Hsp70 response in pigs is affected by their Halothane genotypes after heat stress

Journal of Thermal Biology

Volumn 31, Issue 8, 2006, Pages 605-610

  Khazzaka, A ^a   Figwer, P ^a   Poirel, M T ^a   Serrar, M ^b   Franck, M ^a  

^a VETAGRO SUP   (France)

^b Laboratoire Texinfine   (France)

Author keywords

Calcium; Halothane genotype; Heat stress; Hsp70; Pigs

Indexed keywords

CALCIUM ION; HALOTHANE; HEAT SHOCK PROTEIN 70;

ANIMAL EXPERIMENT; ARTICLE; BLOOD ANALYSIS; CALCIUM HOMEOSTASIS; CONTROLLED STUDY; FEMALE; GENOTYPE; HEAT STRESS; MALE; NONHUMAN; REGULATORY MECHANISM; SWINE;

EID: 33750505214     PISSN: 03064565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jtherbio.2006.08.003     Document Type: Article

References (49)

1. Asea A., Kraeft S.K., Kurt-Jones E.A., Stevenson M.A., Chen L.B., Finberg R.W., Koo G.C., and Calderwood S.K. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6 (2000) 435-442
2. Bachelet M., Mariethoz E., Banzet N., Souil E., Pinot F., Polla C.Z., Durand P., Bouchaert I., and Polla B.S. Flow cytometry is a rapid and reliable method for evaluating heat shock protein 70 expression in human monocytes. Cell Stress Chaperon. 3 4 (1998) 273
3. Bukau B., and Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92 3 (1998) 351-366
4. Campisi J., Leem T.H., and Fleshner M. Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system. Cell Stress Chaperon. 8 3 (2003) 272-286
5. Chang Y.S., Lo C.W., Sun F.C., Chang M.D., and Lai Y.K. Differential expression of Hsp90 isoforms in geldanamycin-treated 9L cells. Biochem. Biophys. Res. Commun. 344 1 (2006) 37-44
6. Ding X.Z., Tsokos G.C., and Kiang J.G. Overexpression of HSP-70 inhibits the phosphorylation of HSF1 by activating protein phosphatase and inhibiting protein kinase C activity. Faseb J. 12 6 (1998) 451-459
7. Dressel R., and Gunther E. Heat-induced expression of MHC-linked HSP70 genes in lymphocytes varies at the single-cell level. J. Cell Biochem. 72 4 (1999) 558-569
8. Ducreux S., Zorzato F., Muller C., Sewry C., Muntoni F., Quinlivan R., Restagno G., Girard T., and Treves S. Effect of ryanodine receptor mutations on interleukin-6 release and intracellular calcium homeostasis in human myotubes from malignant hyperthermia-susceptible individuals and patients affected by central core disease. J. Biol. Chem. 279 42 (2004) 43838-43846
9. Duthie G.G., and Arthur J.R. Blood antioxidant status and plasma pyruvate kinase activity of halothane-reacting pigs. Am. J. Vet. Res. 48 2 (1987) 309-310
10. Eickelberg O., Geibel J., Seebach F., Giebisch G., and Kashgarian M. K(+)-induced HSP-72 expression is mediated via rapid Ca(2+) influx in renal epithelial cells. Am. J. Physiol. Renal Physiol. 281 2 (2001) F280-F287
11. Fleshner M., and Johnson J.D. Endogenous extra-cellular heat shock protein 72: releasing signal(s) and function. Int. J. Hyperthermia 21 5 (2005) 457-471
12. Franck M., Monin G., and Legault C. Les viandes PSE: un défaut majeur mais difficile à prévoir. Viandes et produits carnés 21 2 (2000) 103-107
13. Franck M., Svensson M., Von Seth G., Jossel A., Figwer Ph., Poirel M.T., and Monin G. Effect of stunning conditions on occurrence of PSE defects in hams of RN+/RN- pigs. Meat Sci. 64 4 (2003) 351-355
