Linked Life Data

1824257

Source:http://linkedlifedata.com/resource/pubmed/id/1824257

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1992-10-16
pubmed:abstractText
FD/PMA is a subclone of the interleukin-3 (IL-3)-dependent, FDC-P1 cell line, which proliferates in response to either 12-O-tetradecanoylphorbol-13 acetate (PMA) or IL-3. While several endogenous substrates were phosphorylated in response to protein kinase C (PKC) activation in FDC-P1, phospholipid-dependent phosphorylation in the FD/PMA grown in PMA was not observed. Basal, phosphatidylserine-independent, and diolein-independent phosphorylation of cytosolic substrates with molecular weights of 17, 52, 57, and 105 Kd were enhanced in FD/PMA cells grown in PMA as compared with FDC-P1 cells cultured in IL-3. Phosphorylation of a 105-Kd substrate was enhanced in the particulate fraction of FD/PMA cells maintained in PMA. The 17-Kd substrate in FD/PMA cells comigrated with a substrate phosphorylated in a PKC-dependent manner in FDC-P1 cells. Phosphorylation of the 52- and 57-Kd substrates, but not of the 17-Kd substrate, was inhibited by H-7 and staurosporine. A portion of the PMA-induced cytosolic kinase activity coeluted with PKC on diethyl aminoethyl chromatography. While FD/PMA cells cultured in PMA contained negligible PKC-dependent phosphorylation of endogenous substrates or histone, alpha and epsilon PKC isoforms were detected by Western blot analysis. PKC phosphotransferase activity was observed in FD/PMA cells grown in PMA when peptides corresponding to residues 720 to 737 of PKC-epsilon or residues 4 to 14 of myelin basic protein were used as substrates. These data indicate that maintenance of FD/PMA cells in PMA stimulates proliferation and markedly alters PKC substrate specificity. Generation of at least two phospholipid-independent kinases occurs in PMA-treated cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2633-41
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:1824257-Adenosine Triphosphate, pubmed-meshheading:1824257-Amino Acid Sequence, pubmed-meshheading:1824257-Animals, pubmed-meshheading:1824257-Antibodies, pubmed-meshheading:1824257-Autoradiography, pubmed-meshheading:1824257-Blotting, Western, pubmed-meshheading:1824257-Cell Line, pubmed-meshheading:1824257-Chromatography, DEAE-Cellulose, pubmed-meshheading:1824257-Clone Cells, pubmed-meshheading:1824257-Interleukin-3, pubmed-meshheading:1824257-Isoenzymes, pubmed-meshheading:1824257-Kinetics, pubmed-meshheading:1824257-Mice, pubmed-meshheading:1824257-Molecular Sequence Data, pubmed-meshheading:1824257-Molecular Weight, pubmed-meshheading:1824257-Peptides, pubmed-meshheading:1824257-Phosphoproteins, pubmed-meshheading:1824257-Phosphorus Radioisotopes, pubmed-meshheading:1824257-Phosphorylation, pubmed-meshheading:1824257-Protein Kinase C, pubmed-meshheading:1824257-Substrate Specificity, pubmed-meshheading:1824257-Tetradecanoylphorbol Acetate
pubmed:year
1991
pubmed:articleTitle
Differential effect of phorbol esters and interleukin-3 on protein kinase C isoform content and kinase activity in the FDC-P1 cell line.
pubmed:affiliation
Department of Medicine, East Carolina University School of Medicine, Greenville, NC 27858-4354.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't