____ _ _ _ _
| _ \ ___ | |_ (_) _ __ ___ __| | (_) __ _
| |_) | / _ \ | __| | | | '_ \ / _ \ / _| | | | / _ |
| _ < | __/ | |_ | | | |_) | | __/ | (_| | | | | (_| |
|_| \_\ \___| \__| |_| | .__/ \___| \__,_| |_| \__,_|
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Transcortin
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
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Transcortin (CBG, von engl.: Corticosteroid binding globulin) ist ein Plasmaprotein in SΓ€ugetieren, dessen Aufgabe die Bindung und der Transport von Glukokortikoiden und Progesteron im Blut ist. Es gehΓΆrt zur Gruppe der Ξ±β-Globuline. Die Produktion findet in der Leber statt und wird von Γstrogen reguliert.
Transcortin hat eine hohe AffinitΓ€t fΓΌr Cortisol, von dem vermutet wird, dass es nur in seiner nicht an Transcortin gebundenen Form biologisch aktiv ist. Etwa 75 % des Cortisols im Kreislauf sind an Transcortin gebunden.
Die MolekΓΌlmasse von Transcortin betrΓ€gt 52000 Dalton, die normale Konzentration im Serum betrΓ€gt etwa 37 mg/l, kann sich aber in der Schwangerschaft oder nach Einnahme von Ovulationshemmern verdoppeln. Bei einer Leberzirrhose verringert sich die Konzentration.
Contents
β’ Literatur
β’ Einzelnachweise
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
Literatur
β’ A. Zhou, Z. Wei, P. L. Stanley, R. J. Read, P. E. Stein, R. W. Carrell: The S-to-R transition of corticosteroid-binding globulin and the mechanism of hormone release. In: J. Mol. Biol. 380 (1), June 2008, S. 244β251. doi:10.1016/j.jmb.2008.05.012. PMID 18513745.
β’ G. L. Hammond, C. L. Smith, I. S. Goping, D. A. Underhill, M. J. Harley, J. Reventos, N. A. Musto, G. L. Gunsalus, C. W. Bardin: Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors. In: Proc Natl Acad Sci U S A. 84 (15), Aug 1987, S. 5153β5157. doi:10.1073/pnas.84.15.5153. PMC 298812 (freier Volltext). PMID 3299377.
β’ B. C. Byth, G. D. Billingsley, D. W. Cox: Physical and genetic mapping of the serpin gene cluster at 14q32.1: allelic association and a unique haplotype associated with alpha 1-antitrypsin deficiency. In: Am J Hum Genet. 55 (1), Jul 1994, S. 126β133. PMC 1918218 (freier Volltext). PMID 7912884.
β’ E. Edward Bittar, Neville Bittar: Molecular and Cellular Endocrinology. Elsevier, 1997, ISBN 1-55938-815-3, S. 238.
β’ Principles and Practice of Endocrinology and Metabolism. Lippincott Williams & Wilkins, 2001, ISBN 0-7817-1750-7, S. 712.
β’ Negi: Introduction To Endocrinology. PHI Learning Pvt., 2009, ISBN 978-81-203-3850-0, S. 268.
β’ J. F. Dunn, B. C. Nisula, D. Rodbard: Transport of steroid hormones: binding of 21 endogenous steroids to both testosterone-binding globulin and corticosteroid-binding globulin in human plasma. In: The Journal of Clinical Endocrinology and Metabolism. 53 (1), July 1981, S. 58β68. doi:10.1210/jcem-53-1-58. PMID 7195404.
β’ B. U. Musa, U. S. Seal, R. P. Doe: Elevation of certain plasma proteins in man following estrogen administration: a dose-response relationship. In: J. Clin. Endocrinol. Metab. 25 (9), September 1965, S. 1163β1166. doi:10.1210/jcem-25-9-1163. PMID 4284083.
β’ D. J. Torpy, B. A. Lundgren, J. T. Ho, J. G. Lewis, H. S. Scott, V. Mericq: CBG Santiago: a novel CBG mutation. In: J. Clin. Endocrinol. Metab. 97 (1), January 2012, S. E151βE155. doi:10.1210/jc.2011-2022. PMID 22013108.
β’ M. I. Rosen, S. M. Shnider, G. Levinson, S. C. Hughes: Shnider and Levinson's anesthesia for obstetrics. Lippincott Williams & Wilkins, Hagerstown, MD 2002, ISBN 0-683-30665-0, S. 13.
Einzelnachweise