| pubmed-article:2244923 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2244923 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:2244923 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:2244923 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:2244923 | lifeskim:mentions | umls-concept:C0055278 | lld:lifeskim |
| pubmed-article:2244923 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2244923 | pubmed:dateCreated | 1990-12-28 | lld:pubmed |
| pubmed-article:2244923 | pubmed:abstractText | The benzophenanthridine alkaloid chelerythrine is a potent, selective antagonist of the Ca++/phospholopid-dependent protein kinase (Protein kinase C: PKC) from the rat brain. Half-maximal inhibition of the kinase occurs at 0.66 microM. Chelerythrine interacted with the catalytic domain of PKC, was a competitive inhibitor with respect to the phosphate acceptor (histone IIIS) (Ki = 0.7 microM) and a non-competitive inhibitor with respect to ATP. This effect was further evidenced by the fact that chelerythrine inhibited native PKC and its catalytic fragment identically and did not affect [3H]- phorbol 12,13 dibutyrate binding to PKC. Chelerythrine selectively inhibited PKC compared to tyrosine protein kinase, cAMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase. The potent antitumoral activity of celerythrine measured in vitro might be due at least in part to inhibition of PKC and thus suggests that PKC may be a model for rational design of antitumor drugs. | lld:pubmed |
| pubmed-article:2244923 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2244923 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2244923 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2244923 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2244923 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:2244923 | pubmed:author | pubmed-author:GleyeJJ | lld:pubmed |
| pubmed-article:2244923 | pubmed:author | pubmed-author:MaffrandJ PJP | lld:pubmed |
| pubmed-article:2244923 | pubmed:author | pubmed-author:HerbertJ MJM | lld:pubmed |
| pubmed-article:2244923 | pubmed:author | pubmed-author:AugereauJ MJM | lld:pubmed |
| pubmed-article:2244923 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2244923 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2244923 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:2244923 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2244923 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2244923 | pubmed:pagination | 993-9 | lld:pubmed |
| pubmed-article:2244923 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:2244923 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2244923 | pubmed:articleTitle | Chelerythrine is a potent and specific inhibitor of protein kinase C. | lld:pubmed |
| pubmed-article:2244923 | pubmed:affiliation | Sanofi Recherche, Toulouse, France. | lld:pubmed |
| pubmed-article:2244923 | pubmed:publicationType | Journal Article | lld:pubmed |
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