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S of relaxin family peptides and their receptors have been extensively reviewed (Ivell and Anand-Ivell, 2009; Smith et al., 2011; Bathgate et al., 2013a). In particular, the role of relaxin in female and male reproductive physiology have been well studied (Sherwood, 1994, 2004; Bathgate et al., 2013a, 2006c). For this reason, only brief overviews will be given here. A. Relaxin and Relaxin Family P
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S of relaxin family peptides and their receptors have been extensively reviewed (Ivell and Anand-Ivell, 2009; Smith et al., 2011; Bathgate et al., 2013a). In particular, the role of relaxin in female and male reproductive physiology have been well studied (Sherwood, 1994, 2004; Bathgate et al., 2013a, 2006c). For this reason, only brief overviews will be given here. A. Relaxin and Relaxin Family P
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De Receptor 3 after Activation by the Biased Ligands Human Relaxin and R3(BD23?7)R/I5. The different signaling patterns observed with the biased ligands human relaxin and R3(BD23?7)R/I5 (see section III.C.2 for details) were also reflected in a distinct pattern of G protein coupling inHalls et al.BRET studies (Kocan et al., 2014). The biased ligands coupled only with Gai2 or GaoB, and the signal w
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Rences may relate to different colocalization of receptors and G proteins in particular cell types. More recent studies used BRET to investigate ligand-induced interactions between RXFP3-RLuc8 and G proteins (Gg2-Venus) in live cells. Similar to previous studies, treatment of CHO-RXFP3-RLuc8 cells with human relaxin-3 caused activation of Gai2, GaoA, and GaoB, but also revealed an interaction betw
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Of RXFP1 in the SFO and OVLT that are activated by relaxin to cause a reduction in plasma osmolality (Sunn et al., 2002). This effect in ratsis associated with increased serum relaxin levels during the second half of pregnancy (Sherwood et al., 1980; Lindheimer et al., 1989) and is absent in pregnant rats that have undergone ovariectomy or treatment with relaxin antibodies (Novak et al., 2001). Si
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Rophysiometer, where pretreatment of CHORXFP3 cells with PTX strongly inhibited the extracellular acidification rate, suggesting that the signaling pathways activated by RXFP3 were downstream of Gai/o (van der Westhuizen et al., 2005). As for RXFP1 and RXFP2, PTX-insensitive G proteins were used to determine the particular G proteins involved (van der Westhuizen, 2008). PTX pretreatment completed
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Rophysiometer, where pretreatment of CHORXFP3 cells with PTX strongly inhibited the extracellular acidification rate, suggesting that the signaling pathways activated by RXFP3 were downstream of Gai/o (van der Westhuizen et al., 2005). As for RXFP1 and RXFP2, PTX-insensitive G proteins were used to determine the particular G proteins involved (van der Westhuizen, 2008). PTX pretreatment completed
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T treatment with only the cognate ligand human relaxin-3 causes RXFP3 to undergo classic b-arrestin ependent internalization. The detailed mechanisms involved in RXFP3 internalization, phosphorylation, and recycling/ degradation all remain to be determined. D. Relaxin Family Peptide Receptor 4 1. G Proteins That Couple to Relaxin Family Peptide Receptor 4. There is currently a paucity of informati