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Pressing dominant negative (V53D) versus wild-type (WT) b-arrestin-1. There was no inhibitory effect of the dominant negative b-arrestin-1 on ERK1/2 activation, suggesting that, unlike several other GPCRs (Cottrell et al., 2009; Luttrell and Gesty-Palmer, 2010), the RXFP3/b-arrestin-1 interaction contributes little to ERK1/2 signaling (Kocan et al., 2014). Previous studies demonstrated internaliza
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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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Enta has important roles in pregnancy and parturition and is a major circulating hormone during pregnancy in all mammalian species acting on the pubic symphysis, cervix, uterus, vagina, and mammary glands. It also is responsible for many of the cardiovascular changes that occur during pregnancy (Debrah et al., 2006; Conrad, 2011). Relaxin causes increased flexibility and elasticity of the interpub
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Enta has important roles in pregnancy and parturition and is a major circulating hormone during pregnancy in all mammalian species acting on the pubic symphysis, cervix, uterus, vagina, and mammary glands. It also is responsible for many of the cardiovascular changes that occur during pregnancy (Debrah et al., 2006; Conrad, 2011). Relaxin causes increased flexibility and elasticity of the interpub
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S between RXFP3 and b-arrestins occur after administration of human relaxin-3 but not relaxin or the RXFP3 antagonist R3 (BD23?7)R/I5 as measured by real-time kinetic BRET between RXFP3-Rluc8 and a b-arrestin fusion protein (b-arrestin-1-Venus or b-arrestin-2-Venus). Preincubation with R3(BD2327)R/I5 completely inhibits the human relaxin-3 stimulated recruitment of b-arrestin-1 and b-arrestin-2 to
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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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Pressing dominant negative (V53D) versus wild-type (WT) b-arrestin-1. There was no inhibitory effect of the dominant negative b-arrestin-1 on ERK1/2 activation, suggesting that, unlike several other GPCRs (Cottrell et al., 2009; Luttrell and Gesty-Palmer, 2010), the RXFP3/b-arrestin-1 interaction contributes little to ERK1/2 signaling (Kocan et al., 2014). Previous studies demonstrated internaliza