Abstract:
:In this study we examined the influence on AlF4- and GTP gamma S on amylase secretion from alpha toxin permeabilized pancreatic acini. AlF4- only activates heterotrimeric G-proteins, whereas GTP gamma S activates both small ras-like GTP-binding proteins and heterotrimeric G-proteins (Kahn, R. A., J. Biol. Chem., 266, 15595-15597, 1991). GTP gamma S, but not AlF4-, significantly stimulated Ca2(+)-independent amylase secretion, suggesting that a small GTP-binding protein controls regulated exocytosis distal to the site of action of Ca2+. In contrast, both AlF4- and GTP gamma S modulated Ca(2+)-dependent amylase secretion. AlF4- and GTP gamma S stimulated the initial rapid, ATP-independent, phase of Ca(2+)-dependent secretion but inhibited the second slower sustained, ATP-dependent, phase of release. There were significant differences in the GTP gamma S requirements for the stimulation and inhibition of Ca(2+)-dependent amylase secretion, consistent with GTP gamma S activating separate heterotrimeric G-proteins to modulate each phase of the Ca(2+)-dependent secretory response. Our studies also indicated that neither G-protein is a member of the Gi/o class of heterotrimeric G-proteins.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Padfield PJ,Panesar Ndoi
10.1006/bbrc.1998.8350subject
Has Abstractpub_date
1998-04-17 00:00:00pages
332-6issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(98)98350-4journal_volume
245pub_type
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