메뉴 건너뛰기




Volumn 22, Issue 1, 2009, Pages 125-136

Effect of low temperature on metabolic enzymes and HSP-70 expression of coldwater fish Barilius bendelisis

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84887994450     PISSN: 01166514     EISSN: 20733720     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (5)

References (38)
  • 1
    • 0035089772 scopus 로고    scopus 로고
    • Cold-acclimation increases basal heart rate but decreases its thermal tolerance in rainbow trout (Oncorhynchus mykiss)
    • Aho, E. and M. Vornanen. 2000. Cold-acclimation increases basal heart rate but decreases its thermal tolerance in rainbow trout (Oncorhynchus mykiss). Journal of Comparative Physiology 171: 173-179.
    • (2000) Journal of Comparative Physiology , vol.171 , pp. 173-179
    • Aho, E.1    Vornanen, M.2
  • 4
    • 85072061918 scopus 로고
    • Effect of thermal variation on some haematological values of Schizothorax plagiostomus (Heckel)
    • Bhatt, S.N. and H. R. Singh. 1985. Effect of thermal variation on some haematological values of Schizothorax plagiostomus (Heckel). Uttar Pradesh Journal of Zoology 5: 2004-2009.
    • (1985) Uttar Pradesh Journal of Zoology , vol.5 , pp. 2004-2009
    • Bhatt, S.N.1    Singh, H.R.2
  • 5
    • 33746025348 scopus 로고    scopus 로고
    • Post-genomic approaches to understanding the mechanisms of environmentally induced phenotypic plasticity
    • Cossins, A., J. Fraser, M. Hughes and A. Gracey. 2006. Post-genomic approaches to understanding the mechanisms of environmentally induced phenotypic plasticity. Journal of Experimental Biology 209: 2328-2336.
    • (2006) Journal of Experimental Biology , vol.209 , pp. 2328-2336
    • Cossins, A.1    Fraser, J.2    Hughes, M.3    Gracey, A.4
  • 6
    • 0033845244 scopus 로고    scopus 로고
    • The effects of heat shock and acclimation temperature on heat shock protein 70 and heat shock protein 30 mRNA expression in rainbow trout: In vivo and in vitro comparisons
    • Currie, S, C.D. Moyes and B. L. Tufts. 2000. The effects of heat shock and acclimation temperature on heat shock protein 70 and heat shock protein 30 mRNA expression in rainbow trout: In vivo and in vitro comparisons. Journal of Fish Biology 56: 398-408.
    • (2000) Journal of Fish Biology , vol.56 , pp. 398-408
    • Currie, S.1    Moyes, C.D.2    Tufts, B.L.3
  • 8
    • 0021253718 scopus 로고
    • Pyruvate kinase in fetal plasma and amniotic fluid unsuccessful for the prenatal diagnosis of Duchenne muscular dystrophy
    • Edwards R.J., C.H. Rodeck and D.C. Watts. 1984. Pyruvate kinase in fetal plasma and amniotic fluid unsuccessful for the prenatal diagnosis of Duchenne muscular dystrophy. American Journal Medical Genetics 18:231-235.
    • (1984) American Journal Medical Genetics , vol.18 , pp. 231-235
    • Edwards, R.J.1    Rodeck, C.H.2    Watts, D.C.3
  • 9
    • 0034973280 scopus 로고    scopus 로고
    • Protein function at thermal extremes: Balancing stability and flexibility
    • Fields, P. A. 2001. Protein function at thermal extremes: Balancing stability and flexibility. Comparative Biochemistry and Physiology 129: 417-431.
    • (2001) Comparative Biochemistry and Physiology , vol.129 , pp. 417-431
    • Fields, P.A.1
  • 10
    • 8444235985 scopus 로고    scopus 로고
    • Decreases in Activation Energy and Substrate Affinity in Cold-Adapted A4-Lactate Dehydrogenase: Evidence from the Antarctic Notothenioid Fish Chaenocephalus aceratus
    • Fields, P. A. and D. E. Houseman. 2004. Decreases in Activation Energy and Substrate Affinity in Cold-Adapted A4-Lactate Dehydrogenase: Evidence from the Antarctic Notothenioid Fish Chaenocephalus aceratus. Molecular Biology and Evolution 21: 2246-2255.
    • (2004) Molecular Biology and Evolution , vol.21 , pp. 2246-2255
    • Fields, P.A.1    Houseman, D.E.2
  • 11
    • 0036022336 scopus 로고    scopus 로고
    • Temperature adaptation in Gillichthys (Teleost: Gobiidae) A4-lactate dehydrogenase: Identical primary structures produce subtly different conformations
    • Fields, P. A., Y. S. Kim, J. F. Carpenter and G. N. Somero. 2002. Temperature adaptation in Gillichthys (Teleost: Gobiidae) A4-lactate dehydrogenase: Identical primary structures produce subtly different conformations. Journal of Experimental Biology 205:1293-1303.
