

ANIMALIA; EUKARYOTA; GEODIA CYDONIUM; METAZOA; PORIFERA; PROKARYOTA;

EID: 0030756234     PISSN: 01718630     EISSN: None     Source Type: Journal    
DOI: 10.3354/meps154261     Document Type: Article
Times cited : (33)

References (43)
  • 1
    • 0031585828 scopus 로고    scopus 로고
    • Immediate early response of the marine sponge Suberites domuncula to heat stress: Reduction of trehalose concentration and glutathione S-transferase activity
    • Bachinski N, Koziol C, Batel R, Labura Z, Schröder HC, Müller WEG (1997) Immediate early response of the marine sponge Suberites domuncula to heat stress: reduction of trehalose concentration and glutathione S-transferase activity. J Exp Mar Biol Ecol 210:129-141
    • (1997) J Exp Mar Biol Ecol , vol.210 , pp. 129-141
    • Bachinski, N.1    Koziol, C.2    Batel, R.3    Labura, Z.4    Schröder, H.C.5    Müller, W.E.G.6
  • 2
    • 0000061178 scopus 로고
    • Modulation of organotin-induced apoptosis by the water pollutant methyl mercury in a human lymphoblastoid tumor cell line and a marine sponge
    • Batel R, Bihari N, Rinkevich B, Dapper J, Schäcke H, Schröder HC, Müller WEG (1993) Modulation of organotin-induced apoptosis by the water pollutant methyl mercury in a human lymphoblastoid tumor cell line and a marine sponge. Mar Ecol Prog Ser 93:245-251
    • (1993) Mar Ecol Prog Ser , vol.93 , pp. 245-251
    • Batel, R.1    Bihari, N.2    Rinkevich, B.3    Dapper, J.4    Schäcke, H.5    Schröder, H.C.6    Müller, W.E.G.7
  • 3
    • 0025024265 scopus 로고
    • Discordant expression of heat shock protein mRNAs in tissues of heat-stressed rats
    • Blake M, Gershon D, Fargnoli J, Holbrook N (1990) Discordant expression of heat shock protein mRNAs in tissues of heat-stressed rats. J Biol Chem 265:15275-15279
    • (1990) J Biol Chem , vol.265 , pp. 15275-15279
    • Blake, M.1    Gershon, D.2    Fargnoli, J.3    Holbrook, N.4
  • 4
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski MS, McCormick F (1993) Proteins regulating Ras and its relatives. Nature 366:643-654
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 6
    • 0026586906 scopus 로고
    • A module of the DnaJ heat shock proteins in malaria parasites
    • Bork P, Sander C, Valencia A, Bukau B (1992) A module of the DnaJ heat shock proteins in malaria parasites. Trends Biochem Sci 17:129
    • (1992) Trends Biochem Sci , vol.17 , pp. 129
    • Bork, P.1    Sander, C.2    Valencia, A.3    Bukau, B.4
  • 7
    • 0027254809 scopus 로고
    • Induction of heat shock response leads to apoptosis in endothelial cells previously exposed to endotoxin
    • Buchman TG, Abello PA, Smith EH, Bulkley GB (1993) Induction of heat shock response leads to apoptosis in endothelial cells previously exposed to endotoxin. Am J Physiol 265:H165-H170
    • (1993) Am J Physiol , vol.265
    • Buchman, T.G.1    Abello, P.A.2    Smith, E.H.3    Bulkley, G.B.4
  • 8
    • 0028099817 scopus 로고
    • Regulation of the 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b
    • Cheetham ME, Jackson AP, Anderton BH (1994) Regulation of the 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b. Europ J Biochem 226:99-107
    • (1994) Europ J Biochem , vol.226 , pp. 99-107
    • Cheetham, M.E.1    Jackson, A.P.2    Anderton, B.H.3
  • 9
    • 0028593565 scopus 로고
    • Nondestructive biomarkers in ecotoxicology
    • Fossi MC (1994) Nondestructive biomarkers in ecotoxicology. Environ Health Perspect 102(Suppl 12):49-54
    • (1994) Environ Health Perspect , vol.102 , Issue.12 SUPPL. , pp. 49-54
    • Fossi, M.C.1
  • 10
    • 0000757557 scopus 로고
    • Properties of the heat shock proteins of Escherichia coil and the autoregulation of the heat shock response
    • Morimoto RI, Tissères A, Georgopoulos C (eds) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Georgopoulos C, Liberek K, Zylicz M, Ang D (1994) Properties of the heat shock proteins of Escherichia coil and the autoregulation of the heat shock response. In: Morimoto RI, Tissères A, Georgopoulos C (eds) The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, p 209-249
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 209-249
    • Georgopoulos, C.1    Liberek, K.2    Zylicz, M.3    Ang, D.4
  • 11
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J (1992) Protein folding in the cell. Nature 355:33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 12
