pubmed-article:3162730 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3162730 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:3162730 | lifeskim:mentions | umls-concept:C0034802 | lld:lifeskim |
pubmed-article:3162730 | lifeskim:mentions | umls-concept:C0007137 | lld:lifeskim |
pubmed-article:3162730 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:3162730 | lifeskim:mentions | umls-concept:C1518174 | lld:lifeskim |
pubmed-article:3162730 | lifeskim:mentions | umls-concept:C0037907 | lld:lifeskim |
pubmed-article:3162730 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
pubmed-article:3162730 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:3162730 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:3162730 | pubmed:dateCreated | 1988-5-23 | lld:pubmed |
pubmed-article:3162730 | pubmed:abstractText | The regulation of protein phosphorylation by sphingosine in A431 human epidermoid carcinoma cells was examined. Sphingosine is a competitive inhibitor of phorbol ester binding to protein kinase C (Ca2+/phospholipid-dependent enzyme) and potently inhibits phosphotransferase activity in vitro. Addition of sphingosine to intact A431 cells caused an inhibition of the phorbol ester-stimulated phosphorylation of two protein kinase C substrates, epidermal growth factor (EGF) receptor threonine 654 and transferrin receptor serine 24. We conclude that sphingosine inhibits the activity of protein kinase C in intact A431 cells. However, further experiments demonstrated that sphingosine-treatment of A431 cells resulted in the regulation of the EGF receptor by a mechanism that was independent of protein kinase C. First, sphingosine caused an increase in the threonine phosphorylation of the EGF receptor on a unique tryptic peptide. Second, sphingosine caused an increase in the affinity of the EGF receptor in A431 and in Chinese hamster ovary cells expressing wild-type (Thr654) and mutated (Ala654) EGF receptors. Sphingosine was also observed to cause an increase in the number of EGF-binding sites expressed at the surface of A431 cells. Examination of the time course of sphingosine action demonstrated that the effects on EGF binding were rapid (maximal at 2 mins) and were observed prior to the stimulation of receptor phosphorylation (maximal at 20 mins). We conclude that sphingosine is a potently bioactive molecule that modulates cellular functions by: 1) inhibiting protein kinase C; 2) stimulating a protein kinase C-independent pathway of protein phosphorylation; and 3) increasing the affinity and number of cell surface EGF receptors. | lld:pubmed |
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pubmed-article:3162730 | pubmed:language | eng | lld:pubmed |
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pubmed-article:3162730 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3162730 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3162730 | pubmed:month | Apr | lld:pubmed |
pubmed-article:3162730 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:3162730 | pubmed:author | pubmed-author:BellR MRM | lld:pubmed |
pubmed-article:3162730 | pubmed:author | pubmed-author:DavisR JRJ | lld:pubmed |
pubmed-article:3162730 | pubmed:author | pubmed-author:HannunY AYA | lld:pubmed |
pubmed-article:3162730 | pubmed:author | pubmed-author:GironèsNN | lld:pubmed |
pubmed-article:3162730 | pubmed:author | pubmed-author:FaucherMM | lld:pubmed |
pubmed-article:3162730 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3162730 | pubmed:day | 15 | lld:pubmed |
pubmed-article:3162730 | pubmed:volume | 263 | lld:pubmed |
pubmed-article:3162730 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3162730 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3162730 | pubmed:pagination | 5319-27 | lld:pubmed |
pubmed-article:3162730 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:3162730 | pubmed:meshHeading | pubmed-meshheading:3162730-... | lld:pubmed |
pubmed-article:3162730 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:3162730 | pubmed:articleTitle | Regulation of the epidermal growth factor receptor phosphorylation state by sphingosine in A431 human epidermoid carcinoma cells. | lld:pubmed |
pubmed-article:3162730 | pubmed:affiliation | Department of Biochemistry, University of Massachusetts Medical School, Worcester 01655. | lld:pubmed |
pubmed-article:3162730 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3162730 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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