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Relaxin 1
Symbol(s): RLN1
Locus: 9 qter -q12
EC number [1]
EntrezGene 6013
OMIM 179730
RefSeq [2]
UniProt [3]
Relaxin 2
Symbol(s): RLN2
Locus: 9 qter -q12
EC number [4]
EntrezGene 6019
OMIM 179740
RefSeq [5]
UniProt [6]
Relaxin 3
Symbol(s): RLN3
Locus: 19 p13.3
EC number [7]
EntrezGene 117579
OMIM 606855
RefSeq [8]
UniProt [9]

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.


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.


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.


The function of relaxin in humans is not clear, although it has several functions in animals.

In humans

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

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 by increasing matrix metalloproteinases.[3] It also enhances angiogenesis and is a potent renal vasodilator.


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.


Specific disorders related to relaxin have not been described, yet it has been suggested that it could be linked to scleroderma and to fibromyalgia.[4]


  2. Becker G, Hewitson T (2001). Relaxin and renal fibrosis. Kidney Int 59 (3): 1184-5.
  3. 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.
  4. 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.

External links


Target-derived NGF, BDNF, NT-3


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