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The heterotrimeric GTP-binding protein, GS, modulates the Cl- conductance of rat parotid acinar secretory granules.

作者信息

Watson E L, Izutsu K T, Jacobson K L, Dijulio D H

机构信息

Department of Oral Biology, University of Washington, Seattle, Washington 98195, USA.

出版信息

Biochem Biophys Res Commun. 1997 Sep 18;238(2):638-42. doi: 10.1006/bbrc.1997.7354.

DOI:10.1006/bbrc.1997.7354
PMID:9299566
Abstract

Gsalpha has been reported to be present in rat parotid acinar secretory granule membrane (SGM) fractions. In the present study, we evaluated epitope orientation of Gsalpha on the secretory granule (SG) and the ability of Gs to modulate the Cl- conductance of isolated granules by measuring granule lysis. Gsalpha was found to be associated with the cytoplasmic face of the SGM. Aluminum fluroide (AlF4-, 20 microM Al3+ and 10 mM F-) significantly increased granule lysis and this effect was blocked by GDPbetaS. Cholera toxin (5 microg/ml) mimicked the effects of AlF4- on granule lysis, whereas pertussis toxin (0.5 microg/ml) was without effect. GTPgammaS, however, reduced granule lysis in a concentration-dependent manner. The orientation of Gsalpha on the SGM as well as the effects of AlF4- and cholera toxin on granule lysis lends support for a role of Gs in the exocytotic process.

摘要

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