Transcortin
Vorhandene Strukturdaten: 2VDX, 2VDY
| Transcortin | ||
|---|---|---|
| Eigenschaften des menschlichen Proteins | ||
| Masse/Länge Primärstruktur | 383 Aminosäuren | |
| Bezeichner | ||
| Gen-Name | SERPINA6 | |
| Externe IDs | ||
| Inhibitorklassifikation | ||
| MEROPS | I04.954 | |
| Vorkommen | ||
| Homologie-Familie | Hovergen | |
| Übergeordnetes Taxon | Säugetiere[1] | |
| Orthologe | ||
| Mensch | Hausmaus | |
| Entrez | 866 | 12401 |
| Ensembl | ENSG00000170099 | ENSMUSG00000060807 |
| UniProt | P08185 | Q06770 |
| Refseq (mRNA) | NM_001756 | NM_007618 |
| Refseq (Protein) | NP_001747 | NP_031644 |
| Genlocus | Chr 14: 94.3 – 94.32 Mb | Chr 12: 103.65 – 103.66 Mb |
| PubMed-Suche | 866 | 12401
|
Transcortin (CBG, von engl.: Corticosteroid binding globulin) ist ein Plasmaprotein in Säugetieren, dessen Aufgabe die Bindung und der Transport von Glukokortikoiden und Progesteron im Blut ist. Es gehört zur Gruppe der α₁-Globuline. Die Produktion findet in der Leber statt und wird von Östrogen reguliert.
Transcortin hat eine hohe Affinität für 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 Molekülmasse von Transcortin beträgt 52000 Dalton, die normale Konzentration im Serum beträgt etwa 37 mg/l, kann sich aber in der Schwangerschaft oder nach Einnahme von Ovulationshemmern verdoppeln. Bei einer Leberzirrhose verringert sich die Konzentration.
Literatur
- 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. 244–251. doi:10.1016/j.jmb.2008.05.012. PMID 18513745.
- 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. 5153–5157. doi:10.1073/pnas.84.15.5153. PMC 298812 (freier Volltext). PMID 3299377.
- 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. 126–133. PMC 1918218 (freier Volltext). PMID 7912884.
- E. Edward Bittar, Neville Bittar: Molecular and Cellular Endocrinology. Elsevier, 1997, ISBN 1-55938-815-3, S. 238.
- Principles and Practice of Endocrinology and Metabolism. Lippincott Williams & Wilkins, 2001, ISBN 0-7817-1750-7, S. 712.
- Negi: Introduction To Endocrinology. PHI Learning Pvt., 2009, ISBN 978-81-203-3850-0, S. 268.
- 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. 58–68. doi:10.1210/jcem-53-1-58. PMID 7195404.
- 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. 1163–1166. doi:10.1210/jcem-25-9-1163. PMID 4284083.
- 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. E151–E155. doi:10.1210/jc.2011-2022. PMID 22013108.
- 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
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