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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1983-9-9
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pubmed:abstractText |
Calcium-activated neutral protease has been purified partially from A431-V1 cells, a high passage variant of human epidermoid carcinoma A431 cells having extraordinary activity of this protease. This activity cleaves Mr = 160,000 epidermal growth factor receptors, converting them to a Mr = 145,000 form in detergent-treated membrane preparations, but not in intact cells or membrane vesicles. Properties of this activity, including molecular weight, resemble those of previously described Ca2+-activated neutral proteases. A431-V1 cell Ca2+-activated neutral protease action on epidermal growth factor receptors required 0.5 mM Ca2+ for half-maximal activity and the optimal pH was 6.5. Degradation was inhibited completely by Ca2+ chelators (EDTA and ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid) and sulfhydryl group specific reagents (iodoacetate and 5,5'-dithiobis-(2-nitrobenzoic acid] and was inhibited partially by leupeptin. Degradation of epidermal growth factor receptors by Ca2+-activated neutral protease or trypsin was compared in intact cells, membrane vesicles, detergent-solubilized membranes, and membranes subjected to hypotonic shock in solutions containing protease. Results support the hypothesis that protease-susceptible domains of epidermal growth factor receptors, including the Ca2+-activated neutral protease-sensitive domain, are located on the cytosolic surface. The localization of Ca2+-activated neutral protease in A431-V1 cells is entirely cytosolic, making it available in cells to the protease-susceptible site on epidermal growth factor receptor substrates.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
258
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9254-61
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6307999-Animals,
pubmed-meshheading:6307999-Calcium,
pubmed-meshheading:6307999-Calpain,
pubmed-meshheading:6307999-Cations, Divalent,
pubmed-meshheading:6307999-Cell Line,
pubmed-meshheading:6307999-Endopeptidases,
pubmed-meshheading:6307999-Fibroblasts,
pubmed-meshheading:6307999-Humans,
pubmed-meshheading:6307999-Membranes,
pubmed-meshheading:6307999-Molecular Weight,
pubmed-meshheading:6307999-Receptor, Epidermal Growth Factor,
pubmed-meshheading:6307999-Receptors, Cell Surface,
pubmed-meshheading:6307999-Teratoma
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pubmed:year |
1983
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pubmed:articleTitle |
Calcium-mediated degradation of epidermal growth factor receptor in dislodged A431 cells and membrane preparations.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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