14. Guidon Jr. P.T., and Hightower L.E. Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins. Biochemistry 25 (1986) 3231-3239
15. Hunter-Lavin C., Davies E.L., Bacelar M.M., Marshall M.J., Andrew S.M., and Williams J.H. Hsp70 release from peripheral blood mononuclear cells. Biochem. Biophys. Res. Commun. 324 2 (2004) 511-517
16. Johnson J.D., Campisi J., Sharkey C.M., Kennedy S.L., Nickerson M., and Fleshner M. Adrenergic receptors mediate stress-induced elevations in extracellular Hsp72. J. Appl. Physiol. 99 5 (2005) 1789-1795
17. Johnson J.D., and Fleshner M. Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72. J. Leukoc. Biol. 79 3 (2006) 425-434
18. Kagaya A., Okada A., Jitsuiki H., Tawara Y., Inagaki M., Takebayashi M., Saeki T., Nishida A., Nakata Y., and Yamawaki S. Effect of heat stress on serotonin-2A receptor-mediated intracellular calcium mobilization in rat C6 glioma cells. J. Neural Transm. 107 8-9 (2000) 919-929
19. Kauffman R.G., van Laack R.L., Russell R.L., Pospiech E., Cornelius C.A., Suckow C.E., and Greaser M.L. Can pale, soft, exudative pork be prevented by postmortem sodium bicarbonate injection?. J. Anim. Sci. 76 12 (1998) 3010-3015
20. 2+ mobilization from inositol trisphosphate-insensitive pools. Toxicol. Appl. Pharmacol. 127 2 (1994) 173-181
21. i or activation of G proteins but not pHi or camp. Am. J. Physiol. (Cell Physiol. 36) 265 (1994) C104-C114
22. i and protects human epidermoid A-431 cells after chemical hypoxia. Toxicol. Appl. Pharmacol. 149 (1998) 185-194
23. Kiang J.G., and Tsokos G.C. Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacol. Ther. 80 2 (1998) 183-201 (Review)
24. i and tyrosine phosphorylation. J. Cell Biochem. 89 5 (2003) 1030-1043
25. Kiang J.G., Bowman P.D., Wu B.W., Hampton N., Kiang A.G., Zhao B., Juang Y.T., Atkins J.L., and Tsokos G.C. Geldanamycin treatment inhibits hemorrhage-induced increases in KLF6 and iNOS expression in unresuscitated mouse organs: role of inducible HSP70. J. Appl. Physiol. 97 2 (2004) 564-569
26. Kiang J.G., Bowman P.D., Lu X., Li Y., Ding X.Z., Zhao B., Juang Y.T., Atkins J.L., and Tsokos G.C. Geldanamycin prevents hemorrhage-induced ATP loss by overexpressing inducible HSP70 and activating pyruvate dehydrogenase. Am. J. Physiol. Gastrointest. Liver Physiol. 291 1 (2006) G117-G127
27. Kimura F., Itoh H., Ambiru S., Shimizu H., Togawa A., Yoshidome H., Ohtsuka M., Shimamura F., Kato A., Nukui Y., and Miyazaki M. Circulating heat-shock protein 70 is associated with postoperative infection and organ dysfunction after liver resection. Am. J. Surg. 187 (2004) 777-784
28. 2+ stores. Biochem. Cell Biol. 64 11 (1986) 1181-1189
29. 2+ in blood cells in malignant hyperthermia. Am. J. Physiol. 258 3 Pt 1 (1990) C495-C503
30. Klont R.E., Lambooy E., and van Logtestijnt J.G. Effect of preslaughter anesthesia on muscle metabolism and meat quality of pigs of different Halothane genotypes. J. Anim. Sci. 71 (1993) 1477-1485
31. 2+ homeostasis in rat ventricular myocytes subjected to simulated ischemia. Am. J. Physiol. Cell Physiol. 290 2 (2006) C583-C591
32. MacLennan D.H., Duff C., Zorzato F., Fujii J., Phillips M., Korneluk R.G., Frodis W., Britt B.A., and Worton R.G. Ryanodine receptor gene is a candidate for predisposition to malignant hyperthermia. Nature (London) 343 (1990) 559-561
