Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1992-12-11
|
| 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcitriol,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Dimethyl Sulfoxide,
http://linkedlifedata.com/resource/pubmed/chemical/Granulocyte-Macrophage...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0301-4681
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
50
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
189-202
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:1426703-Biological Transport,
pubmed-meshheading:1426703-Bone Marrow,
pubmed-meshheading:1426703-Bone Marrow Cells,
pubmed-meshheading:1426703-Calcitriol,
pubmed-meshheading:1426703-Calcium,
pubmed-meshheading:1426703-Cell Differentiation,
pubmed-meshheading:1426703-Cells, Cultured,
pubmed-meshheading:1426703-Cyclosporine,
pubmed-meshheading:1426703-Dimethyl Sulfoxide,
pubmed-meshheading:1426703-Enzyme Activation,
pubmed-meshheading:1426703-Granulocyte-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:1426703-Hematopoietic Stem Cells,
pubmed-meshheading:1426703-Humans,
pubmed-meshheading:1426703-Macrophages,
pubmed-meshheading:1426703-Monocytes,
pubmed-meshheading:1426703-Neutrophils,
pubmed-meshheading:1426703-Peptide Hydrolases,
pubmed-meshheading:1426703-Protein Kinase C,
pubmed-meshheading:1426703-Tetradecanoylphorbol Acetate
|
| pubmed:year |
1992
|
| pubmed:articleTitle |
Examination of the role of the proteolytically-activated form of protein kinase C in the differentiation of human haemopoietic cells.
|
| pubmed:affiliation |
School of Biological Sciences, Flinders University of South Australia, Adelaide.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|