    • (2002) Journal of Experimental Biology , vol.205 , pp. 1293-1303
    • Fields, P.A.1    Kim, Y.S.2    Carpenter, J.F.3    Somero, G.N.4
  • 13
    • 0025372837 scopus 로고
    • The isozymes of Pyruvate kinase in zebra fish
    • Granner, D. and S. Pilkis. 1990. The isozymes of Pyruvate kinase in zebra fish. Journal of Biological Chemistry 265: 10173-10176
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 10173-10176
    • Granner, D.1    Pilkis, S.2
  • 14
    • 0024787445 scopus 로고
    • The temperature dependence of the time course of growth and decay of miniature end-plate currents in carp extraocular muscle following thermal acclimation
    • Harper A. A, J. R. Shelton and P. W. Watt. 1989. The temperature dependence of the time course of growth and decay of miniature end-plate currents in carp extraocular muscle following thermal acclimation. Journal of Experimental Biology 147: 237-248
    • (1989) Journal of Experimental Biology , vol.147 , pp. 237-248
    • Harper, A.A.1    Shelton, J.R.2    Watt, P.W.3
  • 15
    • 0000513081 scopus 로고
    • Consequences of thermal change on the myofibrillar ATPase of five freshwater teleosts
    • Heap, S. P., P. W. Watt, and G. Goldspink. 1985. Consequences of thermal change on the myofibrillar ATPase of five freshwater teleosts. Journal of Fish Biology 26: 733-738.
    • (1985) Journal of Fish Biology , vol.26 , pp. 733-738
    • Heap, S.P.1    Watt, P.W.2    Goldspink, G.3
  • 19
    • 0018820757 scopus 로고
    • Some haematological values of Clarius batrachus L. Following its sudden transfer to varying temperatures
    • Joshi, B.D., L.D. Chaturvedi and R. Debral. 1980. Some haematological values of Clarius batrachus L. following its sudden transfer to varying temperatures. Indian Journal Experimental Biology 18 (1): 76-77.
    • (1980) Indian Journal Experimental Biology , vol.18 , Issue.1 , pp. 76-77
    • Joshi, B.D.1    Chaturvedi, L.D.2    Debral, R.3
  • 20
    • 0036384940 scopus 로고    scopus 로고
    • Differential gene expression in the brain of channel of cat fish (Ictarus punctatus) in response to cold acclimation
    • Ju, Z., R.A. Dunham, and Z. Liu. 2002. Differential gene expression in the brain of channel of cat fish (Ictarus punctatus) in response to cold acclimation. Molecular Genetics and Genomics 268: 87-95.
    • (2002) Molecular Genetics and Genomics , vol.268 , pp. 87-95
    • Ju, Z.1    Dunham, R.A.2    Liu, Z.3
  • 21
    • 84857970312 scopus 로고    scopus 로고
    • Impact of temperature variation on haematology and serum enzymes of Schizothorax richardsonii
    • Kapila, R., S. Kapila and Y. Basade. 2002. Impact of temperature variation on haematology and serum enzymes of Schizothorax richardsonii. Indian Journal of Fisheries 49 (2): 187-192
    • (2002) Indian Journal of Fisheries , vol.49 , Issue.2 , pp. 187-192
    • Kapila, R.1    Kapila, S.2    Basade, Y.3
  • 22
    • 85072065056 scopus 로고    scopus 로고
    • Eterase as a marker for identification of genetic variations in coldwater fish, Schizothorax richardsonii (Gray)
    • Kapila, R and D.P. Mishra. 2006. Eterase as a marker for identification of genetic variations in coldwater fish, Schizothorax richardsonii (Gray). Journal of. Inland Fisheries Society of India 38(1):68-71.
    • (2006) Journal Of. Inland Fisheries Society of India , vol.38 , Issue.1 , pp. 68-71
    • Kapila, R.1    Mishra, D.P.2
  • 23
    • 31344476167 scopus 로고    scopus 로고
    • Comparisons of physiological and biochemical responses between milk fish and grass carp to cold shock
    • Kuo, C.M. and S.L. Hsieh. 2006. Comparisons of physiological and biochemical responses between milk fish and grass carp to cold shock. Aquaculture 251: 525-536
    • (2006) Aquaculture , vol.251 , pp. 525-536
    • Kuo, C.M.1    Hsieh, S.L.2
  • 24
    • 0030879226 scopus 로고    scopus 로고
    • Characterization of cold-induced HSP expression in neonatal rat cardiomyocytes
    • Laios, E., I. M. Rebeyka, and C.A. Prody. 1997. Characterization of cold-induced HSP expression in neonatal rat cardiomyocytes. Molecular Cellular Endocrinology 173: 153-159.
