We have located links that may give you full text access.
Journal Article
Research Support, Non-U.S. Gov't
Role of cytosolic phospholipase A(2)α in cell rounding and cytotoxicity induced by ceramide-1-phosphate via ceramide kinase.
Archives of Biochemistry and Biophysics 2011 August 2
Ceramide-1-phosphate (C1P), produced by ceramide kinase (CERK), is implicated in the regulation of many biological functions including cell growth and inflammation. C1P is a direct activator of group IVA cytosolic phospholipsase A(2) (PLA2G4A or cPLA(2)α). Although activation of the CERK-C1P pathway causes mitogenic and cytoprotective responses in many cells, the pathway shows cytotoxicity in several cells and the precise mechanism has not been elucidated. In the present study, we examined the effect of human CERK (hCERK) expression on cytotoxicity in two cell lines. Expression of hCERK in CHO cells caused cell rounding and lactate dehydrogenase (LDH) leakage, and co-addition of ceramide enhanced these responses. Expression of hCERK enhanced C1P formation and release of arachidonic acid in Ca(2+) ionophore-stimulated cells. Treatment with 20μM C2-C1P for 24 h caused cell rounding, and the response was significantly decreased by an inhibitor of cPLA(2)α. In L929 cells, expression of hCERK with and without ceramide caused cell rounding and LDH leakage, respectively, and the responses were significantly less in a stable clone of L929 cells lacking cPLA(2)α. These findings suggest the involvement of cPLA(2)α in CERK-C1P pathway-induced cytotoxicity.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app