Relaxin
Relaxin 1 | |
---|---|
Identifiers | |
Symbol | RLN1 |
Entrez | 6013 |
HUGO | 10026 |
OMIM | 179730 |
Other data | |
Locus | Chr. 9 qter-q12 |
Relaxin 2 | |
---|---|
Identifiers | |
Symbol | RLN2 |
Entrez | 6019 |
HUGO | 10027 |
OMIM | 179740 |
Other data | |
Locus | Chr. 9 qter-q12 |
Relaxin 3 | |
---|---|
Identifiers | |
Symbol | RLN3 |
Entrez | 117579 |
HUGO | 17135 |
OMIM | 606855 |
Other data | |
Locus | Chr. 19 p13.3 |
WikiDoc Resources for Relaxin |
Articles |
---|
Most recent articles on Relaxin |
Media |
Evidence Based Medicine |
Clinical Trials |
Ongoing Trials on Relaxin at Clinical Trials.gov Clinical Trials on Relaxin at Google
|
Guidelines / Policies / Govt |
US National Guidelines Clearinghouse on Relaxin
|
Books |
News |
Commentary |
Definitions |
Patient Resources / Community |
Directions to Hospitals Treating Relaxin Risk calculators and risk factors for Relaxin
|
Healthcare Provider Resources |
Causes & Risk Factors for Relaxin |
Continuing Medical Education (CME) |
International |
|
Business |
Experimental / Informatics |
Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1] Phone:617-632-7753
Overview
Relaxin is a peptide hormone that was first described in 1926 by Frederick Hisaw.[1][2]
Different forms of relaxin have been described: relaxin 1, 2, and 3.
Production
In the female, it is produced by the corpus luteum of the ovary, the breast and, during pregnancy, also by the placenta, chorion, and decidua.
In the male, relaxin is produced in the testes.
Structure
Structurally, relaxin is a heterodimer of two peptide chains of 24 and 29 amino acids that are linked by disulfide bridges and it appears related to insulin. Relaxin is produced from its prohormone, “pro-relaxin”, by splitting off one additional peptide chain.
Function
In women relaxin levels rise after ovulation as a result of its production by the corpus luteum. In the absence of pregnancy its level declines at menstruation. During the first trimester of pregnancy levels rise and additional relaxin is produced by the decidua. Relaxin's role or necessity in human pregnancy remains under investigation, as in humans its peak is reached during the first trimester, not toward the end of pregnancy.
In animals relaxin widens the pubic bone and facilitates labor, it also softens the cervix (cervical ripening), and relaxes the uterine musculature. Thus, for a long time, relaxin was looked at as a pregnancy hormone. However, its significance may reach much further. Relaxin affects collagen metabolism, inhibiting collagen synthesis and enhancing its breakdown via transactivation of nitric oxide synthases which in turn upregulates matrix metalloproteinases and downregulates TGF-β by inhibiting phosphorylation of Smad2.[3][4] In addition to its antifibrotic effects, relaxin also exhibits vasodilatory actions by increasing NO which results in release of vasoactive peptide ET-1 (1-32) that acts on the ETB receptors to cause NO-dependent vasorelaxation.[5] It also enhances angiogenesis and is a potent renal vasodilator.
Receptors
Relaxin interacts with the relaxin receptor LGR7 (RXFP1) and LGR8 (RXFP2) which belong to the G-protein-coupled receptor superfamily. They contain a heptahelical transmembrane domain and a large glycosylated ectodomain, distantly related to the receptors for the glycoproteohormones, such as the LH-receptor or FSH-receptor.
Relaxin receptors have been found in the heart, smooth muscle, the connective tissue, and central and autonomous nervous system.
Disorders
Specific disorders related to relaxin have not been described, yet it has been suggested that it could be linked to scleroderma and to fibromyalgia.[6]
References
- ↑ http://www.time.com/time/magazine/article/0,9171,796530,00.html
- ↑ Becker G, Hewitson T (2001). "Relaxin and renal fibrosis". Kidney Int. 59 (3): 1184–5. PMID 11231378.
- ↑ Mookerjee I, Solly N, Royce S, Tregear G, Samuel C, Tang M (2006). "Endogenous relaxin regulates collagen deposition in an animal model of allergic airway disease". Endocrinology. 147 (2): 754–61. PMID 16254028.
- ↑ Bathgate, RA.; Halls, ML.; van der Westhuizen, ET.; Callander, GE.; Kocan, M.; Summers, RJ. (2013). "Relaxin family peptides and their receptors". Physiol Rev. 93 (1): 405–80. doi:10.1152/physrev.00001.2012. PMID 23303914. Unknown parameter
|month=
ignored (help) - ↑ Jeyabalan, A.; Shroff, SG.; Novak, J.; Conrad, KP. (2007). "The vascular actions of relaxin". Adv Exp Med Biol. 612: 65–87. doi:10.1007/978-0-387-74672-2_6. PMID 18161482.
- ↑ Van Der Westhuizen E, Summers R, Halls M, Bathgate R, Sexton P (2007). "Relaxin receptors--new drug targets for multiple disease states". Curr Drug Targets. 8 (1): 91–104. PMID 17266534.
External links
- Human Protein Reference Database
- Relaxin at the US National Library of Medicine Medical Subject Headings (MeSH)