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Volumn 17, Issue 5, 2008, Pages 565-572

Rapid cold hardening elicits changes in brain protein profiles of the flesh fly, Sarcophaga crassipalpis

Author keywords

ATP synthase; Heat shock proteins; Proteomics; Rapid cold hardening; Sarcophaga crassipalpis

Indexed keywords

INSECT PROTEIN; PROTEOME;

EID: 52049103363     PISSN: 09621075     EISSN: 13652583     Source Type: Journal    
DOI: 10.1111/j.1365-2583.2008.00827.x     Document Type: Article
Times cited : (42)

References (43)
  • 1
    • 0028903288 scopus 로고
    • 14-3-3 proteins on the MAP
    • Aitken, A. (1995) 14-3-3 proteins on the MAP. Trends Biochem Sci 20 : 95 97.
    • (1995) Trends Biochem Sci , vol.20 , pp. 95-97
    • Aitken, A.1
  • 2
    • 0025344531 scopus 로고
    • Disruption of the actin cytoskeleton in yeast capping protein mutants
    • Amatruda, J.F., Cannon, J.F., Tatchell, K., Hug, C. Cooper, J.A. (1990) Disruption of the actin cytoskeleton in yeast capping protein mutants. Nature 344 : 352 354.
    • (1990) Nature , vol.344 , pp. 352-354
    • Amatruda, J.F.1    Cannon, J.F.2    Tatchell, K.3    Hug, C.4    Cooper, J.A.5
  • 3
    • 0026035853 scopus 로고
    • A unique zinc finger protein is associated preferentially with active ecdysone-responsive loci in Drosophila
    • Amero, S.A., Elgin, S.C. Beyer, A.L. (1991) A unique zinc finger protein is associated preferentially with active ecdysone-responsive loci in Drosophila. Genes & Dev 5 : 188 200.
    • (1991) Genes & Dev , vol.5 , pp. 188-200
    • Amero, S.A.1    Elgin, S.C.2    Beyer, A.L.3
  • 5
    • 0023052752 scopus 로고
    • Thin filament regulatory proteins of smooth and nonmuscle cells
    • Bretscher, A. (1986) Thin filament regulatory proteins of smooth and nonmuscle cells. Nature 321 : 726 727.
    • (1986) Nature , vol.321 , pp. 726-727
    • Bretscher, A.1
  • 6
    • 0000146539 scopus 로고
    • Cold-shock injury and rapid cold hardening in the flesh fly Sarcophaga crassipalpis
    • Chen, C.P., Denlinger, D.L. Lee Jr., R.E. (1987) Cold-shock injury and rapid cold hardening in the flesh fly Sarcophaga crassipalpis. Physiol Zool 60 : 297 304.
    • (1987) Physiol Zool , vol.60 , pp. 297-304
    • Chen, C.P.1    Denlinger, D.L.2    Lee Jr., R.E.3
  • 7
    • 34748843152 scopus 로고    scopus 로고
    • Proteomic profiling of a parasitic wasp exposed to constant and fluctuating cold exposure
    • Colinet, H., Nguyen, T.T.A., Cloutier, C., Michaud, D. Hance, T. (2007) Proteomic profiling of a parasitic wasp exposed to constant and fluctuating cold exposure. Insect Biochem Mol Biol 37 : 1177 1188.
    • (2007) Insect Biochem Mol Biol , vol.37 , pp. 1177-1188
    • Colinet, H.1    Nguyen, T.T.A.2    Cloutier, C.3    Michaud, D.4    Hance, T.5
  • 8
    • 25444465680 scopus 로고    scopus 로고
    • Key themes in the study of seasonal adaptation in insects: Patterns of cold hardiness
    • Danks, H.V. (2005) Key themes in the study of seasonal adaptation in insects: patterns of cold hardiness. Appl Entomol Zool 40 : 199 211.
    • (2005) Appl Entomol Zool , vol.40 , pp. 199-211
    • Danks, H.V.1
  • 9
    • 0002557687 scopus 로고
    • Induction and termination of pupal diapause in Sarcophaga (Diptera: Sarcophagidae
    • Woods Hole
    • Denlinger, D.L. (1972) Induction and termination of pupal diapause in Sarcophaga (Diptera: Sarcophagidae). Biol Bull, Woods Hole 142 : 11 24.
