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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.
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 member and ancestral gene of the relaxin family of peptides, which includes the namesake hormone relaxin (designated 'H2 relaxin' in humans) which mediates peripheral actions during pregnancy and which was found to relax the pelvic ligament in guinea pigs almost a century ago.
The relaxin receptors are a subclass of four closely related G protein-coupled receptors (GPCR) that bind relaxin peptide hormones. [ 1 ] [ 2 ] Below is list of human relaxin receptors, their endogenous peptide hormones, and what downstream enzymes are activated or inhibited by the receptor.
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The insulin/IGF/relaxin family is a group of evolutionary related proteins which possess a variety of hormonal activities. [1] Family members in human include two subfamilies: 1) insulin and insulin-like growth factors [2] 2) relaxin family peptides: relaxins 1 and 2; relaxin 3; Leydig cell-specific insulin-like peptide (gene INSL3) [3]
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