pubmed-article:2278876 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2278876 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:2278876 | lifeskim:mentions | umls-concept:C0007595 | lld:lifeskim |
pubmed-article:2278876 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
pubmed-article:2278876 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
pubmed-article:2278876 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:2278876 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
pubmed-article:2278876 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:2278876 | lifeskim:mentions | umls-concept:C2752630 | lld:lifeskim |
pubmed-article:2278876 | pubmed:dateCreated | 1991-3-12 | lld:pubmed |
pubmed-article:2278876 | pubmed:abstractText | A protein complex (PC) composed of the MRP8 and MRP14 proteins has previously been shown to be a specific inhibitor of casein kinase I and II. This PC is expressed during the late stages of terminal differentiation induced in human promyelocytic HL-60 leukemia cells by 1 alpha,25-dihydroxyvitamin D3 and in human monocytic THP-1 leukemia cells by phorbol 12-myristate 13-acetate. This expression is associated with terminal cell differentiation because incubation of HL-60 cells with an agent or condition that causes suppression of growth but not induction of differentiation does not result in expression of the PC. At concentrations of 5-15 nM, the purified PC inhibited the growth of HL-60 cells and THP-1 cells, as well as other cell types belonging to different cell lineages. This growth inhibition was preceded by a reduction in [32P]phosphate incorporation and, at the higher PC concentrations, was associated with a reduction in [3H]thymidine, [3H]uridine, and [32S]methionine incorporation. The specific expression pattern and growth-inhibitory character of the PC suggests that the complex may have a role in suppressing cell growth during monomyelocytic terminal differentiation induced by specific chemical stimuli and during physiological and pathological events associated with monomyelocytic cell functions. | lld:pubmed |
pubmed-article:2278876 | pubmed:language | eng | lld:pubmed |
pubmed-article:2278876 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2278876 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2278876 | pubmed:author | pubmed-author:MuraoSS | lld:pubmed |
pubmed-article:2278876 | pubmed:author | pubmed-author:HubermanEE | lld:pubmed |
pubmed-article:2278876 | pubmed:author | pubmed-author:CollartFF | lld:pubmed |
pubmed-article:2278876 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2278876 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2278876 | pubmed:pagination | 447-54 | lld:pubmed |
pubmed-article:2278876 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:2278876 | pubmed:articleTitle | A protein complex expressed during terminal differentiation of monomyelocytic cells is an inhibitor of cell growth. | lld:pubmed |
pubmed-article:2278876 | pubmed:affiliation | Biological and Medical Research Division, Argonne National Laboratory, Illinois 60439. | lld:pubmed |
pubmed-article:2278876 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2278876 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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