Title: Characterization of the effects of adenosine 5'-[beta-thio]-diphosphate in rat liver
Authors: Keppens, Stefaan ×
Vandekerckhove, A
De Wulf, H #
Issue Date: Mar-1993
Publisher: Scientific & Medical Division, Macmillan Press
Series Title: British Journal of Pharmacology vol:108 issue:3 pages:663-8
Abstract: 1. In rat liver cells micromolar concentrations of adenosine 5'-[beta-thio]diphosphate (ADP beta S), activate glycogen phosphorylase by an adenosine 3':5'-cyclic monophosphate (cyclic AMP)- independent mechanism. 2. As with adenosine 5'-triphosphate (ATP), ADP beta S also inhibits the rise in cyclic AMP after glucagon. 3. Cytosolic Ca2+ measured in single cells is rapidly increased with a pattern similar for ADP beta S and for ATP. 4. At variance with ATP, ADP beta S hardly increases inositol 1,4,5-trisphosphate (IP3) levels. 5. Phorbol myristic acetate, which inhibits only slightly the glycogenolytic effect of ATP, almost completely abolishes this effect of ADP beta S. 6. With adenosine 5'-[beta-[35S]thio]diphosphate (ADP beta[35S]) as radioligand, we detected specific purinoceptors on rat liver plasma membranes. Binding consists of a major binding component with KD = 0.7 microM and Bmax = 51 pmol mg-1 of protein, probably mediating the activation of glycogen phosphorylase, and a minor high affinity, low capacity binding component with no obvious function. 7. It is concluded that the differences in biological effects between ATP and ADP beta S may involve different receptors and/or different transduction mechanisms and that ADP beta[35S] can be used to detect the specific binding sites for ADP beta S.
ISSN: 0007-1188
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
× corresponding author
# (joint) last author

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