Periportal and perivenous hepatocytes respond equally to glycogenolytic agonists
- 6 June 1988
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 233 (1), 47-50
- https://doi.org/10.1016/0014-5793(88)81353-x
Abstract
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.Keywords
This publication has 13 references indexed in Scilit:
- Characterization of the liver P2-purinoceptor involved in the activation of glycogen phosphorylaseBiochemical Journal, 1986
- Stimulation of glycogenolysis by adenine nucleotides in the perfused rat liverBiochemical Journal, 1986
- Functional Heterogeneity of Periportal and Perivenous HepatocytesEnzyme, 1986
- P2-purinergic control of liver glycogenolysisBiochemical Journal, 1985
- Gluconeogenesis in periportal and perivenous hepatocytes of rat liver, isolated by a new high-yield digitonin/collagenase perfusion techniqueBiochemical Journal, 1985
- Digitonin-collagenase perfusion for efficient separation of periportal or perivenous hepatocytesBiochemical Journal, 1985
- Vasopressin and angiotensin control the activity of liver phosphodiesteraseBiochemical Journal, 1984
- Heterologous desensitization of the cyclic AMP-independent glycogenolytic response in rat liver cellsBiochemical Journal, 1981
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- The Stimulation of Liver Phosphorylase b by AMP, Fluoride and SulfateEuropean Journal of Biochemistry, 1975