메뉴 건너뛰기




Volumn 31, Issue 7, 2006, Pages 546-555

Expression of HSP60 homologue in sheep blowfly Lucilia cuprina during development and heat stress

Author keywords

Blowfly; Chaperonin; Heat shock; Heat shock proteins (HSPs); HSP60; Lucilia cuprina; Stress proteins; Thermotolerance

Indexed keywords

HEAT SHOCK PROTEIN 60;

EID: 33748779303     PISSN: 03064565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jtherbio.2006.05.010     Document Type: Article
Times cited : (28)

References (47)
  • 2
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0033976869 scopus 로고    scopus 로고
    • Localization of mitochondrial 60-KD heat shock chaperonin protein (Hsp60) in pituitary growth hormone secretory granules and pancreatic zymogen granules
    • Cechetto J.D., Soltys B.J., and Gupta R.S. Localization of mitochondrial 60-KD heat shock chaperonin protein (Hsp60) in pituitary growth hormone secretory granules and pancreatic zymogen granules. J. Histochem. Cytochem. 48 (2000) 45-56
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 45-56
    • Cechetto, J.D.1    Soltys, B.J.2    Gupta, R.S.3
  • 5
    • 0024298706 scopus 로고
    • 70 KD heat shock related proteins stimulate protein translocations into microsomes
    • Chirico W.J., Walters M.G., and Blobel G. 70 KD heat shock related proteins stimulate protein translocations into microsomes. Nature 333 (1988) 805-810
    • (1988) Nature , vol.333 , pp. 805-810
    • Chirico, W.J.1    Walters, M.G.2    Blobel, G.3
  • 6
    • 0024298711 scopus 로고
    • A sub family of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies R.J., Koch B.D., Weiner-Washburne M., Craig E.A., and Schekman R. A sub family of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332 (1988) 800-805
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Weiner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 7
    • 0024314918 scopus 로고
    • Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures
    • Ellis R.J., and Hemmingsen S.M. Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci. 14 (1989) 339-342
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 339-342
    • Ellis, R.J.1    Hemmingsen, S.M.2
  • 8
    • 0015863794 scopus 로고
    • The synthetic and minimal culture requirements for evagination of imaginal disc of Drosophila melanogaster in vitro
    • Fristrom J.W., Logan W.R., and Murphy N.C. The synthetic and minimal culture requirements for evagination of imaginal disc of Drosophila melanogaster in vitro. Dev. Biol. 33 (1973) 441-456
    • (1973) Dev. Biol. , vol.33 , pp. 441-456
    • Fristrom, J.W.1    Logan, W.R.2    Murphy, N.C.3
  • 9
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes B-acting folding
    • Gao Y., Thomas J.O., Chow R.L., Lee G.H., and Cown N.J. A cytoplasmic chaperonin that catalyzes B-acting folding. Cell 69 (1992) 1043-1050
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cown, N.J.5
  • 12
    • 0026610981 scopus 로고
    • An interaction between p21ras and heat shock protein hsp90, a chaperonin
    • Ikawa S., and Weinberg R.A. An interaction between p21ras and heat shock protein hsp90, a chaperonin. Pro. Natl. Acad. Sci. USA 89 (1992) 2012-2016
    • (1992) Pro. Natl. Acad. Sci. USA , vol.89 , pp. 2012-2016
    • Ikawa, S.1    Weinberg, R.A.2
  • 14
    • 0028158395 scopus 로고
    • Enhancement in amount of P1 (hsp60) in mutants of Chinese hamster ovary (CHO-K1) cells exhibiting increases in the A system of amino acid transport
    • Jones M., Gupta R.S., and Englesberg E. Enhancement in amount of P1 (hsp60) in mutants of Chinese hamster ovary (CHO-K1) cells exhibiting increases in the A system of amino acid transport. Proc. Natl. Acad. Sci. USA 91 (1994) 858-862
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 858-862
    • Jones, M.1    Gupta, R.S.2    Englesberg, E.3
  • 16
    • 0037129860 scopus 로고    scopus 로고
    • Cytosolic heat shock protein HSP60, apoptosis and myocardial injury
