| pubmed-article:2190939 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2190939 | lifeskim:mentions | umls-concept:C0034678 | lld:lifeskim |
| pubmed-article:2190939 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:2190939 | lifeskim:mentions | umls-concept:C0013081 | lld:lifeskim |
| pubmed-article:2190939 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:2190939 | lifeskim:mentions | umls-concept:C0181586 | lld:lifeskim |
| pubmed-article:2190939 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:2190939 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:2190939 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:2190939 | pubmed:dateCreated | 1990-7-19 | lld:pubmed |
| pubmed-article:2190939 | pubmed:abstractText | The effect of mutated c-Ha-ras expression on Ca2+ and phospholipid-dependent protein kinase C (PKC) activity during the process of transformation was analysed using an inducible metallothionein-ras hybrid oncogene system. A close correlation was found between the timing of ras expression and the loss of PKC enzymatic activity measured in a cell-free system. Examination of the subcellular distribution of the enzyme in inducible and constitutive ras-transformants revealed that expression of ras was associated with an apparent translocation of PKC to the plasma membrane concomitant with down-regulation of PKC enzymatic activity in particulate as well as cytosolic fractions. Quantitation of PKC protein utilizing a PKC-specific antiserum showed that ras expression was associated with a decrease in the total amount of PKC protein present in the cell. We conclude that transformation by c-Ha-ras is accompanied by down-regulation of PKC activity and that the basis of this effect may, to a large extent, lie in the down-regulation of the amount of PKC protein. | lld:pubmed |
| pubmed-article:2190939 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2190939 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2190939 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2190939 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2190939 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2190939 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2190939 | pubmed:issn | 0020-7136 | lld:pubmed |
| pubmed-article:2190939 | pubmed:author | pubmed-author:KuoJ FJF | lld:pubmed |
| pubmed-article:2190939 | pubmed:author | pubmed-author:HozumiNN | lld:pubmed |
| pubmed-article:2190939 | pubmed:author | pubmed-author:MillsGG | lld:pubmed |
| pubmed-article:2190939 | pubmed:author | pubmed-author:GirardPP | lld:pubmed |
| pubmed-article:2190939 | pubmed:author | pubmed-author:ChowSS | lld:pubmed |
| pubmed-article:2190939 | pubmed:author | pubmed-author:BullSS | lld:pubmed |
| pubmed-article:2190939 | pubmed:author | pubmed-author:HaliotisTT | lld:pubmed |
| pubmed-article:2190939 | pubmed:author | pubmed-author:TrimbleWW | lld:pubmed |
| pubmed-article:2190939 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2190939 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2190939 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:2190939 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2190939 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2190939 | pubmed:pagination | 1177-83 | lld:pubmed |
| pubmed-article:2190939 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:meshHeading | pubmed-meshheading:2190939-... | lld:pubmed |
| pubmed-article:2190939 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2190939 | pubmed:articleTitle | Expression of ras oncogene leads to down-regulation of protein kinase C. | lld:pubmed |
| pubmed-article:2190939 | pubmed:affiliation | Mount Sinai Hospital Research Institute, University of Toronto, Ontario, Canada. | lld:pubmed |
| pubmed-article:2190939 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2190939 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2190939 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2190939 | lld:pubmed |
