Document Detail


Regulation of phosphatidylcholine biosynthesis by the methylation pathway in rat pituitary gland.
MedLine Citation:
PMID:  6469209     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Rat pituitary extracts catalyze methylation of phosphatidylethanolamine to phosphatidylcholine using S-adenosyl-L-methionine as the methyl donor. In vitro incubation of hemipituitaries with 1 mM 2-methylaminoethanol led to a dose dependent decrease in phosphatidylethanolamine methyltransferase activity as well as the incorporation of the radioactivity from [3H-methyl]-L-methionine into phosphatidyl-choline. The inhibitory effect of 2-methylaminoethanol was selective for phospholipids methylation since protein carboxymethyltransferase and catechol-o-methyltransferase activities were not affected.
Authors:
C Prasad; R M Edwards
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et métabolisme     Volume:  16     ISSN:  0018-5043     ISO Abbreviation:  Horm. Metab. Res.     Publication Date:  1984 Aug 
Date Detail:
Created Date:  1984-10-19     Completed Date:  1984-10-19     Revised Date:  2009-02-19    
Medline Journal Info:
Nlm Unique ID:  0177722     Medline TA:  Horm Metab Res     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  431-4     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Catechol O-Methyltransferase / metabolism
Ethanolamines / pharmacology
Male
Methionine / metabolism
Methylation
Methyltransferases / metabolism
Phosphatidylcholines / biosynthesis*
Phosphatidylethanolamine N-Methyltransferase
Pituitary Gland / enzymology,  metabolism*
Protein Biosynthesis
Protein O-Methyltransferase / metabolism
Rats
Rats, Inbred Strains
Chemical
Reg. No./Substance:
0/Ethanolamines; 0/Phosphatidylcholines; 109-83-1/N-methylaminoethanol; 63-68-3/Methionine; EC 2.1.1.-/Methyltransferases; EC 2.1.1.-/Protein O-Methyltransferase; EC 2.1.1.17/Phosphatidylethanolamine N-Methyltransferase; EC 2.1.1.6/Catechol O-Methyltransferase

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


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