Document Detail

Heterogeneity of phospholipid synthesis in rat liver endoplasmic reticulum during proliferation of smooth membranes.
MedLine Citation:
PMID:  185227     Owner:  NLM     Status:  MEDLINE    
During proliferation of smooth endoplasmic reticulum (SER) induced by phenobarbital the specific activity of acyltransferases of the smooth microsomes increases, there is a transient rise in the phospholipid/protein ratio of these membranes, and an increased incorporation of [14C]glycerol into smooth-membrane phospholipid. Microsomes separated into subfractions on 2 gradients exhibited a heterogeneous distribution of these characteristics, indicating a non-uniform distribution of the site of phospholipid synthesis in the ER under these conditions. Cytochemical localization of acyltransferases on whole liver and smooth and rough microsomes confirmed this heterogeneity, and indicated that the distribution of this activity was not restricted to any morphologically distinct site in the ER of the intact cell. After 4 days of phenobarbital treatment the increased membrane is restricted to lighter subfractions and is similar in distribution to that of increased acyltransferase activity. These results indicate that the synthesis of membrane phospholipid and the growth of the SER in response to phenobarbital is not uniform but occurs at randomly dispersed sites in the SER while proteins may be added preferentially at these sites resulting in a final uniform distribution.
J A Higgins
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of cell science     Volume:  22     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  1976 Oct 
Date Detail:
Created Date:  1976-12-30     Completed Date:  1976-12-30     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  173-97     Citation Subset:  IM    
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MeSH Terms
Acyltransferases / analysis,  metabolism
Endoplasmic Reticulum / metabolism*
Glucose-6-Phosphatase / analysis
Glycerol / metabolism
Liver / metabolism*,  ultrastructure
Microsomes / enzymology,  ultrastructure
Microsomes, Liver / metabolism
Nucleotidases / analysis
Phenobarbital / pharmacology
Phospholipids / biosynthesis*
Proteins / metabolism
Reg. No./Substance:
0/Phospholipids; 0/Proteins; 50-06-6/Phenobarbital; 56-81-5/Glycerol; EC 2.3.-/Acyltransferases; EC 3.1.3.-/Nucleotidases; EC

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

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