    • Kirchhoff S.R., Gupta S., and Knowlton A.A. Cytosolic heat shock protein HSP60, apoptosis and myocardial injury. Circulation 105 (2002) 2899-2904
    • (2002) Circulation , vol.105 , pp. 2899-2904
    • Kirchhoff, S.R.1    Gupta, S.2    Knowlton, A.A.3
  • 17
    • 0028281597 scopus 로고
    • Molecular and cytogenetical characterization of the 10A1-2 band and adjoining regions in the Drosophila melanogaster polytene X chromosome
    • Kozlova T., Semeshin S.V., Tretyakova I.V., Kokoza E.B., Pirrotta V., Grafodatskaya V.E., Belyaeva E.S., and Zhimulev I.F. Molecular and cytogenetical characterization of the 10A1-2 band and adjoining regions in the Drosophila melanogaster polytene X chromosome. Genetics 136 (1994) 1063-1073
    • (1994) Genetics , vol.136 , pp. 1063-1073
    • Kozlova, T.1    Semeshin, S.V.2    Tretyakova, I.V.3    Kokoza, E.B.4    Pirrotta, V.5    Grafodatskaya, V.E.6    Belyaeva, E.S.7    Zhimulev, I.F.8
  • 18
    • 0030691192 scopus 로고    scopus 로고
    • The Drosophila melanogaster homologue of the hsp60 gene is encoded by the essential locus l(1)10Ac and is differentially expressed during fly development
    • Kozlova T., Perezgasga T., Reynaud E., and Zurita M. The Drosophila melanogaster homologue of the hsp60 gene is encoded by the essential locus l(1)10Ac and is differentially expressed during fly development. Dev. Genes Evol. 207 (1997) 253-263
    • (1997) Dev. Genes Evol. , vol.207 , pp. 253-263
    • Kozlova, T.1    Perezgasga, T.2    Reynaud, E.3    Zurita, M.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227 (1970) 682-685
    • (1970) Nature , vol.227 , pp. 682-685
    • Laemmli, U.K.1
  • 20
    • 0001525288 scopus 로고
    • A novel set of heat shock polypeptides in Malpighian tubules of Drosophila melanogaster
    • Lakhotia S.C., and Singh A.K. A novel set of heat shock polypeptides in Malpighian tubules of Drosophila melanogaster. J. Genet. 68 (1989) 129-137
    • (1989) J. Genet. , vol.68 , pp. 129-137
    • Lakhotia, S.C.1    Singh, A.K.2
  • 21
    • 0029783093 scopus 로고    scopus 로고
    • Synthesis of ubiquitously present new hsp60 family protein is enhanced by heat shock only in the Malpighian tubules of Drosophila
    • Lakhotia S.C., and Singh B.N. Synthesis of ubiquitously present new hsp60 family protein is enhanced by heat shock only in the Malpighian tubules of Drosophila. Experientia 52 (1996) 751-756
    • (1996) Experientia , vol.52 , pp. 751-756
    • Lakhotia, S.C.1    Singh, B.N.2
  • 22
    • 0018221572 scopus 로고
    • Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
    • Laskey R.A., Honda B.M., Mills A.D., and Finch J.T. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature 275 (1978) 416-420
    • (1978) Nature , vol.275 , pp. 416-420
    • Laskey, R.A.1    Honda, B.M.2    Mills, A.D.3    Finch, J.T.4
  • 23
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S. The heat-shock response. Annu. Rev. Biochem. 55 (1986) 1151-1191
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 24
    • 12244263525 scopus 로고    scopus 로고
    • Chaperonin 60 unfolds its secrets of cellular communication
    • Maguire M., Coates A.R.M., and Henderson B. Chaperonin 60 unfolds its secrets of cellular communication. Cell Stress Chaperones 7 (2002) 317-329
    • (2002) Cell Stress Chaperones , vol.7 , pp. 317-329
    • Maguire, M.1    Coates, A.R.M.2    Henderson, B.3
  • 25
    • 0000306312 scopus 로고
    • Structure and physiology of the egg shell
    • Gilbert L.I., and Kerkut G.A. (Eds), Pergamon Press, Oxford
    • Margaritis L.H. Structure and physiology of the egg shell. In: Gilbert L.I., and Kerkut G.A. (Eds). Comprehensive Insect Physiology, Biochemistry and Pharmacology (1985), Pergamon Press, Oxford 153-230
    • (1985) Comprehensive Insect Physiology, Biochemistry and Pharmacology , pp. 153-230
    • Margaritis, L.H.1
  • 26
    • 0023673510 scopus 로고
    • A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene
    • McMullin T.W., and Hallberg R.L. A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene. Mol. Cell Biol. 8 (1988) 371-380