33. Monin G. Stress d'abattage et qualités de la viande. Rec. Med. Vet. 164 (1988) 835-842
34. Monin G., Larzul C., Le Roy P., Culioli J., Mourot J., Rousset-Akrim S., Talmant A., Touraille C., and Sellier P. Effects of the halothane genotype and slaughter weight on texture of pork. J. Anim. Sci. 77 (1999) 408-415
35. Morimoto R.I. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12 (1998) 3788-3796
36. Nguyen V.T., Morange M., and Bensaude O. Protein denaturation during heat shock and related stress. Escherichia coli beta-galactosidase and Photinus pyralis luciferase inactivation in mouse cells. J. Biol. Chem. 264 (1989) 10487-10492
37. Njemini R., Demanet C., and Mets T. Comparison of two ELISAs for the determination of Hsp70 in serum. J. Immunol. Methods 306 (2005) 176-182
38. O'Brien P.J., Kalow B.I., Brown B.D., Lumsden J.H., and Jacobs R.M. Porcine malignant hyperthermia susceptibility: halothane-induced increase in cytoplasmic free calcium in lymphocytes. Am. J. Vet. Res. 50 1 (1989) 131-135
39. Oehler R., Pusch E., Zellner M., Dungel P., Hergovics N., Homoncik M., Eliasen M.M., Brabec M., and Roth E. Cell type-specific variations in the induction of hsp70 in human leukocytes by feverlike whole body hyperthermia. Cell Stress Chaperon. 6 4 (2001) 306-315
40. Pockley A.G., Wu R., Lemne C., Kiessling R., de Faire U., and Frostegard J. Circulating heat shock protein 60 is associated with early cardiovascular disease. Hypertension 36 2 (2000) 303-307
41. Reik T.R., Rempel W.E., McGrath C.J., and Addis P.B. Further evidence on the inheritance of halothane reaction in pigs. J. Anim. Sci. 57 (1983) 826-831
42. Riabowol K.T., Mizzen L.A., and Welch W.J. Heat shock is lethal to fibroblasts microinjected with antibodies against hsp70. Science 242 (1988) 433-436
43. Sayre R.N., Briskey E.J., and Hoekstra W.G. Effect of excitement, fasting and sucrose feeding on porcine muscle phosphorylase and postmortem glycolysis. J. Food Sci. 28 (1963) 472-477
44. Sei Y., Brandom B.W., Bina S., Hosoi E., Gallagher K.L., Wyre H.W., Pudimat P.A., Holman S.J., Venzon D.J., Daly J.W., and Muldoon S. Patients with malignant hyperthermia demonstrate an altered calcium control mechanism in B lymphocytes. Anesthesiology 97 5 (2002) 1052-1058
45. Sharma N., Okere I.C., Brunengraber D.Z., McElfresh T.A., King K.L., Sterk J.P., Huang H., Chandler M.P., and Stanley W.C. Regulation of pyruvate dehydrogenase activity and citric acid cycle intermediates during high cardiac power generation. J. Physiol. 562 Pt 2 (2005) 593-603
46. Shu C.W., Cheng N.L., Chang W.M., Tseng T.L., and Lai Y.K. Transactivation of hsp70-1/2 in geldanamycin-treated human non-small cell lung cancer H460 cells: involvement of intracellular calcium and protein kinase C. J. Cell Biochem. 94 6 (2005) 1199-1209
47. Smith C., and Bampton P.R. Inheritance of reaction to halothane anesthesia in pigs. Genet. Res. 29 (1977) 287-292
48. Tonner P.H., Scholz J., Richter A., Loscher W., Steinfath M., Wappler F., Wlaz P., Hadji B., Roewer N., and Schulte am Esch J. Alterations of inositol polyphosphates in skeletal muscle during porcine malignant hyperthermia. Br. J. Anaesth. 75 4 (1995) 467-471
49. Tsai M.J., and O'Malley B.W. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63 (1994) 451-486