    • (1972) Biol Bull , vol.142 , pp. 11-24
    • Denlinger, D.L.1
  • 10
    • 0002650343 scopus 로고
    • Relationship between cold hardiness and diapause
    • In. Lee, R.E. Denlinger, D.L., eds. pp. Chapman and Hall, New York/London.
    • Denlinger, D.L. (1991) Relationship between cold hardiness and diapause. In Insects at Low Temperature (Lee, R.E. Denlinger, D.L., eds pp. 174 198. Chapman and Hall, New York/London.
    • (1991) Insects at Low Temperature , pp. 174-198
    • Denlinger, D.L.1
  • 11
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology
    • Feder, M.E. Hoffmann, G.E. (1999) Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Ann Rev Physiol 61 : 243 282.
    • (1999) Ann Rev Physiol , vol.61 , pp. 243-282
    • Feder, M.E.1    Hoffmann, G.E.2
  • 12
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosin-based regulation of the actin cytoskeleton in time and space
    • Gunning, P., O'Neill, G. Hardeman, E. (2008) Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol Rev 88 : 1 35.
    • (2008) Physiol Rev , vol.88 , pp. 1-35
    • Gunning, P.1    O'Neill, G.2    Hardeman, E.3
  • 14
    • 0000990781 scopus 로고
    • Cold shock elicits expression of heat-shock proteins in the flesh fly, Sarcophaga crassipalpis
    • Joplin, K.H., Yocum, G.D. Denlinger, D.L. (1990) Cold shock elicits expression of heat-shock proteins in the flesh fly, Sarcophaga crassipalpis. J Insect Physiol 36 : 825 834.
    • (1990) J Insect Physiol , vol.36 , pp. 825-834
    • Joplin, K.H.1    Yocum, G.D.2    Denlinger, D.L.3
  • 15
    • 26944497670 scopus 로고    scopus 로고
    • Expression of mRNA for the t-complex polypeptide-1, a subunit of chaperonin CCT, is upregulated in association with increased cold hardiness in Delia antiqua
    • Kayukawa, T., Chen, B., Miyazaki, S., Itoyama, K., Shinoda, T. Ishikawa, Y. (2005) Expression of mRNA for the t-complex polypeptide-1, a subunit of chaperonin CCT, is upregulated in association with increased cold hardiness in Delia antiqua. Cell Stress Chaperones 10 : 204 210.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 204-210
    • Kayukawa, T.1    Chen, B.2    Miyazaki, S.3    Itoyama, K.4    Shinoda, T.5    Ishikawa, Y.6
  • 16
    • 0035745506 scopus 로고    scopus 로고
    • Rapid cold-hardening of Drosophila melanogaster (Diptera: Drosophilidae) during ecologically based thermoperiodic cycles
    • Kelty, J.D. Lee Jr., R.E. (2001) Rapid cold-hardening of Drosophila melanogaster (Diptera: Drosophilidae) during ecologically based thermoperiodic cycles. J Exp Biol 204 : 1659 1666.
    • (2001) J Exp Biol , vol.204 , pp. 1659-1666
    • Kelty, J.D.1    Lee Jr., R.E.2
  • 17
    • 0001027139 scopus 로고    scopus 로고
    • Increased levels of mitochondrial ATP synthase α-subunit in fast skeletal muscle of carp acclimated to cold temperature
    • Kikuchi, K., Itoi, S. Watabe, S. (1999) Increased levels of mitochondrial ATP synthase α-subunit in fast skeletal muscle of carp acclimated to cold temperature. Fish Sci 65 : 629 636.
    • (1999) Fish Sci , vol.65 , pp. 629-636
    • Kikuchi, K.1    Itoi, S.2    Watabe, S.3
  • 18
    • 33751002961 scopus 로고    scopus 로고
    • Upregulation of two actin genes and redistribution of actin during diapause and cold stress in the northern house mosquito, Culex pipiens
    • Kim, M., Robich, R.M., Rinehart, J.P. Denlinger, D.L. (2006) Upregulation of two actin genes and redistribution of actin during diapause and cold stress in the northern house mosquito, Culex pipiens. J Insect Physiol 52 : 1226 1233.
