Document Detail

Evidence that ceramide selectively inhibits protein kinase C-alpha translocation and modulates bradykinin activation of phospholipase D.
MedLine Citation:
PMID:  7890607     Owner:  NLM     Status:  MEDLINE    
Sphingomyelinase (SMase) treatment (0.1 unit/ml for up to 30 min) of mouse epidermal (HEL-37) or human skin fibroblast (SF 3155) cells preincubated with [3H]serine to label the sphingomyelin pool caused the accumulation of labeled ceramide but not sphingosine or ceramide 1-phosphate. Incubation of HEL-37 cells with dioctanoylglycerol (diC8) or SF 3155 cells with bradykinin caused translocation of calcium/phosphatidylserine-dependent protein kinase C (PKC) activity to particulate material. In both cell lines the translocation was blocked by SMase treatment of the cells or by incubation with the cell-permeable ceramide analogue N-acetylsphingosine (C2-Cer). Western blot analysis indicated that treatment of HEL-37 cells with diC8 or SF 3155 cells with bradykinin resulted in the translocation of both PKC-alpha and PKC-espilon to particulate material. Treatment with SMase or C2-Cer specifically blocked the translocation of PKC-alpha but not that of PKC-epsilon. Pretreatment of cells with SMase or C2-Cer also inhibited the activation of phospholipase D activity induced by either diC8 (HEL-37 cells) or bradykinin (SF 3155 cells). The data provide strong evidence that ceramide can negatively regulate the translocation of PKC-alpha but not PKC-epsilon and further suggest that PKC-alpha may be involved in regulating phospholipase D activity.
M J Jones; A W Murray
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  270     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1995 Mar 
Date Detail:
Created Date:  1995-04-14     Completed Date:  1995-04-14     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5007-13     Citation Subset:  IM    
School of Biological Sciences, Faculty of Science and Engineering, Flinders University, Adelaide, Australia.
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MeSH Terms
Blotting, Western
Bradykinin / pharmacology*
Cell Line
Ceramides / physiology*
Enzyme Activation
Inositol Phosphates / metabolism
Isoenzymes / antagonists & inhibitors,  metabolism*
Phospholipase D / metabolism*
Protein Kinase C / antagonists & inhibitors,  metabolism*
Skin / enzymology
Sphingomyelin Phosphodiesterase / pharmacology*
Sphingosine / analogs & derivatives,  pharmacology
Time Factors
Reg. No./Substance:
0/Ceramides; 0/Inositol Phosphates; 0/Isoenzymes; 0/N-acetylsphingosine; 123-78-4/Sphingosine; 58-82-2/Bradykinin; EC Kinase C; EC Phosphodiesterase; EC D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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