    • (1988) Mol. Cell Biol. , vol.8 , pp. 371-380
    • McMullin, T.W.1    Hallberg, R.L.2
  • 27
    • 0033088466 scopus 로고    scopus 로고
    • Expression of mitochondrial marker proteins during spermatogenesis
    • Meinhardt A., Wilhem B., and Seitz J. Expression of mitochondrial marker proteins during spermatogenesis. Human Reprod. Update 5 (1999) 108-119
    • (1999) Human Reprod. Update , vol.5 , pp. 108-119
    • Meinhardt, A.1    Wilhem, B.2    Seitz, J.3
  • 28
    • 0029889530 scopus 로고    scopus 로고
    • Developmental expression of heat shock protein60 (HSP60) in rat testes and ovary
    • Paranko J., Seitz J., and Meinhardt A. Developmental expression of heat shock protein60 (HSP60) in rat testes and ovary. Differentiation 60 (1996) 159-167
    • (1996) Differentiation , vol.60 , pp. 159-167
    • Paranko, J.1    Seitz, J.2    Meinhardt, A.3
  • 29
    • 85012505857 scopus 로고    scopus 로고
    • Chaperonins are signaling proteins: the unfolding biology of molecular chaperones
    • Ranford J.C., Anthony R.M.C., and Henderson B. Chaperonins are signaling proteins: the unfolding biology of molecular chaperones. Exp. Rev. Mol. Med. (2000) 1-17
    • (2000) Exp. Rev. Mol. Med. , pp. 1-17
    • Ranford, J.C.1    Anthony, R.M.C.2    Henderson, B.3
  • 30
    • 0028823401 scopus 로고
    • Cpn60 is exclusively localized into mitochondria of rat liver and embryonic Drosophila cells
    • San Martin C., Flores A.I., and Cuezva J.M. Cpn60 is exclusively localized into mitochondria of rat liver and embryonic Drosophila cells. J. Cell Biochem. 59 (1995) 235-245
    • (1995) J. Cell Biochem. , vol.59 , pp. 235-245
    • San Martin, C.1    Flores, A.I.2    Cuezva, J.M.3
  • 31
    • 0027979131 scopus 로고
    • Heat-inducible proteins that react with antibodies to chaperonin60 are localized in the nucleus of a fish cell line
    • Sanders B.M., Nguyen J., Douglass T.G., and Miller S. Heat-inducible proteins that react with antibodies to chaperonin60 are localized in the nucleus of a fish cell line. J. Biochem. 297 (1994) 21-25
    • (1994) J. Biochem. , vol.297 , pp. 21-25
    • Sanders, B.M.1    Nguyen, J.2    Douglass, T.G.3    Miller, S.4
  • 32
    • 0031877537 scopus 로고    scopus 로고
    • Differential localization of heat shock protein 90, 70, 60 and 27 in human deciduas and placenta during pregnancy
    • Shah M., Stanek J., and Handwerger S. Differential localization of heat shock protein 90, 70, 60 and 27 in human deciduas and placenta during pregnancy. J. Histochem. 30 (1998) 509-518
    • (1998) J. Histochem. , vol.30 , pp. 509-518
    • Shah, M.1    Stanek, J.2    Handwerger, S.3
  • 33
    • 0033637554 scopus 로고    scopus 로고
    • Tissue-specific variations in the induction of Hsp70 and Hsp64 by heat shock in insects
    • Singh A.K., and Lakhotia S.C. Tissue-specific variations in the induction of Hsp70 and Hsp64 by heat shock in insects. Cell Stress Chaperones 5 (2000) 90-97
    • (2000) Cell Stress Chaperones , vol.5 , pp. 90-97
    • Singh, A.K.1    Lakhotia, S.C.2
  • 34
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells
    • Soltys B.J., and Gupta R.S. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp. Cell Res. 222 (1996) 16-27
    • (1996) Exp. Cell Res. , vol.222 , pp. 16-27
    • Soltys, B.J.1    Gupta, R.S.2
  • 35
    • 0003015274 scopus 로고    scopus 로고
    • The mitochondrial molecular chaperones Hsp60 and mHsp70: are their roles restricted to mitochondria?
    • Latchman D.S. (Ed), Springer, New York
    • Soltys B.J., and Gupta R.S. The mitochondrial molecular chaperones Hsp60 and mHsp70: are their roles restricted to mitochondria?. In: Latchman D.S. (Ed). Stress Proteins. Handbook of Experimental Pharmacology vol. 136 (1999), Springer, New York 69-100
    • (1999) Stress Proteins. Handbook of Experimental Pharmacology , vol.136 , pp. 69-100
    • Soltys, B.J.1    Gupta, R.S.2
  • 36
    • 0033133729 scopus 로고    scopus 로고
