Linked Life Data

7535766

Source:http://linkedlifedata.com/resource/pubmed/id/7535766

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1995-5-10
pubmed:abstractText
The effect of alkylglycerol supplementation on protein kinase C (PKC)-mediated signaling events has been studied in fibroblasts from Zellweger patients (SF 3271 cells). Western blotting analysis established that Zellweger fibroblasts express PKC alpha, epsilon, and zeta. Incubation with bradykinin induced a rapid transient translocation of PKC alpha and a more sustained translocation of PKC epsilon to the particulate fraction; translocation of PKC zeta was unaffected. Bradykinin-induced translocation and activation of PKC alpha, but not translocation of PKC epsilon, was blocked in SF 3271 cells which had been incubated with 1-O-hexadecylglycerol (1-O-HDG; 20 micrograms/ml) for 24 h and then incubated in the absence of 1-O-HDG and serum for a further 24 h. Supplementation with 1-O-HDG increased the mass of ether-linked phospholipid. Bradykinin initiated a transient increase in cytosolic Ca2+ concentration in both control and 1-O-HDG supplemented cells, indicating that the initial receptor linked events were not affected by 1-O-HDG supplementation. Bradykinin also caused a rapid activation of phospholipase D (PLD), measured by phosphatidylbutanol accumulation, and mitogen-activated protein kinase (MAPK) determined by myelin basic protein phosphorylation of Mono Q fractions. Both events were blocked by preincubation of the cells with 12-O-tetradecanoylphorbol-13-acetate for 24 h to deplete PKC protein. 1-O-HDG supplementation prevented the bradykinin-induced activation of PLD, but had no effect on the stimulation of MAPK activity. These results establish that modulation of the ether lipid composition of membranes can alter PKC isozyme translocation and indicate that a PKC isozyme other than PKC alpha, most likely PKC epsilon, is involved in MAPK activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7097-103
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:7535766-Bradykinin, pubmed-meshheading:7535766-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:7535766-Cells, Cultured, pubmed-meshheading:7535766-Culture Media, Serum-Free, pubmed-meshheading:7535766-Enzyme Activation, pubmed-meshheading:7535766-Epidermal Growth Factor, pubmed-meshheading:7535766-Fibroblasts, pubmed-meshheading:7535766-Glyceryl Ethers, pubmed-meshheading:7535766-Humans, pubmed-meshheading:7535766-Isoenzymes, pubmed-meshheading:7535766-Kinetics, pubmed-meshheading:7535766-Myelin Basic Proteins, pubmed-meshheading:7535766-Phospholipase D, pubmed-meshheading:7535766-Phosphorylation, pubmed-meshheading:7535766-Protein Kinase C, pubmed-meshheading:7535766-Protein Processing, Post-Translational, pubmed-meshheading:7535766-Skin, pubmed-meshheading:7535766-Tetradecanoylphorbol Acetate, pubmed-meshheading:7535766-Zellweger Syndrome
pubmed:year
1995
pubmed:articleTitle
Evidence that the bradykinin-induced activation of phospholipase D and of the mitogen-activated protein kinase cascade involve different protein kinase C isoforms.
pubmed:affiliation
School of Biological Sciences, Flinders University of South Australia, Adelaide.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't