TiPS receptor and ion channel nomenclature supplement 1996

Watson, Steve P.; Girdlestone, D.

doi:10.1016/s0165-6147(96)90289-8

Cited by 36 publications

(55 citation statements)

References 1 publication

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“…Schulz and colleagues as yet at the clinical level. 58 Interestingly, natural had found an opioid in the blood of mammals in 1977 63 that was suspected to permeate into mam-peptide antagonists-in part natural sequences, but 5470 / 8J0E$$5470 05-29-97 12:09:53 pscias W: Pep Sci mary tissue, i.e., into milk; in fact, it appeared there, but it was rather identical to the opioid described by Hazum and colleagues 51 than to an opioid peptide. 64 Trying to trace it, Brantl and colleagues succeeded in the first identification of milk protein-derived opioid receptor ligands, the b-casomorphins.…”

Section: Milk Protein-derived Opioid Receptor Ligandsmentioning

confidence: 99%

“…87,104 -109 (See of the blood-brain barrier obviously is restricted Table II). Attention may be drawn to morphiceptin for b-casomorphins-just brain regions without the and PL017; PL017 is regarded as a standard mblood-brain barrier may be accessible for these selective opioid receptor ligand 58 and morphiceptin peptides. 91 has been used in view of its m-receptor selectivity b-Casomorphins, occurring in the blood in conas a tool in many studies, performed on the opioid centrations as allowed by the rate of absorption from research field.…”

Section: Milk Protein-derived Opioid Receptor Ligandsmentioning

confidence: 99%

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Milk protein-derived opioid receptor ligands

1997

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Section: Milk Protein-derived Opioid Receptor Ligandsmentioning

confidence: 99%

Section: Milk Protein-derived Opioid Receptor Ligandsmentioning

confidence: 99%

Milk protein-derived opioid receptor ligands

1997

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“…Given the clinical importance of CCK-BR-mediated functions, there has been considerable interest in the identification of drugs that selectively activate or block this receptor subtype (9). Resulting from these efforts, it has recently been discovered that, in addition to peptide hormones, synthetic molecules have the potential to activate the CCK-BR.…”

mentioning

confidence: 99%

Inter- and intraspecies polymorphisms in the cholecystokinin-B/gastrin receptor alter drug efficacy

Kopin

McBride

Gordon

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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The brain cholecystokinin-B͞gastrin receptor (CCK-BR) is a major target for drug development because of its postulated role in modulating anxiety, memory, and the perception of pain. Drug discovery efforts have resulted in the identification of small synthetic molecules that can selectively activate this receptor subtype. These drugs include the peptide-derived compound PD135,158 as well as the nonpeptide benzodiazepine-based ligand, L-740,093 (S enantiomer). We now report that the maximal level of receptor-mediated second messenger signaling that can be achieved by these compounds (drug efficacy) markedly differs among species homologs of the CCK-BR. Further analysis reveals that the observed differences in drug efficacy are in large part explained by single or double aliphatic amino acid substitutions between respective species homologs. This interspecies variability in ligand efficacy introduces the possibility of species differences in receptor-mediated function, an important consideration when selecting animal models for preclinical drug testing. The finding that even single amino acid substitutions can significantly affect drug efficacy prompted us to examine ligandinduced signaling by a known naturally occurring human CCK-BR variant (glutamic acid replaced by lysine in position 288; 288 E 3 K). When examined using the 288 E 3 K receptor, the efficacies of both PD135,158 and L-740,093 (S) were markedly increased compared with values obtained with the wild-type human protein. These observations suggest that functional variability resulting from human receptor polymorphisms may contribute to interindividual differences in drug effects.

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“…Receptor heterogeneity as a consequence of the species being used may offer an explanation for the lack of effect of idazoxam: We have previously shown that inhibition by classical antagonists of serotoninergic and muscarinic contractions of rainbow trout intestine is non-competitive (Burka et al 1989), in comparison to competitive antagonism observed in mammalian intestine. At present, there are at least three different types of t~2-adrenoceptors and there is considerable evidence that there are differences in t~2-adrenoceptors between species (Ruffolo and Hieble 1994;Watson and Girdlestone 1995). Idiosyncracies in ~2-adrenoceptor agonists have previously been reported in experiments on rainbow trout stomach (Kitazawa et al 1988).…”

Section: Discussionmentioning

confidence: 94%

Effects of modulatory agents on neurally-mediated responses of trout intestinal smooth musclein vitro

Burka

Briand

Wartman

et al. 1996

Fish Physiol Biochem

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Mediators and mechanisms responsible for the inhibitory modulation of trout intestinal smooth muscle were examined using a series of putative mediators and substances known to modulate neurotransmission in mammalian systems. Frequency response relationships to transmural stimulation and concentration response relationships to 5-hydroxytryptamine, carbachol, and substance P were established on paired segments of rainbow trout intestinein vitro in the presence and absence of putative modulatory agents. Modulation of neurally-mediated contractions of trout intestine was achieved with dibutyryl cyclic AMP and forskolin, agents that increase intracellular levels of cyclic AMP. The effect appears to be at the level of the smooth muscle, since the adenylate cyclase activator, forskolin, inhibited muscarinic and serotoninergic contractions as well as transmurally stimulated contractions. Substance P-induced contractions were unaffected by forskolin. The endogenous agonists/neurotransmitters which would increase cyclic AMP levels in rainbow trout intestinal smooth muscle are as yet unknown. The effects do not appear to be modulated by vasoactive intestinal peptide (VIP), calcitonin, calcitonin gene-related peptide (CGRP), or agents that activate β-adrenoceptors. Prostaglandin E2 (PGE2) and α2-adrenergenic agonists are possible agents which will decrease contractility of the smooth muscle. They were only active in the proximal intestine and on transmurally stimulated contractions. The effects of both PGE2 and α2-agonists appear to be prejunctional, decreasing release of contractile neurotransmitters in the enteric nervous system.

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TiPS receptor and ion channel nomenclature supplement 1996

Cited by 36 publications

References 1 publication

Milk protein-derived opioid receptor ligands

Milk protein-derived opioid receptor ligands

Inter- and intraspecies polymorphisms in the cholecystokinin-B/gastrin receptor alter drug efficacy

Effects of modulatory agents on neurally-mediated responses of trout intestinal smooth musclein vitro

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