    • Mitochondrial matrix proteins at unexpected locations: are they exported?
    • Soltys B.J., and Gupta R.S. Mitochondrial matrix proteins at unexpected locations: are they exported?. Trends Biochem. Sci. 24 (1999) 174-177
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 174-177
    • Soltys, B.J.1    Gupta, R.S.2
  • 37
    • 0033988390 scopus 로고    scopus 로고
    • Mitochondrial matrix proteins at unexpected cellular locations: protein export from mitochondria from an evolutionary perspective
    • Soltys B.J., and Gupta R.S. Mitochondrial matrix proteins at unexpected cellular locations: protein export from mitochondria from an evolutionary perspective. Int. Rev. Cytol. 194 (1999) 133-195
    • (1999) Int. Rev. Cytol. , vol.194 , pp. 133-195
    • Soltys, B.J.1    Gupta, R.S.2
  • 38
    • 0035067292 scopus 로고    scopus 로고
    • The hsp60B gene in Drosophila melanogaster is essential for the spermatid individualization process
    • Timakov B., and Zhang P. The hsp60B gene in Drosophila melanogaster is essential for the spermatid individualization process. Cell Stress Chaperones 6 (2001) 71-77
    • (2001) Cell Stress Chaperones , vol.6 , pp. 71-77
    • Timakov, B.1    Zhang, P.2
  • 39
    • 51249164237 scopus 로고
    • Developmental study of thermotolerance and the heat shock response in Lucilia cuprina (Weidemann)
    • Tiwari P.K., Mohan D.R.K., and Archana J. Developmental study of thermotolerance and the heat shock response in Lucilia cuprina (Weidemann). J. Biosci. 20 (1995) 341-354
    • (1995) J. Biosci. , vol.20 , pp. 341-354
    • Tiwari, P.K.1    Mohan, D.R.K.2    Archana, J.3
  • 40
    • 0023711176 scopus 로고
    • A Drosophila melanogaster gene encodes a protein homologous to the mouse t-complex polypeptide-1
    • Ursic D., and Ganetzky B. A Drosophila melanogaster gene encodes a protein homologous to the mouse t-complex polypeptide-1. Gene 68 (1988) 267-274
    • (1988) Gene , vol.68 , pp. 267-274
    • Ursic, D.1    Ganetzky, B.2
  • 41
    • 0032437394 scopus 로고    scopus 로고
    • Heat shock proteins chaperoning life and death
    • Vayssier M., and Polla B.S. Heat shock proteins chaperoning life and death. Cell Stress Chaperones 3 (1998) 221-227
    • (1998) Cell Stress Chaperones , vol.3 , pp. 221-227
    • Vayssier, M.1    Polla, B.S.2
  • 42
    • 0029550391 scopus 로고
    • Presence of Chromatium vinosum chaperonins10 and 60 in mitochondria and peroxisomes of rat hepatocytes
    • Velez-Granell C.S., Arias A.E., Torres-Ruiz J.A., and Bendayan M. Presence of Chromatium vinosum chaperonins10 and 60 in mitochondria and peroxisomes of rat hepatocytes. Biol. Cell 85 (1995) 67-75
    • (1995) Biol. Cell , vol.85 , pp. 67-75
    • Velez-Granell, C.S.1    Arias, A.E.2    Torres-Ruiz, J.A.3    Bendayan, M.4
  • 43
    • 0031002389 scopus 로고    scopus 로고
    • Restoration of MHC class I surface expression and endogenous antigen presentation by a molecular chaperone
    • Wells A.D., Rai S.K., Salvato M.S., Band H., and Malkovsky M. Restoration of MHC class I surface expression and endogenous antigen presentation by a molecular chaperone. Scand. J. Immunol. 45 (1997) 605-612
    • (1997) Scand. J. Immunol. , vol.45 , pp. 605-612
    • Wells, A.D.1    Rai, S.K.2    Salvato, M.S.3    Band, H.4    Malkovsky, M.5
  • 44
    • 33748785341 scopus 로고    scopus 로고
    • Wigglesworth, V.B. (Ed.), 1972. Circulatory system and associated tissues, In: The Principles of Insect Physiology, seventh edition, Chapter X. English Language Book Society & Chapman and Hall, Great Britain, pp., 442-451.
  • 47
    • 0011039179 scopus 로고
    • The egg shell of Drosophila melanogaster. V Structure and morphogenesis of micropylar apparatus
    • Zarani F.E., and Margaritis L.H. The egg shell of Drosophila melanogaster. V Structure and morphogenesis of micropylar apparatus. Can. J. Zool. 64 (1986) 2509-2519
    • (1986) Can. J. Zool. , vol.64 , pp. 2509-2519
    • Zarani, F.E.1    Margaritis, L.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.