pubmed-article:8299418 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8299418 | lifeskim:mentions | umls-concept:C0015283 | lld:lifeskim |
pubmed-article:8299418 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
pubmed-article:8299418 | lifeskim:mentions | umls-concept:C0678257 | lld:lifeskim |
pubmed-article:8299418 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:8299418 | pubmed:dateCreated | 1994-3-9 | lld:pubmed |
pubmed-article:8299418 | pubmed:abstractText | Introduction 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 |
pubmed-article:8299418 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8299418 | pubmed:language | eng | lld:pubmed |
pubmed-article:8299418 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8299418 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8299418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8299418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8299418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8299418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8299418 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8299418 | pubmed:issn | 0300-5208 | lld:pubmed |
pubmed-article:8299418 | pubmed:author | pubmed-author:GompertsB DBD | lld:pubmed |
pubmed-article:8299418 | pubmed:author | pubmed-author:LillieT HTH | lld:pubmed |
pubmed-article:8299418 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8299418 | pubmed:volume | 176 | lld:pubmed |
pubmed-article:8299418 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8299418 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8299418 | pubmed:pagination | 164-79; discussion 180-4 | lld:pubmed |
pubmed-article:8299418 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
pubmed-article:8299418 | pubmed:meshHeading | pubmed-meshheading:8299418-... | lld:pubmed |
pubmed-article:8299418 | pubmed:meshHeading | pubmed-meshheading:8299418-... | lld:pubmed |
pubmed-article:8299418 | pubmed:meshHeading | pubmed-meshheading:8299418-... | lld:pubmed |
pubmed-article:8299418 | pubmed:meshHeading | pubmed-meshheading:8299418-... | lld:pubmed |
pubmed-article:8299418 | pubmed:meshHeading | pubmed-meshheading:8299418-... | lld:pubmed |
pubmed-article:8299418 | pubmed:meshHeading | pubmed-meshheading:8299418-... | lld:pubmed |
pubmed-article:8299418 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8299418 | pubmed:articleTitle | A cell-physiological description of GE, a GTP-binding protein that mediates exocytosis. | lld:pubmed |
pubmed-article:8299418 | pubmed:affiliation | Department of Physiology, University College London, UK. | lld:pubmed |
pubmed-article:8299418 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8299418 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:8299418 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:8299418 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8299418 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8299418 | lld:pubmed |