    • (2006) J Insect Physiol , vol.52 , pp. 1226-1233
    • Kim, M.1    Robich, R.M.2    Rinehart, J.P.3    Denlinger, D.L.4
  • 20
    • 0038119929 scopus 로고    scopus 로고
    • The pyruvate decarboxylase1 gene of Arabidopsis is required during anoxia but not other environmental stresses
    • Kursteiner, O., Dupuis, I. Kuhlemeier, C. (2003) The pyruvate decarboxylase1 gene of Arabidopsis is required during anoxia but not other environmental stresses. Plant Physiol 132 : 968 978.
    • (2003) Plant Physiol , vol.132 , pp. 968-978
    • Kursteiner, O.1    Dupuis, I.2    Kuhlemeier, C.3
  • 21
    • 0017288488 scopus 로고
    • Actin, a-actinin, and tropomyosin interaction in the structural organization of actin filaments in nonmuscle cells
    • Lazarides, E. (1976) Actin, a-actinin, and tropomyosin interaction in the structural organization of actin filaments in nonmuscle cells. J Cell Biol 68 : 202 219.
    • (1976) J Cell Biol , vol.68 , pp. 202-219
    • Lazarides, E.1
  • 22
    • 0023490966 scopus 로고
    • A rapid cold-hardening process in insects
    • Lee, R.E., Chen, C.-P. Denlinger, D.L. (1987) A rapid cold-hardening process in insects. Science 238 : 1415 1417.
    • (1987) Science , vol.238 , pp. 1415-1417
    • Lee, R.E.1    Chen, C.-P.2    Denlinger, D.L.3
  • 23
    • 33947618939 scopus 로고    scopus 로고
    • Proteomics of the flesh fly brain reveals an abundance of upregulated heat shock proteins during pupal diapause
    • Li, A.Q., Popova-Butler, A., Dean, D.H. Denlinger, D.L. (2007) Proteomics of the flesh fly brain reveals an abundance of upregulated heat shock proteins during pupal diapause. J Insect Physiol 53 : 385 391.
    • (2007) J Insect Physiol , vol.53 , pp. 385-391
    • Li, A.Q.1    Popova-Butler, A.2    Dean, D.H.3    Denlinger, D.L.4
  • 24
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang, P. MacRae, T.H. (1997) Molecular chaperones and the cytoskeleton. J Cell Sci 110 : 1431 1440.
    • (1997) J Cell Sci , vol.110 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 25
    • 0024516197 scopus 로고
    • Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton
    • Liu, H. Bretscher, A. (1989) Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton. Cell 57 : 233 242.
    • (1989) Cell , vol.57 , pp. 233-242
    • Liu, H.1    Bretscher, A.2
  • 26
    • 0020538452 scopus 로고
    • Isolation and characterization of tropomyosin-containing microfilaments from cultured cells
    • Matsumura, F., Yamashiro-Matsumura, S. Lin, J.J. (1983) Isolation and characterization of tropomyosin-containing microfilaments from cultured cells. J Biol Chem 258 : 6636 6644.
    • (1983) J Biol Chem , vol.258 , pp. 6636-6644
    • Matsumura, F.1    Yamashiro-Matsumura, S.2    Lin, J.J.3
  • 27
    • 24344460521 scopus 로고    scopus 로고
    • 14-3-3 proteins - An update
    • Mhawech, P. (2005) 14-3-3 proteins - an update. Cell Res 15 : 228 236.
    • (2005) Cell Res , vol.15 , pp. 228-236
    • Mhawech, P.1
  • 28
    • 33750318810 scopus 로고    scopus 로고
    • Oleic acid is elevated in cell membranes during rapid cold-hardening and pupal diapause in the flesh fly, Sarcophaga crassipalpis
    • Michaud, M.R. Denlinger, D.L. (2006) Oleic acid is elevated in cell membranes during rapid cold-hardening and pupal diapause in the flesh fly, Sarcophaga crassipalpis. J Insect Physiol 52 : 1073 1082.