    • (1997) Molecular Cellular Endocrinology , vol.173 , pp. 153-159
    • Laios, E.1    Rebeyka, I.M.2    Prody, C.A.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophages T4
    • Laemmli, U.K. 1970. Cleavage of structure proteins during the assembly of the head of bacteriophages T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0242660607 scopus 로고    scopus 로고
    • Up regulation of HSP-70 in reloading rat soleus muscle after prolonged hindlimb unloading
    • Oishi, Y., K. Taniguchi, F. Kawano, A. Ishihara and Y. Ohira. 2003. Up regulation of HSP-70 in reloading rat soleus muscle after prolonged hindlimb unloading. Japanese Journal of Physiology 53: 281-286.
    • (2003) Japanese Journal of Physiology , vol.53 , pp. 281-286
    • Oishi, Y.1    Taniguchi, K.2    Kawano, F.3    Ishihara, A.4    Ohira, Y.5
  • 31
    • 3142533071 scopus 로고    scopus 로고
    • Changes in gene expression associated with acclimation to constant temperatures and fluctuating daily temperatures in an annual killifish Austrofundulus limnaeus
    • Podrabsky, J.E. and G.N. Somero. 2004. Changes in gene expression associated with acclimation to constant temperatures and fluctuating daily temperatures in an annual killifish Austrofundulus limnaeus. Journal of Experimental Biology 207: 2237-2254.
    • (2004) Journal of Experimental Biology , vol.207 , pp. 2237-2254
    • Podrabsky, J.E.1    Somero, G.N.2
  • 33
    • 0033851893 scopus 로고    scopus 로고
    • The biomechanics and evolutionary significance of thermal acclimation in the common carp Cypinus carpio
    • Wakeling, J.M., N.J. Cole, K.M. Kemp and I.A. Johnston. 2000. The biomechanics and evolutionary significance of thermal acclimation in the common carp Cypinus carpio. American Journal of Physiology 279: 657-665
    • (2000) American Journal of Physiology , vol.279 , pp. 657-665
    • Wakeling, J.M.1    Cole, N.J.2    Kemp, K.M.3    Johnston, I.A.4
  • 34
    • 0019729164 scopus 로고
    • Temperature acclimation of Mg2+Ca2+ myofibrillar ATPase from a cold.Selective teleost, Salvelinus fontinalis: A compromise solution
    • Walesby, N. J. and I. A. Johnston. 1981. Temperature acclimation of Mg2+Ca2+ myofibrillar ATPase from a cold.selective teleost, Salvelinus fontinalis: A compromise solution. Experientia 37: 116-718.
    • (1981) Experientia , vol.37 , pp. 116-718
    • Walesby, N.J.1    Johnston, I.A.2
  • 35
    • 11144297719 scopus 로고    scopus 로고
    • Lipopolysaccharide regulates myostatin and MyoD independently of an increase in plasma cortisol in channel cat fish (Ictarus punctatus)
    • Weber, T.E., B.C. Small and B.G. Bosworth. 2005. Lipopolysaccharide regulates myostatin and MyoD independently of an increase in plasma cortisol in channel cat fish (Ictarus punctatus). Domestic Animal Endocrinology 28: 64-73.
    • (2005) Domestic Animal Endocrinology , vol.28 , pp. 64-73
    • Weber, T.E.1    Small, B.C.2    Bosworth, B.G.3
  • 36
    • 85072068365 scopus 로고
    • Enzymatic synthesis of acetylcholine by a serotonin containing neuron from helix
    • Wolfgong B. F., G. Steiner and C. Kuhne. 1974. Enzymatic synthesis of acetylcholine by a serotonin containing neuron from helix. Nature 252: 631-637.
    • (1974) Nature , vol.252 , pp. 631-637
    • Wolfgong, B.F.1    Steiner, G.2    Kuhne, C.3
  • 37
    • 0033373016 scopus 로고    scopus 로고
    • Control of pulmonary surfactant secretion from type II pneumocytes isolated from the lizard, Pogona vitticeps
    • Wood, P. G., O. V. Lopatko, S. Orgeig, J. R. Codd, and C. B. Daniels. 1999. Control of pulmonary surfactant secretion from type II pneumocytes isolated from the lizard, Pogona vitticeps. American Journal of Physiology 277: R1705-R1711.
    • (1999) American Journal of Physiology , vol.277 , pp. R1705-R1711
    • Wood, P.G.1    Lopatko, O.V.2    Orgeig, S.3    Codd, J.R.4    Daniels, C.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.