JPET

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fedan, J. S.
Right arrow Articles by Chideckel, E. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fedan, J. S.
Right arrow Articles by Chideckel, E. W.

Evidence that the P2x purinoceptor of the smooth muscle of the guinea pig vas deferens is an ATP4- receptor

JS Fedan, JP Dagirmanjian, MD Attfield and EW Chideckel

Division of Respiratory Disease Studies, National Institute for Occupational Safety and Health, Morgantown, West Virginia.

In solutions containing Mg2+ and Ca2+, ATP is in equilibrium between the tetrabasic form (ATP4-) and its bidentate coordination complexes, i.e., MgATP2- and CaATP2-. We sought evidence to determine whether contractions of the smooth muscle of the guinea pig vas deferens to ATP are in response to ATP4- or its bidentate complexes. Contractions to ATP were elicited in seven modified Krebs-Henseleit solutions containing varied concentrations of free and total Mg2+ and Ca2+ to alter the concentration of ATP4- at given ATPtotal concentrations. As the concentration of Mg2+ increased the concentration of ATP required to stimulate contraction to an equivalent degree also increased. Regardless of the free or total Mg2+ and Ca2+ concentrations, response magnitude was generally correlated with [ATP4-]. This suggests that ATP4- is the agonist at the P2x purinoceptor of the guinea pig vas deferens. The potency of ATP4- is high; the threshold, occurring at approximately 1 nM ATP4-, is 1000-fold less than that for norepinephrine. The implications of ATP4- as agonist are discussed in relation to adenine nucleotide potency, metabolism and P2 purinoceptor classification.

Volume 255, Issue 1, pp. 46-51, 10/01/1990
Copyright © 1990 by American Society for Pharmacology and Experimental Therapeutics




This article has been cited by other articles:


Home page
Am. J. Physiol. Cell Physiol.Home page
F.-P. Gendron, J. T. Neary, P. M. Theiss, G. Y. Sun, F. A. Gonzalez, and G. A. Weisman
Mechanisms of P2X7 receptor-mediated ERK1/2 phosphorylation in human astrocytoma cells
Am J Physiol Cell Physiol, February 1, 2003; 284(2): C571 - C581.
[Abstract] [Full Text] [PDF]


Home page
Pharmacol. Rev.Home page
V. Ralevic and G. Burnstock
Receptors for Purines and Pyrimidines
Pharmacol. Rev., September 1, 1998; 50(3): 413 - 492.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
All ASPET Journals Molecular Pharmacology Pharmacological Reviews
 Molecular Interventions Drug Metabolism and Disposition

Copyright © 1990 by the American Society for Pharmacology and Experimental Therapeutics.