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热休克蛋白90在糖皮质激素受体信号通路中的分子伴侣作用 被引量:1

Mechanism of Heat Shock Protein 90 as Molecular Chaperone in Glucocorticoid Receptor Signal Pathway
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摘要 在应激反应时,下丘脑-垂体-肾上腺轴(HPA)在机体的调节方面起主要作用,而糖皮质激素(GC)是HPA轴中的关键物质,因此在考量急性和慢性应激反应时,GC及其受体(GR)的变化常常是首选的研究内容。而GR正常构象的形成、激活、功能发挥与其分子伴侣-热休克蛋白90(HSP90)关系密切。综述了HSP90的结构和功能、GC-GR信号通路中GC和GR的作用机制以及HSP90在GR信号通路中的分子伴侣作用。 In the stress response, the hypothalamus-pituitary-adrenal axis (HPA) plays a major role in the regulation of body, while the glucoeorticoid (GC) is the key material in HPA-axis. Therefore, when acute and chronic stress reactions are evaluated, GC and its receptor (GR) are often the first choice. Moreover, the formation of the normal conformation, activation and function of GR is closely related to heat shock protein 90 (HSP90). This article overviewed the structure and function of HSP90, the mechanism of GC and GR in GC-GR signal pathway, and the effect of HSP90 as molecular chaperone in glucoeorticoid receptor signal pathway.
出处 《家畜生态学报》 2009年第6期6-9,共4页 Journal of Domestic Animal Ecology
基金 973课题后续研究计划资助项目(2004CB117500) 动物营养学国家重点实验室开放课题资助项目(2004DA125184F0801)
关键词 热休克蛋白90 糖皮质激素受体 分子伴侣 Heat Shock Protein 90 Glucocorticoid Receptor molecular chaperone
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参考文献24

  • 1王选年,冯春花,刘远升,王新华,王水琴,潘耀谦.热应激时鸡糖皮质激素受体和热休克蛋白的变化[J].中国兽医杂志,2000,26(11):6-8. 被引量:5
  • 2Nollen E A, Morimoto R I. Chaperoning signaling pathways, molecular chaperones as stress-sensing"heat shock" proteins [J]. J Cell Sci, 2002, 115 (14), 2 809-2 816.
  • 3Kenji Y, Yoichiro F, Makoto H, et al. Cytosolie HSP90 Regulates the Heat Shock Response That Is Responsible for Heat Acclimation in Arabidopsis thaliana[J]. J Biol Chem, 2007, 282(52) : 37794-37804.
  • 4Christians E S, Yan L J, Benjamin I J. Heat shock factor 1 and heat shock proteins: critical partners in protection against acute cell injury. Crit Care Med, 2002, 30 ( S 1): 43-50.
  • 5Pearl L H, Prodromou C. Structure, function, and Mechanism of the HSP90 molecular chaperone[J]. Adv Protein Chem,2001, 59: 157-186.
  • 6Matsumoto S, Tanaka E, Nemoto T K, et al. Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone[J]. J Biol Chem, 2002, 277(38) : 34 959-34 966.
  • 7Katsuya T, Tsukahara F, Naruse M, et al. HSP90 inhibitors attenuate effect of dexamethasone on activated NF-kappaB and AP-1[J]. Life Sci, 2004, 74 (16), 1 981-1 992.
  • 8Felts S J, Owen BA, Nguyen P, et al. The HSP90-related protein TRAPI is a mitochondrial protein with distinct functional properties[J]. J Biol Chem, 2000, 275 (5):3 305-3 312.
  • 9Amere S S. HSP90 isoforms: functions, expression and clinical importance[J]. FEBS Letters, 2004, 562(1-3) : 11-15.
  • 10Heitzer M D, Wofl IM, Sanchez E R, et al. Glucocorticoid receptor physiology[J]. Reviews in Endocrine & Metabolic Disorders, 2007(8): 321-330.

二级参考文献12

  • 1徐仁宝,谭金兴.糖皮质激素对糖皮质激素受体的调节——Ⅱ.大鼠肝、脑、脾的研究[J].中国科学(B辑),1989(4):399-403. 被引量:7
  • 2徐仁宝.去肾上腺大鼠肝胞液糖皮质激素受体测定[J].第二军医大学学报,1981,2(3):161-165.
  • 3WelechWJ.Mammalianstressresponsecellphysiology,structure/functionofstressproteinsandimplicationsformedicineanddisease[J].PhysicRev,1972,72:1062-1081.
  • 4ItohH,TashimaY.Thestress(heatshock)proteins[J].IntJBiochem,1991,23:1185.
  • 5SahchezER,ToftDO,SchlesingerMJ,etal.Evidencethatthe90-KDaphosphoproteinassociatedwiththeuntransformedL-cellglucocorticoidreceptorisamurineheatshockprotein[J].JBiolChem,1985,260:12398-12401.
  • 6HodardKJ,DistelhorstCW.Evidenceforintracellularoftheglucocorticoidreceptorwiththe90-KDaheatshockprotein[J].JBiolChem,1988,263:3474-3481.
  • 7SahchezER,HirstM,ScherrorLC,etal.Hormone-freemouseglucocorticoidreceptorsoverexpressedinChineseHamsterOvarycellsarelocalizedtothenucleusandareassociatedwithbothHSP70andHSP90[J].JBiolChej.1990,265:20123-20130.
  • 8LaemmliUK.CleavageofstructuralproteinsduringtheassemblyofbacterophageT4[J].Nature,1970,227(15):680-685.
  • 9WelthWJ,SuhanJP.Cellularandbiochemicaleventsinmammaliancellsduringandafterrecoveryfromphysiologicalstress[J].JCellBiol,1986,103:2035-2052.
  • 10PelkgamHRB.HSP70acceleratestherecoveryofnucleolarmorphologyafterheatshock[J].EMBOJ.1984,3:3095-3100.

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