| pubmed-article:7532666 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0151686 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0001455 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0441471 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C2350701 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C1158423 | lld:lifeskim |
| pubmed-article:7532666 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:7532666 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7532666 | pubmed:dateCreated | 1995-3-29 | lld:pubmed |
| pubmed-article:7532666 | pubmed:abstractText | The immunoregulatory C-C chemokine, macrophage inflammatory protein-1 alpha (MIP-1 alpha) has suppressive activity on proliferation of stem cells and early subsets of myeloid progenitor cells. A receptor for C-C chemokines that binds MIP-1 alpha has been characterized, cloned, and shown to be related structurally to neuropeptide receptors that couple through G-proteins to phospholipase-C and adenyl cyclase. Yet, very little information on the intracellular mechanisms of action of MIP-1 alpha is available. We show here that the human factor-dependent cell line M07e is responsive to the cell cycle-suppressive effects of MIP-1 alpha, has specific membrane-binding sites for MIP-1 alpha, and that treatment of these cells with this chemokine increases the phosphatidylcholine (PC) and phosphocholine turnover rates in cells that are synergistically stimulated by the combination of granulocyte-macrophage colony-stimulating factor and steel factor but not these factors acting singly. Additional, MIP-1 alpha treatment induces a dose- and time-dependent increase in intracellular cAMP levels in M07e cells. Both exogenous PC and dibutyryl cAMP were found to suppress the proliferation of M07e colony-forming cells to a level similar to that of MIP-1 alpha, further implicating cAMP and PC metabolism in MIP-1 alpha-induced M07e suppression. RANTES, a related chemokine, with weak or incomplete binding to the cloned MIP-1 alpha receptor, did not suppress M07e colony-forming cells, nor did it increase intracellular cAMP levels, but it did enhance growth factor-induced PC turnover, further supporting the involvement of cAMP in MIP-1 alpha suppression while demonstrating that increased PC turnover alone is not sufficient for suppression. These findings support the idea that the human MIP-1 alpha receptor is coupled to phospholipid and cAMP metabolism in a manner similar to other 7-transmembrane, G-protein-linked receptors and suggest that a phosphatidylcholine hydrolytic cycle and an associated increase in cAMP are part of the mechanisms of action of MIP-1 alpha. | lld:pubmed |
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| pubmed-article:7532666 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7532666 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7532666 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7532666 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7532666 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:7532666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7532666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7532666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7532666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7532666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7532666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7532666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7532666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7532666 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7532666 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7532666 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:7532666 | pubmed:author | pubmed-author:BroxmeyerH... | lld:pubmed |
| pubmed-article:7532666 | pubmed:author | pubmed-author:MantenAA | lld:pubmed |
| pubmed-article:7532666 | pubmed:author | pubmed-author:CooperSS | lld:pubmed |
| pubmed-article:7532666 | pubmed:author | pubmed-author:KimY JYJ | lld:pubmed |
| pubmed-article:7532666 | pubmed:author | pubmed-author:MarshallM SMS | lld:pubmed |
| pubmed-article:7532666 | pubmed:author | pubmed-author:LuxSS | lld:pubmed |
| pubmed-article:7532666 | pubmed:author | pubmed-author:AronicaSS | lld:pubmed |
| pubmed-article:7532666 | pubmed:author | pubmed-author:HagueNN | lld:pubmed |
| pubmed-article:7532666 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7532666 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7532666 | pubmed:volume | 154 | lld:pubmed |
| pubmed-article:7532666 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7532666 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7532666 | pubmed:pagination | 2342-50 | lld:pubmed |
| pubmed-article:7532666 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:7532666 | pubmed:meshHeading | pubmed-meshheading:7532666-... | lld:pubmed |
| pubmed-article:7532666 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7532666 | pubmed:articleTitle | Macrophage inflammatory protein-1 alpha enhances growth factor-stimulated phosphatidylcholine metabolism and increases cAMP levels in the human growth factor-dependent cell line M07e, events associated with growth suppression. | lld:pubmed |
| pubmed-article:7532666 | pubmed:affiliation | Department of Medicine (Hematology/Oncology), Indiana University School of Medicine, Indianapolis 46202. | lld:pubmed |
| pubmed-article:7532666 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7532666 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7532666 | lld:pubmed |
