Pergolide, Terguride and N,N'-spacer-linked Oligomers of Both Interact with 5-HT2A Receptors of Rat Tail Artery

Title:

Pergolide, Terguride and N,N'-spacer-linked Oligomers of Both Interact with 5-HT2A Receptors of Rat Tail Artery

Creator:

Křen, V., Eich, E., and Pertz, H.H.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:1a1f16da-0545-4345-81ee-d094205d6975
uuid:1a1f16da-0545-4345-81ee-d094205d6975

Subject:

Pergolide, Terguride, Oligomers of pergolide and terguride, 5HT2A receptors, Contraction, and Rat tail artery

Type:

article, model:article, and TEXT

Description:

Pergolide, terguride and N,N'-spacer-linked oligomers of both have been tested for their ability to interact with 5 hydroxytryptamine(HT)2A receptors of rat tail artery. Pergolide was a potent partial agonist (pEC50 7.5, Emax 55 %) and antagonized 5-HT-induced contractions (pKP 7.2). Pergolide dimer 3 with a p-xylene spacer between the indole nitrogens (N-1) displayed somewhat lower agonist potency than pergolide (pEC50 7.0, Emax 55 %, pKP 6.6). The contractile responses to pergolide and dimer 3 were antagonized by the 5-HT2A receptor antagonist ketanserin (pA2 9.4, 9.1). In contrast to pergolide dimer 3, pergolide dimers 5 and 9 with an alkyl and an aralkyl spacer between the piperidine nitrogens (N-6) lacked agonism and displayed low affinity at 5-HT2A receptors (pA2 < 5.5). Terguride behaved as an insurmountable antagonist of 5-HT (pA2 8.4). Oligomers of terguride showed 5 to 50-fold lower affinity. It is concluded that pergolide and terguride show a high affinity for 5-HT2A receptors, but dimerization (oligomerization) of both drugs fails to increase affinity.

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2004 Volume:53 | Number:1

Harvested from:

CDK

Metadata only:

false