| pubmed-article:1426703 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1426703 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1426703 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:1426703 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:1426703 | lifeskim:mentions | umls-concept:C0031809 | lld:lifeskim |
| pubmed-article:1426703 | lifeskim:mentions | umls-concept:C0007589 | lld:lifeskim |
| pubmed-article:1426703 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:1426703 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:1426703 | lifeskim:mentions | umls-concept:C1511938 | lld:lifeskim |
| pubmed-article:1426703 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1426703 | pubmed:dateCreated | 1992-12-11 | lld:pubmed |
| pubmed-article:1426703 | pubmed:abstractText | In neutrophils, the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) induced the translocation of the Ca(++)- and phospholipid-dependent protein kinase, protein kinase C (PK-C) from the soluble to the particulate fraction. At the same time there was a corresponding increase in the amount of Ca(++)- and phospholipid-independent protein kinase activity recovered in the soluble fraction. This soluble Ca(++)- and phospholipid-independent protein kinase presumably reflects proteolytic activation of the particulate associated PK-C. Bone marrow and undifferentiated HL-60 cells also translocated PK-C to the particulate fraction in response to TPA but did not accumulate the soluble Ca(++)- and phospholipid-independent form of the enzyme. Similar results were obtained using HL-60 cells induced to differentiate with dimethyl sulphoxide (DMSO), recombinant human granulocyte-macrophage colony-stimulating factor (rh GM-CSF) or 1 alpha,25-dihydroxyvitamin D3. There was also no significant change in either the number or time of expression of differentiation-specific cell surface antigens observed on HL-60 cells induced to differentiate with either DMSO, 1 alpha,25-dihydroxyvitamin D3 or TPA in the presence of cyclosporin A, an agent reported to inhibit the proteolytic breakdown of PK-C to the Ca(++)- and phospholipid-independent form. Likewise, cyclosporin A did not affect the rate of extent of differentiation of primary bone marrow cell cultures. These results suggest that the proteolytically activated and phospholipid-independent form of PK-C is probably not involved in haemopoietic cell differentiation. | lld:pubmed |
| pubmed-article:1426703 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1426703 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1426703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1426703 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1426703 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1426703 | pubmed:issn | 0301-4681 | lld:pubmed |
| pubmed-article:1426703 | pubmed:author | pubmed-author:MurrayA WAW | lld:pubmed |
| pubmed-article:1426703 | pubmed:author | pubmed-author:LopezA FAF | lld:pubmed |
| pubmed-article:1426703 | pubmed:author | pubmed-author:HardyS JSJ | lld:pubmed |
| pubmed-article:1426703 | pubmed:author | pubmed-author:HaylockD NDN | lld:pubmed |
| pubmed-article:1426703 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1426703 | pubmed:volume | 50 | lld:pubmed |
| pubmed-article:1426703 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1426703 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1426703 | pubmed:pagination | 189-202 | lld:pubmed |
| pubmed-article:1426703 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:1426703 | pubmed:meshHeading | pubmed-meshheading:1426703-... | lld:pubmed |
| pubmed-article:1426703 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1426703 | pubmed:articleTitle | Examination of the role of the proteolytically-activated form of protein kinase C in the differentiation of human haemopoietic cells. | lld:pubmed |
| pubmed-article:1426703 | pubmed:affiliation | School of Biological Sciences, Flinders University of South Australia, Adelaide. | lld:pubmed |
| pubmed-article:1426703 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1426703 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
