title: Growth hormone attenuates branchial HSP70 expression in silver sea bream.
abstract: In this study the effects of growth hormone (GH) on silver sea bream branchial heat-shock protein 70 (HSP70) expression was investigated using in-vivo and in-vitro experiments. For in-vivo experiments, sea bream were administered recombinant bream GH or the GH secretagogue hexarelin. Pituitary levels of GH were unchanged in fish administered exogenous GH but decreased on hexarelin administration, in comparison with saline controls. Levels of HSP70 were measured using immunoanalysis and it was found that both GH and hexarelin administration caused a significant decrease in branchial HSP70 abundance. For in-vitro analysis, branchial filaments were exposed to a range of GH concentrations (1, 10, and 100 ng/ml) and it was found that HSP70 levels were significantly lowered in all cases. This study adds to the growing body of evidence surrounding the importance of hormones in regulating heat-shock protein expression in fish.
authors.affiliation: Department of Biology, The Chinese University of Hong Kong, Shatin, NT, Hong Kong SAR, China.
authors.forename: Eddie E
authors.initials: EE
authors.lastname: Deane
authors.forename: Norman Y S
authors.initials: NY
authors.lastname: Woo
mesh_terms: D000818:Animals; D001934:Branchial Region / Q000187:drug effects / Q000378:metabolism; D029941:Fish Proteins / Q000378:metabolism* / Q000494:pharmacology; D005880:Gills / Q000187:drug effects / Q000378:metabolism; D013006:Growth Hormone / Q000378:metabolism / Q000494:pharmacology*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D007150:Immunohistochemistry; D066298:In Vitro Techniques; D009842:Oligopeptides / Q000494:pharmacology; D010902:Pituitary Gland / Q000378:metabolism; D011994:Recombinant Proteins / Q000494:pharmacology; D021541:Sea Bream / Q000378:metabolism*
chemical_list: D029941:Fish Proteins; D018840:HSP70 Heat-Shock Proteins; D009842:Oligopeptides; D011994:Recombinant Proteins; C086184:hexarelin; D013006:Growth Hormone
references.citation: Biochem Biophys Res Commun. 2006 Apr 21;342(4):1077-82
references.pmid: 16513086
references.citation: Nature. 1970 Aug 15;227(5259):680-5
references.pmid: 5432063
references.citation: Anal Biochem. 1976 May 7;72:248-54
references.pmid: 942051
references.citation: Am J Physiol Regul Integr Comp Physiol. 2004 Nov;287(5):R1054-63
references.pmid: 15242828
references.citation: Gene. 2002 Aug 7;295(2):173-83
references.pmid: 12354651
references.citation: Crit Rev Toxicol. 1993;23(1):49-75
references.pmid: 8471160
references.citation: Mar Biotechnol (NY). 2002 Mar;4(2):193-205
references.pmid: 14961280
references.citation: Gen Comp Endocrinol. 1997 Oct;108(1):35-44
references.pmid: 9378272
references.citation: Gen Comp Endocrinol. 2001 Oct;124(1):97-105
references.pmid: 11703075
references.citation: Ann N Y Acad Sci. 2005 Apr;1040:293-6
references.pmid: 15891045
references.citation: Mol Cell Endocrinol. 2006 Oct 19;259(1-2):57-64
references.pmid: 16989943
references.citation: Annu Rev Pharmacol Toxicol. 1997;37:297-326
references.pmid: 9131255
references.citation: Ann N Y Acad Sci. 2005 Apr;1040:288-92
references.pmid: 15891044
references.citation: Science. 1992 Nov 6;258(5084):995-8
references.pmid: 1359644
references.citation: Mol Endocrinol. 1993 Jan;7(1):4-11
references.pmid: 8446107
references.citation: Nature. 1989 Sep 14;341(6238):125-30
references.pmid: 2528694
references.citation: J Endocrinol. 1999 Jun;161(3):413-21
references.pmid: 10333544
references.citation: Nature. 1992 Jan 2;355(6355):33-45
references.pmid: 1731198