    • (2006) J Insect Physiol , vol.52 , pp. 1073-1082
    • Michaud, M.R.1    Denlinger, D.L.2
  • 29
    • 34548718338 scopus 로고    scopus 로고
    • Shifts in the carbohydrate, polyol, and amino acid pools during rapid cold-hardening and diapause-associated cold-hardening in flesh flies (Sarcophaga crassipalpis): A metabolomic comparison
    • Michaud, M.R. Denlinger, D.L. (2007) Shifts in the carbohydrate, polyol, and amino acid pools during rapid cold-hardening and diapause-associated cold-hardening in flesh flies (Sarcophaga crassipalpis): a metabolomic comparison. J Comp Physiol B 177 : 753 763.
    • (2007) J Comp Physiol B , vol.177 , pp. 753-763
    • Michaud, M.R.1    Denlinger, D.L.2
  • 30
    • 33746123027 scopus 로고    scopus 로고
    • Actin-capping protein is involved in controlling organization of actin cytoskeleton together with ADF/cofilin, profilin and F-actin crosslinking proteins in fission yeast
    • Nakano, K. Mabuchi, I. (2006) Actin-capping protein is involved in controlling organization of actin cytoskeleton together with ADF/cofilin, profilin and F-actin crosslinking proteins in fission yeast. Genes Cells 11 : 893 905.
    • (2006) Genes Cells , vol.11 , pp. 893-905
    • Nakano, K.1    Mabuchi, I.2
  • 31
    • 27644459878 scopus 로고    scopus 로고
    • Changes in membrane lipid composition following rapid cold hardening in Drosphila melanogaster
    • Overgaard, J., Sorensen, J.G., Petersen, S.O., Loeschcke, V. Holmstrup, M. (2005) Changes in membrane lipid composition following rapid cold hardening in Drosphila melanogaster. J Insect Physiol 51 : 1173 1182.
    • (2005) J Insect Physiol , vol.51 , pp. 1173-1182
    • Overgaard, J.1    Sorensen, J.G.2    Petersen, S.O.3    Loeschcke, V.4    Holmstrup, M.5
  • 32
    • 0011740229 scopus 로고
    • Heat-shock messenger-RNA accumulation during recovery from cold shock in Drosophila melanogaster
    • Petersen, N.S., Young, P. Burton, V. (1990) Heat-shock messenger-RNA accumulation during recovery from cold shock in Drosophila melanogaster. Insect Biochem 20 : 679 684.
    • (1990) Insect Biochem , vol.20 , pp. 679-684
    • Petersen, N.S.1    Young, P.2    Burton, V.3
  • 33
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • Pruyne, D.W., Schott, D.H. Brestscher, A. (1998) Tropomyosin-containing actin cables direct the myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J Cell Biol 143 : 1931 1945.
    • (1998) J Cell Biol , vol.143 , pp. 1931-1945
    • Pruyne, D.W.1    Schott, D.H.2    Brestscher, A.3
  • 34
    • 0034517966 scopus 로고    scopus 로고
    • Heat shock protein 90 is downregulated during pupal diapause in the flesh fly, Sarcophaga crassipalpis, but remains responsive to thermal stress
    • Rinehart, J.P. Denlinger, D.L. (2000) Heat shock protein 90 is downregulated during pupal diapause in the flesh fly, Sarcophaga crassipalpis, but remains responsive to thermal stress. Insect Mol Biol 9 : 641 645.
    • (2000) Insect Mol Biol , vol.9 , pp. 641-645
    • Rinehart, J.P.1    Denlinger, D.L.2
  • 36
    • 0034096932 scopus 로고    scopus 로고
    • Developmental upregulation of inducible hsp70 transcripts, but not the cognate form, during pupal diapause in the flesh fly, Sarcophaga crassipalpis
    • Rinehart, J.P., Yocum, G.D. Denlinger, D.L. (2000) Developmental upregulation of inducible hsp70 transcripts, but not the cognate form, during pupal diapause in the flesh fly, Sarcophaga crassipalpis. Insect Biochem Mol Biol 30 : 515 521.
