Cell surface localization of P2-purinergic receptors in vas deferens.
Head-RJ; O'Donnell-JP; Hogaboom-GK; Fedan-JS
Biochem Pharmacol 1983; 32(3):563-565
Derivatives of ATP were used to induce a contractile response in guinea-pig vas deferens to determine the site of action of ATP and arylazido-aminopropionyl-ATP (ANAPP3). The ability of ATP covalently linked to 4 percent agarose beads to evoke responses was evaluated. Concentration response relationships were determined for three preparations of ATP linked to agarose beads which differed in the site of the attachment of ATP to the hexane bridge connecting the ATP moiety to the agarose bead. In agarose-ATP type 4 (AGATP- 4), ATP was bound at the ribose hydroxyl group; in agarose-ATP type 3 (AGATP-3), ATP was bound at the C8 position of adenine; and in agarose-ATP type 2 (AGATP-2), ATP was bound at the N6 position of adenine. The responses of AGATP-4 were reduced significantly following photolytic treatment of the tissues with ANAPP3. The addition of AGATP-3 and agarose not covalently bound to ATP to the organ bath failed to contract the vasa deferentia. The results indicated that ATP bound to agarose through the ribose hydroxyl moiety can cause contraction of the guinea-pig vas deferens in- vitro, and that this contraction can be markedly attenuated by a P2- receptor antagonist. The failure of AGATP-3 and AGATP-2 to elicit a similar response suggests that there exist distinct structural requirements for the ATP analogs at the site of initiation of responses to ATP and AGATP-4.
NIOSH-Author; Enzyme-activity; Cell-cultures; Laboratory-animals; Nucleotides; Purines