Characterization of the purinoceptors present in rabbit and guinea pig liver.

Micromolar concentrations of ATP induced a cAMP-independent glycogenolytic response in rabbit and guinea pig hepatocytes. With ATP alpha[35S] (adenosine 5'-[alpha-[35S]thio]triphosphate) as radioligand, we detected the presence of specific purinoceptors on hepatocytes and liver plasma membranes of both species. We determined a Kd value of 0.28 microM and a Bmax of 4.8 pmol/10(6) cells for rabbit hepatocytes and a Kd of 0.25 microM and a Bmax of 7.0 pmol/10(6) cells for guinea pig hepatocytes. The Kd values with purified plasma membranes from rabbit and guinea pig liver, were respectively 0.2 and 0.1 microM whereas the Bmax values were respectively 71 and 47 pmol/mg of protein. These purinoceptors belong to the P2Y-subclass as is evidenced by the high degree of similarity which exists between the binding affinities of several ATP analogues to either rabbit or guinea pig liver plasma membranes and rat liver plasma membranes, previously shown to possess P2Y-purinoceptors.