The structure of relaxin-like peptide expressed in the boar testis and the implication in testicular function via its receptor LGR8

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This study has purified native relaxin-like peptide (RLF) from boar testes, and demonstrated for the first time at nay species that native RLF is secreted from the Leydig cells as a 12-kDa heterotrimeric proform structure consisting of an A-B-C-domain with site-specific disulphide bonds and full biological activity. RLF secreted from Leydig cells was released not only into the blood circulation, but also into the interstitial compartment and is transported into the seminiferous compartments, where its own receptor LGR8 was expressed, suggesting that RLF may function as a paracrine and an autocrine and/or endocrine factor on seminiferous germ cells and Leydig cells, respectively.