| pubmed-article:11266452 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C0029431 | lld:lifeskim |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C0443193 | lld:lifeskim |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C1947989 | lld:lifeskim |
| pubmed-article:11266452 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:11266452 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11266452 | pubmed:dateCreated | 2001-3-27 | lld:pubmed |
| pubmed-article:11266452 | pubmed:abstractText | The macrophage colony stimulating factor (M-CSF) and alpha(v)beta(3) integrins play critical roles in osteoclast function. This study examines M-CSF- and adhesion-induced signaling in prefusion osteoclasts (pOCs) derived from Src-deficient and wild-type mice. Src-deficient cells attach to but do not spread on vitronectin (Vn)-coated surfaces and, contrary to wild-type cells, their adhesion does not lead to tyrosine phosphorylation of molecules activated by adhesion, including PYK2, p130(Cas), paxillin, and PLC-gamma. However, in response to M-CSF, Src(-/-) pOCs spread and migrate on Vn in an alpha(v)beta(3)-dependent manner. Involvement of PLC-gamma activation is suggested by using a PLC inhibitor, U73122, which blocks both adhesion- and M-CSF-mediated cell spreading. Furthermore, in Src(-/-) pOCs M-CSF, together with filamentous actin, causes recruitment of beta(3) integrin and PLC-gamma to adhesion contacts and induces stable association of beta(3) integrin with PLC-gamma, phosphatidylinositol 3-kinase, and PYK2. Moreover, direct interaction of PYK2 and PLC-gamma can be induced by either adhesion or M-CSF, suggesting that this interaction may enable the formation of integrin-associated complexes. Furthermore, this study suggests that in pOCs PLC-gamma is a common downstream mediator for adhesion and growth factor signals. M-CSF-initiated signaling modulates the alpha(v)beta(3) integrin-mediated cytoskeletal reorganization in prefusion osteoclasts in the absence of c-Src, possibly via PLC-gamma. | lld:pubmed |
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| pubmed-article:11266452 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11266452 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11266452 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11266452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11266452 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11266452 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11266452 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:11266452 | pubmed:author | pubmed-author:RodanG AGA | lld:pubmed |
| pubmed-article:11266452 | pubmed:author | pubmed-author:NakamuraII | lld:pubmed |
| pubmed-article:11266452 | pubmed:author | pubmed-author:LipfertLL | lld:pubmed |
| pubmed-article:11266452 | pubmed:author | pubmed-author:Le T Duong | lld:pubmed |
| pubmed-article:11266452 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11266452 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:11266452 | pubmed:volume | 152 | lld:pubmed |
| pubmed-article:11266452 | pubmed:owner | NLM | lld:pubmed |
