【摘 要】
：
The dimeric Gh protein is comprised of α and β subunits and known to be associated with FSH-, oxytocin-, or epinephrine-receptors/functions in their respective target cells.After establishing the FSH-
【机 构】
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Department of Physical Medicine and Rehabilitation, Taipei Medical University Hospital Taiwan
【出 处】
：
BIT`s 2nd Annual World Congress of Endobolism-2012(2012第二届内分
论文部分内容阅读
The dimeric Gh protein is comprised of α and β subunits and known to be associated with FSH-, oxytocin-, or epinephrine-receptors/functions in their respective target cells.After establishing the FSH-induced activation of Gαh/phospholipase C (PLC)-δ1 pathway in rat Sertoli cells (rSCs), we have attempted to identify a possible Gαh-coupled novel FSH receptor (FSH-R).A protein with approximately 240-kDa molecular mass was co-immunoprecipitated with Gαh in the fractionated membrane proteins of rSCs.The protein was identified as myosin heavy polypeptide 9 (MyH9) by mass spectrometric analysis and immuno-blotting.In addition, immuno-precipitation analysis reveals that MyH9 is constitutively associated with the classical Gs-coupled FSH-R and inactive GDP-bound Gαh at resting state of rSCs, but did not interact with FSH directly as judged by Far-Western analysis.Upon stimulation by higher levels of extracellular FSH (1000 IU/liter), the classical FSH-R induces phosphorylation of MyH9, dissociation of active GTP-bound Gαh from FSH-R-MyH9 complexes, and elicitation of Gαh/PLC-δ1 pathway-dependent Ca2+-influx in rSCs.The specific inhibition of MyH9 ATPase activity with Blebbistatin dose-dependently suppressed the FSH-induced Gαh/PLC-δ1 signaling and Ca2+-influx, but not intracellular cAMP accumulation, implying that MyH9 mediates FSH-induced activation of Gαh/PLC-δ1/IP 3/Ca2+-influx pathway in rSCs.The filament protein MyH9 constitutively forms a ternary complex with FSH-R and inactive GDP-bound Gαh.At higher FSH levels, this ternary complex executes an alternative signaling of classical Gs-coupled FSH-R through activating a Gs/cAMP-independent,Gαh/PLC--δ1 pathway in rat Sertoli cells.
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