    • 0024121547 scopus 로고
    • cDNA cloning of the immunoglobulin heavy-chain binding protein
    • Haas IG, Meo T (1988) cDNA cloning of the immunoglobulin heavy-chain binding protein. Proc Natl Acad Sci USA 85: 2250-2254
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2250-2254
    • Haas, I.G.1    Meo, T.2
  • 13
    • 0029739708 scopus 로고    scopus 로고
    • Cloning of the heat-inducible biomarker, the cDNA encoding the 70-kDa heat shock protein, from the marine sponge Geodia cydonium: Response to natural stressors
    • Koziol C, Wagner-Hülsmann C, Cetkovic H, Gamulin V, Kruse M, Pancer Z, Schäcke H, Müller WEG (1996) Cloning of the heat-inducible biomarker, the cDNA encoding the 70-kDa heat shock protein, from the marine sponge Geodia cydonium: response to natural stressors. Mar Ecol Prog Ser 136:153-161
    • (1996) Mar Ecol Prog Ser , vol.136 , pp. 153-161
    • Koziol, C.1    Wagner-Hülsmann, C.2    Cetkovic, H.3    Gamulin, V.4    Kruse, M.5    Pancer, Z.6    Schäcke, H.7    Müller, W.E.G.8
  • 14
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along with the pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU (1992) Successive action of DnaK, DnaJ and GroEL along with the pathway of chaperone-mediated protein folding. Nature 356:683-689
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 15
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci USA 88:2874-2878
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 17
    • 0029741321 scopus 로고    scopus 로고
    • Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp70
    • Minami Y, Hohfeld J, Ohtsuka K, Hartl FU (1996) Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp70. J Biol Chem 271: 19617-19624
    • (1996) J Biol Chem , vol.271 , pp. 19617-19624
    • Minami, Y.1    Hohfeld, J.2    Ohtsuka, K.3    Hartl, F.U.4
  • 20
    • 0029092813 scopus 로고
    • Molecular phylogeny of metazoa (animals): Monophyletic origin
    • Müller WEG (1995) Molecular phylogeny of metazoa (animals): monophyletic origin. Naturwissenschaften 82:321-329
    • (1995) Naturwissenschaften , vol.82 , pp. 321-329
    • Müller, W.E.G.1
  • 21
    • 0001959655 scopus 로고    scopus 로고
    • Sponge cells and tissue in vitro: Useful biomarkers of aquatic pollution
    • Wells PG, Lee K, Blaise C (eds) CRC Lewis Publishers, Boca Raton, FL (in press)
    • Müller WEG, Müller I (1997) Sponge cells and tissue in vitro: useful biomarkers of aquatic pollution. In: Wells PG, Lee K, Blaise C (eds) Microscale aquatic toxicology -advances, techniques and practice. CRC Lewis Publishers, Boca Raton, FL (in press)
    • (1997) Microscale Aquatic Toxicology -Advances, Techniques and Practice
    • Müller, W.E.G.1    Müller, I.2
  • 22
    • 0029037081 scopus 로고
    • Combinatory effects of temperature stress and nonionic organic pollutants on stress protein (hsp70) gene expression in the fresh water sponge Ephydatia fluviatilis
    • Müller WEG, Koziol C, Kurelec B, Dapper J, Batel R, Rinkevich B (1995) Combinatory effects of temperature stress and nonionic organic pollutants on stress protein (hsp70) gene expression in the fresh water sponge Ephydatia fluviatilis. Arch Environ Contam Toxicol 14:1203-1208
    • (1995) Arch Environ Contam Toxicol , vol.14 , pp. 1203-1208
    • Müller, W.E.G.1    Koziol, C.2    Kurelec, B.3    Dapper, J.4    Batel, R.5    Rinkevich, B.6
  • 23
    • 0023052239 scopus 로고
    • An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro S, Pelham HRB (1986) An hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46: 291-300
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 25
    • 0003678344 scopus 로고
    • National Academy Press, Washington, DC
    • NRC (National Research Council) (1989) Biologic markers in reproductive toxicology. National Academy Press, Washington, DC, p 395-423
    • (1989) Biologic Markers in Reproductive Toxicology , pp. 395-423
  • 26
    • 0027486385 scopus 로고
    • Cloning of cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ
    • Ohtsuka K (1993) Cloning of cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ. Biochem Biophys Res Commun 197:235-240
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 235-240
    • Ohtsuka, K.1
  • 27
    • 0025092067 scopus 로고
