| pubmed-article:3259317 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3259317 | lifeskim:mentions | umls-concept:C0021757 | lld:lifeskim |
| pubmed-article:3259317 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:3259317 | lifeskim:mentions | umls-concept:C0021547 | lld:lifeskim |
| pubmed-article:3259317 | lifeskim:mentions | umls-concept:C0243127 | lld:lifeskim |
| pubmed-article:3259317 | lifeskim:mentions | umls-concept:C1155437 | lld:lifeskim |
| pubmed-article:3259317 | lifeskim:mentions | umls-concept:C1514485 | lld:lifeskim |
| pubmed-article:3259317 | lifeskim:mentions | umls-concept:C0443331 | lld:lifeskim |
| pubmed-article:3259317 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:3259317 | pubmed:dateCreated | 1988-6-22 | lld:pubmed |
| pubmed-article:3259317 | pubmed:abstractText | Interleukin 3 (IL-3) is required for the survival and proliferation of the FDCP-Mix 1 multipotent stem cell line. IL-3 or phorbol esters can rapidly translocate protein kinase C from a cytosolic to a membrane-bound form in these cells. Phorbol esters were able to partially replace the requirement of FDCP-Mix 1 cells for IL-3. Down-modulation of protein kinase C levels by chronic treatment with phorbol ester markedly reduced the ability of the cells to proliferate in response to either IL-3 or phorbol esters. These data indicate that IL-3 can activate protein kinase C, leading to the survival and proliferation of stem cells. Protein kinase C is activated conventionally by complexing with diacylglycerol which accumulates in the cell membrane after agonist-stimulated hydrolysis of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]. However, there was no detectable breakdown of PtdIns(4,5)P2 when IL-3 was added to FDCP-Mix 1 cells, nor was there detectable accumulation of inositol phosphates in response to IL-3. In contrast, rapid hydrolysis of PtdIns(4,5)P2 and accumulation of inositol 1,4,5-trisphosphate was elicited by readdition of horse serum to serum-starved cells, thus indicating that these cells possess the necessary machinery to undergo agonist-mediated inositol phospholipid breakdown. We conclude that the mechanism whereby IL-3 can activate protein kinase C leading to proliferation is not associated with inositol phospholipid hydrolysis. | lld:pubmed |
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| pubmed-article:3259317 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3259317 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3259317 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3259317 | pubmed:month | May | lld:pubmed |
| pubmed-article:3259317 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3259317 | pubmed:author | pubmed-author:DexterT MTM | lld:pubmed |
| pubmed-article:3259317 | pubmed:author | pubmed-author:WhettonA DAD | lld:pubmed |
| pubmed-article:3259317 | pubmed:author | pubmed-author:DownesC PCP | lld:pubmed |
| pubmed-article:3259317 | pubmed:author | pubmed-author:HuangS JSJ | lld:pubmed |
| pubmed-article:3259317 | pubmed:author | pubmed-author:MonkP NPN | lld:pubmed |
| pubmed-article:3259317 | pubmed:author | pubmed-author:ConsalveyS... | lld:pubmed |
| pubmed-article:3259317 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3259317 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:3259317 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3259317 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3259317 | pubmed:pagination | 3284-8 | lld:pubmed |
| pubmed-article:3259317 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3259317 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3259317 | pubmed:articleTitle | Interleukin 3 stimulates proliferation via protein kinase C activation without increasing inositol lipid turnover. | lld:pubmed |
| pubmed-article:3259317 | pubmed:affiliation | Department of Biochemistry and Applied Molecular Biology, UMIST, Manchester, United Kingdom. | lld:pubmed |
| pubmed-article:3259317 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3259317 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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