AJP - Regu Watch the video to see how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Regul Integr Comp Physiol 272: R1841-R1846, 1997;
0363-6119/97 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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 McLaughlin, P. J.
Right arrow Articles by Wu, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McLaughlin, P. J.
Right arrow Articles by Wu, Y.

AJP - Regulatory, Integrative and Comparative Physiology, Vol 272, Issue 6 1841-R1846, Copyright © 1997 by American Physiological Society

ARTICLES

Identification and characterization of the zeta-opioid receptor in developing rat heart

P. J. McLaughlin and Y. Wu
Department of Neuroscience and Anatomy, Pennsylvania State University, College of Medicine, Hershey 17033, USA.

Opioid growth factor (OGF; [Met5]enkephalin) inhibits DNA synthesis of epicardial and myocardial cells in the neonatal rat heart in a receptor-mediated fashion. Ligand binding assays using newborn rat heart and [3H][Met5]enkephalin were performed to characterize the receptor responsible for the cell replicative effects of OGF in developing heart. Specific and saturable binding was detected, and Scatchard analysis revealed that the data were consistent for a single binding site with a binding affinity of 6.8 +/- 0.3 nM and a binding capacity of 21.8 +/- 1.9 fmol/mg protein. Subcellular fractionation studies revealed that binding was restricted to the nuclear fraction. Competition experiments showed that cold [Met5]enkephalin was the most effective ligand at displacing [3H][Met5]enkephalin. Binding was recorded on gestation days 18 and 20, reached its highest level at birth, and steadily decreased from postnatal days 1 to 15; binding at days 21 and 35 and in adults was negligible. The function, pharmacological and biochemical characteristics, distribution, and subcellular location of this OGF receptor in developing mammalian heart are consistent with the zeta-opioid receptor.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Heart Circ. Physiol.Home page
Z. Cao, L. Liu, and D. M. Van Winkle
Activation of {delta}- and {kappa}-opioid receptors by opioid peptides protects cardiomyocytes via KATP channels
Am J Physiol Heart Circ Physiol, August 7, 2003; 285(3): H1032 - H1039.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online