The heterotrimeric GTP-binding protein, GS, modulates the Cl- conductance of rat parotid acinar secretory granules.
The heterotrimeric GTP-binding protein, GS, modulates the Cl- conductance of rat parotid acinar secretory granules.
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异三聚体 GTP 结合蛋白 GS 调节大鼠腮腺腺泡分泌颗粒的 Cl-电导。
DOI:
10.1006/bbrc.1997.7354
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发表时间:
1997
期刊:
影响因子:
--
通讯作者:
Dijulio,DH
中科院分区:
文献类型:
--
作者:
Watson,EL;Izutsu,KT;Jacobson,KL;Dijulio,DH
Gsαhas been reported to be present in rat parotid acinar secretory granule membrane (SGM) fractions. In the present study, we evaluated epitope orientation of Gsαon the secretory granule (SG) and the ability of Gsto modulate the Cl−conductance of isolated granules by measuring granule lysis. Gsαwas found to be associated with the cytoplasmic face of the SGM. Aluminum fluroide (AlF4−, 20μM Al3+and 10 mM F−) significantly increased granule lysis and this effect was blocked by GDPβS. Cholera toxin (5μg/ml) mimicked the effects of AlF4−on granule lysis, whereas pertussis toxin (0.5μg/ml) was without effect. GTPγS, however, reduced granule lysis in a concentration-dependent manner. The orientation of Gsαon the SGM as well as the effects of AlF4−and cholera toxin on granule lysis lends support for a role of Gsin the exocytotic process.