Document Detail


Angiogenin stimulates endothelial cell prostacyclin secretion by activation of phospholipase A2.
MedLine Citation:
PMID:  2646638     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Angiogenin stimulates capillary and umbilical vein endothelial cell prostacyclin secretion but not that of prostaglandins of the E series. The response was quantitated by radioimmunoassay and by [3H]arachidonate labeling followed by analysis of the secreted prostaglandins. The stimulated secretion lasts for several minutes and is optimal at 2-4 min. The dose-response (peak at 1-10 ng/ml) is similar to that previously observed for activation of endothelial cell phospholipase C. Stimulated secretion was blocked by pretreatment with the inhibitors of prostacyclin synthesis, indomethacin and tranylcypromine, and also the specific inhibitor of phospholipase A2, quinacrine, as well as pertussis toxin and the diglyceryl and monoglyceryl lipase inhibitor RHC 80267. Stimulated secretion was also abolished in cells that were either pretreated for 48 hr with phorbol ester to down-regulate protein kinase C or incubated with the protein kinase inhibitor H7. Hydrolysis of phosphatidylinositol by phospholipase A2 appears to be the source of angiogenin-mobilized arachidonate; angiogenin-induced hydrolysis of phosphatidylcholine was not detected. Activation of phospholipase A2 occurs in the absence of an angiogenin-induced calcium flux. The results are discussed in terms of mechanisms of agonist-induced intracellular arachidonate mobilization and relevance to angiogenesis.
Authors:
R Bicknell; B L Vallee
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  86     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1989 Mar 
Date Detail:
Created Date:  1989-04-13     Completed Date:  1989-04-13     Revised Date:  2011-07-19    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1573-7     Citation Subset:  IM    
Affiliation:
Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, MA 02115.
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MeSH Terms
Descriptor/Qualifier:
Angiogenesis Inducing Agents / pharmacology*
Animals
Arachidonic Acids / metabolism
Cattle
Cells, Cultured
Cyclohexanones / pharmacology
Dexamethasone / pharmacology
Endothelium, Vascular / drug effects,  secretion*
Enzyme Activation
Epoprostenol / secretion*
Growth Substances / pharmacology*
Humans
Kinetics
Lipoprotein Lipase / antagonists & inhibitors
Neoplasm Proteins / pharmacology*
Pertussis Toxin
Phospholipases / metabolism*
Phospholipases A / metabolism*
Phospholipases A2
Protein Kinase C / metabolism
Quinacrine / pharmacology
Ribonuclease, Pancreatic*
Virulence Factors, Bordetella / pharmacology
Chemical
Reg. No./Substance:
0/Angiogenesis Inducing Agents; 0/Arachidonic Acids; 0/Cyclohexanones; 0/Growth Substances; 0/Neoplasm Proteins; 0/Virulence Factors, Bordetella; 35121-78-9/Epoprostenol; 50-02-2/Dexamethasone; 83-89-6/Quinacrine; 83654-05-1/1,6-bis(cyclohexyloximinocarbonyl)hexane; EC 2.4.2.31/Pertussis Toxin; EC 2.7.11.13/Protein Kinase C; EC 3.1.-/Phospholipases; EC 3.1.1.-/Phospholipases A; EC 3.1.1.34/Lipoprotein Lipase; EC 3.1.1.4/Phospholipases A2; EC 3.1.27.-/angiogenin; EC 3.1.27.5/Ribonuclease, Pancreatic
Comments/Corrections

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