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pubmed-article:8299418pubmed:abstractTextIntroduction of GTP gamma S or other non-metabolic analogues of GTP into permeabilized myeloid granulocytes (mast cells, eosinophils, neutrophils) constitutes a sufficient stimulus to induce exocytosis. We concentrate on mast cells. Exocytosis from cells permeabilized in isotonic glutamate solution proceeds in the absence of ATP and at exceedingly low levels (< 10(-9) M) of Ca2+. Mg2+ strongly promotes GTP gamma S-induced exocytosis but this requirement can be spared and then obliterated by lifting Ca2+ through 10(-7) to 10(-6) M. GTP provides only a modest support to exocytosis but becomes almost equipotent with GTP gamma S when Mg2+ is excluded. Ca2+ alone is unable to induce exocytosis. We envisage that the terminal stage of exocytosis (membrane fusion) requires activation of GE, a putative GTPase so far undefined as a molecular entity. Ca2+, presumed to act through a Ca(2+)-binding protein (CE, also undefined) supports exocytosis by promoting the exchange of guanine nucleotides on GE. In the absence of Mg2+ the onset of exocytosis is characterized by delays that have concentration-dependent (binding) and independent components. The latter are sensitive to the identity of the stimulating nucleotide (GTP < GTP gamma S < Gpp [NH]p) and may reflect activation of GE. The activation by Ca2+ and Mg2+ and the delays preceding onset of GTP gamma S-triggered exocytosis are reminiscent of the action of glucagon and Mg2+ in the activation of adenylate cyclase in hepatocyte membranes. The cell-physiological description predicts GE to be an alpha beta gamma heterotrimeric GTP-binding protein with functional similarity to GS.lld:pubmed
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pubmed-article:8299418pubmed:authorpubmed-author:GompertsB DBDlld:pubmed
pubmed-article:8299418pubmed:authorpubmed-author:LillieT HTHlld:pubmed
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pubmed-article:8299418pubmed:volume176lld:pubmed
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pubmed-article:8299418pubmed:pagination164-79; discussion 180-4lld:pubmed
pubmed-article:8299418pubmed:dateRevised2009-9-29lld:pubmed
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pubmed-article:8299418pubmed:year1993lld:pubmed
pubmed-article:8299418pubmed:articleTitleA cell-physiological description of GE, a GTP-binding protein that mediates exocytosis.lld:pubmed
pubmed-article:8299418pubmed:affiliationDepartment of Physiology, University College London, UK.lld:pubmed
pubmed-article:8299418pubmed:publicationTypeJournal Articlelld:pubmed
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pubmed-article:8299418pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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