The rat isolated portal vein: a preparation sensitive to neurokinins, particularly neurokinin B

The rat isolated portal vein is pharmacological preparation more sensitive to neurokinin B than to any other neurokinin or tachykinin. The preparation is more sensitive to C-terminal partial sequences of substance P (SP) particularly SP-(6–11) than to the whole undecapeptide. The order of potency of...

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Veröffentlicht in:European journal of pharmacology 1987-02, Vol.134 (3), p.321-326
Hauptverfasser: Mastrangelo, D., Mathison, R., Huggel, H.J., Dion, S., D'Orléans-Juste, P., Rhaleb, N.E., Drapeau, G., Rovero, P., Regoli, D.
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Sprache:eng
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Zusammenfassung:The rat isolated portal vein is pharmacological preparation more sensitive to neurokinin B than to any other neurokinin or tachykinin. The preparation is more sensitive to C-terminal partial sequences of substance P (SP) particularly SP-(6–11) than to the whole undecapeptide. The order of potency of neurokinins is as follows: neurokinin B > neurokinin A > substance P. The preparation shows high sensitivity also to kassinin and eledoisin. Comparative tests performed with strips of the rat portal vein suspended in a microbath under continuous perfusion (system 1) or in ordinary baths for isolated smooth muscles (system 2) have given similar results and have shown that the myotropic effect of neurokinin B is not modified by a variety of antagonists of endogenous agents as well as by inhibitors of the arachidonic acid cascade. The present results suggest that neurokinin B contracts the rat portal vein by activating specific receptors, presumably located on the smooth muscle membrane, different from those of biologically active amines and peptides which are active stimulants of the vein. Neurokinin B is ten times more active than neurokinin A and at least 100 times more than substance P. Such an order of potency of agonists suggests the existence of a new neurokinin receptor type, particularly sensitive to neurokinin B.
ISSN:0014-2999
1879-0712
DOI:10.1016/0014-2999(87)90363-3