| pubmed-article:8314849 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C0040688 | lld:lifeskim |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C0332197 | lld:lifeskim |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:8314849 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8314849 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8314849 | pubmed:dateCreated | 1993-7-27 | lld:pubmed |
| pubmed-article:8314849 | pubmed:abstractText | The ectodomain of proTGF-alpha, a membrane-anchored growth factor, is converted into soluble TGF-alpha by a regulated cellular proteolytic system that recognizes proTGF-alpha via the C-terminal valine of its cytoplasmic tail. In order to define the biochemical components involved in proTGF-alpha cleavage, we have used cells permeabilized with streptolysin O (SLO) that have been extensively washed to remove cytosol. PMA, acting through a Ca(2+)-independent protein kinase C, activates cleavage as efficiently in permeabilized cells as it does in intact cells. ProTGF-alpha cleavage is also stimulated by GTP gamma S through a mechanism whose pharmacological properties suggest the involvement of a heterotrimeric G protein acting upstream of the PMA-sensitive Ca(2+)-independent protein kinase C. Activated proTGF-alpha cleavage is dependent on ATP hydrolysis, appears not to require vesicular traffic, and acts specifically on proTGF-alpha that has reached the cell surface. These results indicate that proTGF-alpha is cleaved from the cell surface by a regulated system whose signaling, recognition, and proteolytic components are retained in cells devoid of cytosol. | lld:pubmed |
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| pubmed-article:8314849 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8314849 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8314849 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8314849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8314849 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8314849 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8314849 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:8314849 | pubmed:author | pubmed-author:MassaguéJJ | lld:pubmed |
| pubmed-article:8314849 | pubmed:author | pubmed-author:PandiellaAA | lld:pubmed |
| pubmed-article:8314849 | pubmed:author | pubmed-author:BosenbergM... | lld:pubmed |
| pubmed-article:8314849 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8314849 | pubmed:volume | 122 | lld:pubmed |
| pubmed-article:8314849 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8314849 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8314849 | pubmed:pagination | 95-101 | lld:pubmed |
| pubmed-article:8314849 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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