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Molecular Pharmacology

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Abstract

Differential activation of intracellular effector by two isoforms of human neurokinin-1 receptor.

T M Fong, S A Anderson, H Yu, R R Huang and C D Strader
Molecular Pharmacology January 1992, 41 (1) 24-30;
T M Fong
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S A Anderson
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H Yu
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R R Huang
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C D Strader
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Abstract

Two isoforms of the human neurokinin-1 receptor were cloned and characterized in heterologous expression systems of mammalian cell culture and Xenopus oocytes. The two isoforms differ only in the length of the encoded polypeptide. The peptide-binding properties of the long form of human neurokinin-1 receptor are consistent with those of the native neurokinin-1 receptor of mammalian tissues, where substance P is the most potent agonist. Peptide agonists elicit an oscillating current in Xenopus oocytes expressing the long form. In contrast, the short form of human neurokinin-1 receptor expressed in COS cells binds substance P with an apparent affinity at least 10-fold lower than that of the long form, and it elicits the electrophysiological response only weakly in Xenopus oocytes. These data suggest that the short form couples to a different effector system. Sequence analysis suggested that the two isoforms may arise from alternative pre-mRNA splicing. These results indicate that multiple forms of the human neurokinin-1 receptor exist and the differential activation of intracellular effector may be involved in generating the complex biological effects of substance P.

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Molecular Pharmacology
Vol. 41, Issue 1
1 Jan 1992
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Abstract

Differential activation of intracellular effector by two isoforms of human neurokinin-1 receptor.

T M Fong, S A Anderson, H Yu, R R Huang and C D Strader
Molecular Pharmacology January 1, 1992, 41 (1) 24-30;

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Abstract

Differential activation of intracellular effector by two isoforms of human neurokinin-1 receptor.

T M Fong, S A Anderson, H Yu, R R Huang and C D Strader
Molecular Pharmacology January 1, 1992, 41 (1) 24-30;
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