Document Detail

Periportal and perivenous hepatocytes respond equally to glycogenolytic agonists.
MedLine Citation:
PMID:  2838327     Owner:  NLM     Status:  MEDLINE    
We have used the technique of short-term infusion with digitonin to obtain hepatocytes originating either from the periportal or the perivenous zone of the liver acinus [(1985) Biochem. J. 229, 221-226]. Total glycogen phosphorylase content and sensitivity to cyclic AMP-dependent and calcium-mediated glycogenolytic agonists were very similar for both cell sub-populations and did not differ from the values obtained for control cells. We conclude therefore that there is an apparent absence of metabolic zonation as far as receptor-mediated glycogenolysis and glycogenolytic potency is concerned.
S Keppens; H De Wulf
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  233     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1988 Jun 
Date Detail:
Created Date:  1988-08-01     Completed Date:  1988-08-01     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  47-50     Citation Subset:  IM    
Afdeling Biochemie, Campus Gasthuisberg, Katholieke Universiteit Leuven, Belgium.
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MeSH Terms
Adenosine Triphosphate / pharmacology
Angiotensin II / pharmacology
Calcium / physiology
Cyclic AMP / physiology
Digitonin / pharmacology
Glucagon / pharmacology
Glutamate Dehydrogenase / metabolism
Glycogen / metabolism*
Liver / blood supply,  drug effects,  metabolism*
Phenylephrine / pharmacology
Phosphorylase a / metabolism
Portal System
Rats, Inbred Strains
Vasopressins / pharmacology
Reg. No./Substance:
11000-17-2/Vasopressins; 11024-24-1/Digitonin; 11128-99-7/Angiotensin II; 56-65-5/Adenosine Triphosphate; 59-42-7/Phenylephrine; 60-92-4/Cyclic AMP; 7440-70-2/Calcium; 9005-79-2/Glycogen; 9007-92-5/Glucagon; EC Dehydrogenase; EC 2.4.1.-/Phosphorylase a

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