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 515-521
    • Rinehart, J.P.1    Yocum, G.D.2    Denlinger, D.L.3
  • 37
    • 29144527460 scopus 로고    scopus 로고
    • Small heat shock proteins: Molecular structure and chaperone function
    • Sun, Y. MacRae, T.H. (2005) Small heat shock proteins: molecular structure and chaperone function. Cell Mol Life Sci 62 : 2460 2476.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2460-2476
    • Sun, Y.1    MacRae, T.H.2
  • 38
    • 7044222582 scopus 로고    scopus 로고
    • Expression of the Drosophila melanogaster ATP synthase alpha subunit gene is regulated by a transcriptional element containing GAF and Adf-1 binding sites
    • Talamillo, A., Fernandez-Moreno M.A., Martinez-Azorin, F., Bornstein, B., Ochoa, P. Garesse, R. (2004) Expression of the Drosophila melanogaster ATP synthase alpha subunit gene is regulated by a transcriptional element containing GAF and Adf-1 binding sites. Eur J Biochem 271 : 4003 4013.
    • (2004) Eur J Biochem , vol.271 , pp. 4003-4013
    • Talamillo, A.1    Fernandez-Moreno, M.A.2    Martinez-Azorin, F.3    Bornstein, B.4    Ochoa, P.5    Garesse, R.6
  • 39
    • 0026345831 scopus 로고
    • The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes
    • Ursic, D. Culbertson, M.R. (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11 : 2629 2640.
    • (1991) Mol Cell Biol , vol.11 , pp. 2629-2640
    • Ursic, D.1    Culbertson, M.R.2
  • 40
    • 0027988048 scopus 로고
    • The essential yeast Tcp1 protein affects actin and microtubules
    • Ursic, D., Sedbrook, J.C., Himmel, K.L. Culbertson, M.R. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Cell Biol 5 : 1065 1080.
    • (1994) Mol Cell Biol , vol.5 , pp. 1065-1080
    • Ursic, D.1    Sedbrook, J.C.2    Himmel, K.L.3    Culbertson, M.R.4
  • 41
    • 11144245310 scopus 로고    scopus 로고
    • In vivo and in vitro rapid cold-hardening protects cells from cold-shock injury in the flesh fly
    • Yi, S.X. Lee, R.E. (2004) In vivo and in vitro rapid cold-hardening protects cells from cold-shock injury in the flesh fly. J Comp Physiol B 174 : 611 615.
    • (2004) J Comp Physiol B , vol.174 , pp. 611-615
    • Yi, S.X.1    Lee, R.E.2
  • 42
    • 0032169108 scopus 로고    scopus 로고
    • Upregulation of a 23 kDa small heat shock protein transcript during pupal diapause in the flesh fly, Sarcophaga crassipalpis
    • Yocum, G.D., Joplin, K.H. Denlinger, D.L. (1998) Upregulation of a 23 kDa small heat shock protein transcript during pupal diapause in the flesh fly, Sarcophaga crassipalpis. Insect Biochem Mol Biol 28 : 677 682.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 677-682
    • Yocum, G.D.1    Joplin, K.H.2    Denlinger, D.L.3
  • 43
    • 31144445335 scopus 로고    scopus 로고
    • Stress-induced accumulation of glycerol in the flesh fly, Sarcophaga bullata: Evidence indicating anti-desiccant and cryoprotectant functions of this polyol and a role for the brain in coordinating the response
    • Yoder, J.A., Benoit, J.B., Denlinger, D.L. Rivers, D.B. (2006) Stress-induced accumulation of glycerol in the flesh fly, Sarcophaga bullata: evidence indicating anti-desiccant and cryoprotectant functions of this polyol and a role for the brain in coordinating the response. J Insect Physiol 52 : 383 392.
    • (2006) J Insect Physiol , vol.52 , pp. 383-392
    • Yoder, J.A.1    Benoit, J.B.2    Denlinger, D.L.3    Rivers, D.B.4


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