Linked Life Data

9691465

Source:http://linkedlifedata.com/resource/pubmed/id/9691465

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-9-8
pubmed:abstractText
The effects of a series of ceramide analogs with acyl chain lengths of 2, 6, 8 and 16 on the structure of diapalmitoylphosphatidylcholine (DPPC) bilayers and cobra venom phospholipase A2 (PL-A2) activity were studied using 2H-NMR and specific enzymatic assays. C2-ceramide did not induce a significant effect on the structure of DPPC bilayers and did not alter PL-A2 activity. C6- and C8-ceramides increased the ordering of the DPPC acyl chains, correlating with the inhibition of PL-A2 activity which was probably due to the increased lateral surface pressure. The long-chain C16-ceramide induced lateral phase separation of the bilayers into gel and liquid crystalline domains and activated PL-A2, as does natural ceramide (Huang et al. 1996). Taken together, the results strongly suggest a correlation between membrane defects induced by ceramide analogs and their effects on phospholipase A2 activity. Furthermore, the effects of short-chain ceramides on PL-A2 are different from those of natural ceramide, indicating that the cell-permeable short-chain ceramide analogs, widely used to study the shpingomyelin-dependent cellular signal transduction pathway, may not completely mimic the natural product.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0175-7571
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
361-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Ceramides perturb the structure of phosphatidylcholine bilayers and modulate the activity of phospholipase A2.
pubmed:affiliation
Department of Biology, University of California, Riverside 92521, USA.
pubmed:publicationType
Journal Article, In Vitro