Classification and nomenclature of phencyclidine and sigma receptor sites

Quirion, Rémi; Chicheportiche, Robert; Contreras, Patricia C.; Johnson, Kenneth M.; Lodge, David; Tam, S. William; Woods, James H.; Zukin, Stephen R.

doi:10.1016/0166-2236(87)90094-4

Cited by 260 publications

(103 citation statements)

References 8 publications

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“…A very recent review (Guitart et al, 2004) describes the potential involvement of σ receptors in schizophrenia, movement disorders, depression, anxiety, drug abuse, and pain. For general reviews of early investigations with σ receptors and σ receptor ligands, the reader is referred to: Abou-Gharbia et al, 1993;Chavkin, 1990;Domino and Kamenka, 1988;Itzhak, 1994;Itzhak and Stein, 1990;Junien and Leonard, 1989;Musacchio et al, 1989;Quirion et al, 1987;Snyder and Largent, 1989;Walker et al, 1990.…”

Section: Introductionmentioning

confidence: 99%

<![CDATA[Binding characteristics of sigma2 receptor ligands]]>

Glennon¹

2005

Rev. Bras. Cienc. Farm.

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Section: Introductionmentioning

confidence: 99%

<![CDATA[Binding characteristics of sigma2 receptor ligands]]>

Glennon¹

2005

Rev. Bras. Cienc. Farm.

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“…However, subsequent studies demonstrated that the 0 binding sites are distinct from PCP binding sites (PCP receptor) located within the cation channel of the N-methyl-D-aspartate (NMDA) receptor ion channel complex (Quirion et al, 1987;Deutsch et al, 1988;Church and Lodge, 1990;Sanger et al, 199 1). Based on data obtained from biochemical and radioligand-binding experiments, subtypes of a binding sites have been classified into at least two types designated al and ~2, though the physiological roles for these two subtypes remains to be clarified (Walker et al, 1990).…”

mentioning

confidence: 99%

Sigma ligands indirectly modulate the NMDA receptor-ion channel complex on intact neuronal cells via sigma 1 site

Yamamoto

Sagi

et al. 1995

J. Neurosci.

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To investigate the modulatory effects of sigma ligands on the N-methyl- D-aspartate (NMDA) receptor-ion channel complex in vivo, we examined the intact cell binding of 3H-N-[1-(2-thienyl)cyclohexyl]piperidine (3H- TCP) to cultured neuronal cells prepared from fetal rat telencephalon. The 3H-TCP binding was saturable, reversible, and inhibited by a selective NMDA receptor antagonist, D-amino-5-phosphonovaleric acid. MII-limolar Mg2+ inhibited 3H-TCP binding both in the absence and presence of L-glutamate. 5-Methyl-10,11-dihydro-5H-dibenzo [a,d]cyclohepten-5,10-imine maleate (MK801) inhibited 3H-TCP intact cell binding in a competitive manner, while haloperidol inhibited it in a noncompetitive manner. The effect of the test drugs to inhibit 3H-TCP intact cell binding was in the order of dextromethorphan, haloperidol > (+/-)MK 801 > (+)pentazocine > (-)pentazocine > DTG > PCP > (+)-N- allylnormetazocine [(+)SKF 10047] > (+)3-(3-hydroxyphenyl)-N- (1- propyl)piperidine [(+)3-PPP] > (-)SKF 10047 > (-)3-PPP. The IC50 values of the six sigma ligands for 3H-TCP binding were closely correlated with the Ki values of the corresponding drugs for DTG site 1 in the guinea pig brain reported by Rothman et al. (1991). These findings suggest that the sigma ligand indirectly modulates the NMDA receptor ion channel complex, presumably through sigma 1 sites in vivo as well as in vitro.

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“…The differences between the enantioselectivity of SKF-10047 and other benzomorphans for Sigma and opioid receptors further supported the unique classification for Sigma receptors (Zukin, 1982;Tam, 1983). Subsequently, controversy also arose over the identity of Sigma receptor sites versus PCP sites on NMDA receptors due to the similar affinities of several ligands for both sites (Quirion et al, 1987;Zukin et al, 1984), and the modulatory role sigma 1 receptors have on NMDA receptors (Yamamoto et al, 1995) and glutamate release (Debonnel and de Montigny, 1996). When more selective compounds became available, PCP and sigma 1 binding sites were established as belonging to distinct proteins (Tam 1983, Tam andCook 1984).…”

Section: Introductionmentioning

confidence: 98%

An unambiguous assay for the cloned human sigma1 receptor reveals high affinity interactions with dopamine D4 receptor selective compounds and a distinct structure–affinity relationship for butyrophenones

Lee

Chen

Schetz

2008

European Journal of Pharmacology

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The ability of sigma 1 receptors to interact with a huge range of drug structural classes coupled with its wide distribution in the body has contributed to it being implicated as a possible therapeutic target for a broad array of disorders ranging from substance abuse to depression to Alzheimer's disease. Surprisingly, the reported affinity values for some sigma 1 receptor ligands vary more than 50-fold. The potential of the sigma 1 receptor as a pharmacotherapeutic target prompted us to develop an unambiguous assay system for measuring the affinity of ligands to the cloned human sigma 1 receptor. In the course of characterizing this system and determining the true affinity values for almost three dozen compounds, it was discovered that some dopamine D 4 receptor selective compounds bind sigma 1 receptors with high affinity. A systematic analysis of haloperidol-like compounds revealed a clear structure-affinity relationship amongst clinically relevant butyrophenones. The antidepressant fluvoxamine, the drug of abuse methamphetamine, and the neurosteroid progesterone were amongst the many ligands whose interactions with sigma 1 receptor were confirmed with our screening assay.

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Classification and nomenclature of phencyclidine and sigma receptor sites

Cited by 260 publications

References 8 publications

<![CDATA[Binding characteristics of sigma2 receptor ligands]]>

<![CDATA[Binding characteristics of sigma2 receptor ligands]]>

Sigma ligands indirectly modulate the NMDA receptor-ion channel complex on intact neuronal cells via sigma 1 site

An unambiguous assay for the cloned human sigma1 receptor reveals high affinity interactions with dopamine D4 receptor selective compounds and a distinct structure–affinity relationship for butyrophenones

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