    • A novel 40-kDa protein induced by heat shock and other stresses in mammalian and avian cells
    • Ohtsuka K, Masuda A, Nakai A, Nagata K (1990) A novel 40-kDa protein induced by heat shock and other stresses in mammalian and avian cells. Biochem Biophys Res Commun 166:642-647
    • (1990) Biochem Biophys Res Commun , vol.166 , pp. 642-647
    • Ohtsuka, K.1    Masuda, A.2    Nakai, A.3    Nagata, K.4
  • 28
    • 0003764925 scopus 로고
    • IntelliGenetics, Inc, Mountain View, CA
    • PC/GENE (1995) Data Banks CD-ROM; Release 14.0. IntelliGenetics, Inc, Mountain View, CA
    • (1995) Data Banks CD-ROM; Release 14.0
  • 29
    • 0027161599 scopus 로고
    • S-type lectins occur also in invertebrates: Unusual subunit composition and high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium
    • Pfeifer K, Haasemann M, Ugarkovic D, Bretting H, Fahrenholz F, Müller WEG (1993) S-type lectins occur also in invertebrates: unusual subunit composition and high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium. Glycobiology 3:179-184
    • (1993) Glycobiology , vol.3 , pp. 179-184
    • Pfeifer, K.1    Haasemann, M.2    Ugarkovic, D.3    Bretting, H.4    Fahrenholz, F.5    Müller, W.E.G.6
  • 30
    • 0027186197 scopus 로고
    • Plant DnaJ homologue: Molecular cloning, bacterial expression, and expression analysis in tissues of cucumber seedlings
    • Preisig-Müller R, Kindl H (1993) Plant DnaJ homologue: molecular cloning, bacterial expression, and expression analysis in tissues of cucumber seedlings. Arch Biochem Biophys 305:30-37
    • (1993) Arch Biochem Biophys , vol.305 , pp. 30-37
    • Preisig-Müller, R.1    Kindl, H.2
  • 32
    • 0000783063 scopus 로고
    • Ecologie des démosponges
    • Grassé PP (ed) Masson, Paris
    • Sarà M, Vacelet J (1973) Ecologie des démosponges. In: Grassé PP (ed) Traité de zoologie: spongiaires. Tome III(1). Masson, Paris, p 462-576
    • (1973) Traité de Zoologie: Spongiaires , vol.3 , Issue.1 , pp. 462-576
    • Sarà, M.1    Vacelet, J.2
  • 36
    • 0022536553 scopus 로고
    • Stress protein systems of mammalian cells
    • Subjeck JR, Shyy TT (1986) Stress protein systems of mammalian cells. Am J Physiol 17:C1-C17
    • (1986) Am J Physiol , vol.17
    • Subjeck, J.R.1    Shyy, T.T.2
  • 37
    • 0028837979 scopus 로고
    • Interaction between hsp70 and hsp40, eukaryotic homologoues of DnaK and DnaJ, in human cells expressing mutant-type p53
    • Sugito K, Yamane M, Hattori H, Hayashi Y, Tohnai I, Ueda M, Tsuchida N, Ohtsuka K (1995) Interaction between hsp70 and hsp40, eukaryotic homologoues of DnaK and DnaJ, in human cells expressing mutant-type p53. FEBS Lett 358: 161-164
    • (1995) FEBS Lett , vol.358 , pp. 161-164
    • Sugito, K.1    Yamane, M.2    Hattori, H.3    Hayashi, Y.4    Tohnai, I.5    Ueda, M.6    Tsuchida, N.7    Ohtsuka, K.8
  • 38
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 39
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai J, Douglas MG (1996) A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of hsp70 ATPase activity at a site distinct from substrate binding. J Biol Chem 272:9347-9354
    • (1996) J Biol Chem , vol.272 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 40
    • 0027462187 scopus 로고
    • Cloning, nucleotide sequence, and regulatory analysis of the Lactococcus lactis dnaJ gene
    • van Asseldonk M, Simons A, Visser H, de Vos WM, Simons G (1993) Cloning, nucleotide sequence, and regulatory analysis of the Lactococcus lactis dnaJ gene. J Bacteriol 175:1637-1644
    • (1993) J Bacteriol , vol.175 , pp. 1637-1644
    • Van Asseldonk, M.1    Simons, A.2    Visser, H.3    De Vos, W.M.4    Simons, G.5
  • 41
    • 0017386083 scopus 로고
    • Current-induced flow through living sponges in nature
    • Vogel S (1977) Current-induced flow through living sponges in nature. Proc Natl Acad Sci USA 74:2069-2071
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2069-2071
    • Vogel, S.1
  • 42
    • 0028930540 scopus 로고
    • The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone
    • Wall D, Zylicz M, Georgopoulos C (1995) The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J Biol Chem 270:2139-2144
    • (1995) J Biol Chem , vol.270 , pp. 2139-2144
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3


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