Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1997-4-17
pubmed:abstractText
The cytosolic cyclic nucleotide phosphodiesterase (PDE) activity from rat thymocytes was resolved into five peaks by HPLC. Only two forms of the cAMP-specific PDE4 were found to be sensitive to physiologically relevant phosphatidic acid (PA) concentrations. PA activated the PDE4-peak 3 form, the fatty acid composition and unsaturation degree determining the efficiency of PA. The PDE4-peak 2 form was inhibited only by PA with saturated fatty acyl groups. PDE4 activation was specific of anionic phospholipids, a free phosphate group in the phospholipid molecule being required for maximum activation. These results suggest that PA may contribute to the lowering of cAMP level required in the early steps of a lympho-proliferative response, thus regulating immune functions through PDE4 activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0898-6568
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
511-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Activation of a cyclic nucleotide phosphodiesterase 4 (PDE4) from rat thymocytes by phosphatidic acid.
pubmed:affiliation
INSERM U.352, Laboratoire de Biochimie et Pharmacologie, INSA-Lyon, Villeurbanne, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't