| pubmed-article:9371227 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C0015350 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C0431085 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C0007745 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C0008318 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C1704708 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C2699153 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C1269955 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:9371227 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:9371227 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:9371227 | pubmed:dateCreated | 1997-12-8 | lld:pubmed |
| pubmed-article:9371227 | pubmed:abstractText | Increasing phosphorylation reactions by protein kinase A (PKA) or reducing dephosphorylation reactions of protein phosphatase-2A (PP-2A) increases the invasiveness of Lewis lung carcinoma (LLC) cells, as measured by their capacity to traverse extracellular matrix (ECM)-coated filters. Metastatic LLC-LN7 variants have reduced PP-2A activity when compared to nonmetastatic LLC-C8 variants. Immunoblotting showed that this reduced level of PP-2A activity was not due to reduced levels of the PP-2A catalytic (C) subunit. The cellular PP-2A activity could be stimulated by addition of C2-ceramide to LLC-LN7 lysates, or by incubating cells with either C2-ceramide or with a noncalcemic analog of vitamin D3, which has previously been shown to stimulate the release of ceramide. These treatments to elevate PP-2A activity in metastatic LLC-LN7 cells resulted in a decline in their capacity to invade through select (ECM) components, particularly through vitronectin and laminin. Underscoring the importance of PP-2A in limiting the invasiveness of tumor cells was the demonstration that LLC-LN7 cell transfectants overexpressing the PP-2A C alpha subunit were less invasive through ECM components than the wild-type cells. Invasion by these cells was further reduced by additionally increasing PP-2A activity by incubation with C2-ceramide or the vitamin D3 analog. These results suggest a role of a vitamin D3/ceramide/PP-2A pathway in limiting the invasiveness of tumor cells through select ECM components. | lld:pubmed |
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| pubmed-article:9371227 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9371227 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9371227 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9371227 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9371227 | pubmed:issn | 0251-1789 | lld:pubmed |
| pubmed-article:9371227 | pubmed:author | pubmed-author:JacksonJJ | lld:pubmed |
| pubmed-article:9371227 | pubmed:author | pubmed-author:YoungM RMR | lld:pubmed |
| pubmed-article:9371227 | pubmed:author | pubmed-author:PatelSS | lld:pubmed |
| pubmed-article:9371227 | pubmed:author | pubmed-author:MetzR JRJ | lld:pubmed |
| pubmed-article:9371227 | pubmed:author | pubmed-author:BergstromRR | lld:pubmed |
| pubmed-article:9371227 | pubmed:author | pubmed-author:WrightM AMA | lld:pubmed |
| pubmed-article:9371227 | pubmed:author | pubmed-author:VellodyKK | lld:pubmed |
| pubmed-article:9371227 | pubmed:author | pubmed-author:MeisingerJJ | lld:pubmed |
| pubmed-article:9371227 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9371227 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:9371227 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9371227 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9371227 | pubmed:pagination | 280-90 | lld:pubmed |
| pubmed-article:9371227 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:9371227 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:9371227 | pubmed:articleTitle | Vitamin D3 and ceramide reduce the invasion of tumor cells through extracellular matrix components by elevating protein phosphatase-2A. | lld:pubmed |
| pubmed-article:9371227 | pubmed:affiliation | Research Services, Hines VA Hospital, Hines, Ill., USA. | lld:pubmed |
| pubmed-article:9371227 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9371227 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9371227 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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