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Corticosteroid-binding globulin

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==Introduction==
==Introduction==
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Corticosteroid-binding globulin is a blood plasma protein 50 to 60 kDa in size <ref>PMID:13395526 </ref>,<ref>PMID:7074030 </ref>.
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Corticosteroid-binding globulin (CBG) is a blood plasma protein 50 to 60 kDa in size <ref>PMID:13395526 </ref>,<ref>PMID:7074030 </ref>. Although it is a member of the serine protease inhibitor (SERPIN) structural family, it does not have any known intrinsic serine protease inhibitor activity <ref>PMID:3143075 </ref>. Its physiological function is conventionally thought to be the transport of the weakly water-soluble hormone, cortisol, throughout the circulation <ref>PMID:13395526 </ref>,<ref>PMID:7074030 </ref>. Structural studies of native rat CBG <ref>PMID:17644521 </ref> and a cleaved human CBG-antitrypsin chimera <ref>PMID:18513745 </ref> have corroborated earlier biochemical studies showing that cortisol binds to CBG with a one-to-one stoichiometry. Additionally, CBG is believed to buffer the concentration of free cortisol in the blood, keeping the level constant despite its pulsatile secretion pattern.

Revision as of 20:35, 7 June 2012


Introduction

Corticosteroid-binding globulin (CBG) is a blood plasma protein 50 to 60 kDa in size [1],[2]. Although it is a member of the serine protease inhibitor (SERPIN) structural family, it does not have any known intrinsic serine protease inhibitor activity [3]. Its physiological function is conventionally thought to be the transport of the weakly water-soluble hormone, cortisol, throughout the circulation [4],[5]. Structural studies of native rat CBG [6] and a cleaved human CBG-antitrypsin chimera [7] have corroborated earlier biochemical studies showing that cortisol binds to CBG with a one-to-one stoichiometry. Additionally, CBG is believed to buffer the concentration of free cortisol in the blood, keeping the level constant despite its pulsatile secretion pattern.



References

  1. ↑ WESTPHAL U. Steroid-protein interactions. III. Spectrophotometric demonstration of interaction between proteins and progesterone, deoxycorticosterone and cortisol. Arch Biochem Biophys. 1957 Jan;66(1):71-90. PMID:13395526
  2. ↑ Mickelson KE, Harding GB, Forsthoefel M, Westphal U. Steroid-protein interactions. Human corticosteroid-binding globulin: characterization of dimer and electrophoretic variants. Biochemistry. 1982 Feb 16;21(4):654-60. PMID:7074030
  3. ↑ Pemberton PA, Stein PE, Pepys MB, Potter JM, Carrell RW. Hormone binding globulins undergo serpin conformational change in inflammation. Nature. 1988 Nov 17;336(6196):257-8. PMID:3143075 doi:http://dx.doi.org/10.1038/336257a0
  4. ↑ WESTPHAL U. Steroid-protein interactions. III. Spectrophotometric demonstration of interaction between proteins and progesterone, deoxycorticosterone and cortisol. Arch Biochem Biophys. 1957 Jan;66(1):71-90. PMID:13395526
  5. ↑ Mickelson KE, Harding GB, Forsthoefel M, Westphal U. Steroid-protein interactions. Human corticosteroid-binding globulin: characterization of dimer and electrophoretic variants. Biochemistry. 1982 Feb 16;21(4):654-60. PMID:7074030
  6. ↑ Klieber MA, Underhill C, Hammond GL, Muller YA. Corticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered release. J Biol Chem. 2007 Oct 5;282(40):29594-603. Epub 2007 Jul 19. PMID:17644521 doi:10.1074/jbc.M705014200
  7. ↑ Zhou A, Wei Z, Stanley PL, Read RJ, Stein PE, Carrell RW. The S-to-R transition of corticosteroid-binding globulin and the mechanism of hormone release. J Mol Biol. 2008 Jun 27;380(1):244-51. Epub 2008 May 14. PMID:18513745 doi:10.1016/j.jmb.2008.05.012

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