Muscarinic cholinoceptors in the human heart: demonstration, subclassification, and distribution View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-01

AUTHORS

N. M. Deighton, S. Motomura, D. Borquez, H. R. Zerkowski, N. Doetsch, O.-E. Brodde

ABSTRACT

In human atrial and ventricular myocardium, the muscarinic cholinoceptor (M-cholinoceptor) populations were characterized by means of radioligand binding (with [N-methyl-3H]-scopolamine ([3H]-NMS) as the ligand) and functional experiments (negative inotropic effect of carbachol on isolated electrically driven right atrial and left papillary muscle preparations).Binding of [3H]-NMS to human atrial and ventricular membranes was rapid, reversible and saturable (KD-values: 0.5–1.0 nmol/l). The maximal number of [3H]-NMS binding sites, however, was approximately 2.5-fold higher in right and left atrial membranes (200–250 fmol[3H]-NMS specifically bound/mg protein) than in right and left ventricular membranes (80–100 fmol/mg protein).M-cholinoceptor antagonists inhibited [3H]-NMS binding to right atrial and left ventricular membranes with steep, monophasic competition curves indicating interaction with a single class of binding sites. In both tissues the order of potency was: atropine > AF-DX 116 > hexahydro-siladifenidol (HHSiD) > pirenzepine.It is concluded that, in the human heart, functional M-cholinoceptors mediating negative inotropic effects exist that belong predominantly (if not exclusively) to the M2-subtype. However, the atrial regions of the human heart are more densely endowed with these M2-cholinoceptors than the ventricular myocardium. More... »

PAGES

14-21

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00195052

DOI

http://dx.doi.org/10.1007/bf00195052

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045072770

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2314479


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