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Relaxin is a protein hormone of about 6000 Da, [1] first described in 1926 by Frederick Hisaw. [2] [3]The relaxin family peptide hormones belong to the insulin superfamily and consists of seven peptides of high structural but low sequence similarity; relaxin-1 (RLN1), 2 (RLN2) and 3 (), and the insulin-like (INSL) peptides, INSL3, INSL4, INSL5 and INSL6.
All seven relaxin family peptide hormones are synthesized as pre-prohormones, and subsequently cleaved to form two chains stabilized by an intra-α-chain and two disulfide bonds. [5] Members of the human relaxin peptide family share a similar tertiary structure, composed of a β-chain, c-chain, and α-chain at their carboxyl-terminal.
Menstrual cycle The menstrual cycle is a series of natural changes in hormone production and the structures of the uterus and ovaries of the female reproductive system that makes pregnancy possible. The ovarian cycle controls the production and release of eggs and the cyclic release of estrogen and progesterone. The uterine cycle governs the preparation and maintenance of the lining of the ...
As a paracrine hormone, relaxin helps the non-pregnant uterus become ready for pregnancy. [23] Women's endometrium contains relaxin, which is an essential component that helps prepare the body for early pregnancy. [21] The endometrium is transformed into decidua during the early pregnancy maintenance procedure. [21]
Relaxin causes vasodilation by an indirect mechanism, where it inhibits the potent vasoconstrictors angiotensin II and endothelin. [9] In addition to vasodilation, the effects of relaxin are also seen in the kidneys, by significantly increasing creatinine clearance, [ 10 ] which is a measure of kidney function, as well as increased renal blood ...
Relaxin-3 is a neuropeptide that was discovered in 2001, [1] and which is highly conserved in species ranging from flies, fish, rodents and humans. [2]
Women are 4-5 times more likely to develop a clot during pregnancy and in the postpartum period than when they are not pregnant. [25] Hypercoagulability in pregnancy likely evolved to protect women from hemorrhage at the time of miscarriage or childbirth. In developing countries, the leading cause of maternal death is still hemorrhage. [25]
The alpha and beta subunits share approximately 25% sequence similarity, whereas the similarity between beta subunits is approximately 65%. [9]In mammals, four beta subunits have been described, called activin β A, activin β B, activin β C and activin β E.