Monoiodo-[Trp11]neurotensin, a highly radioactive ligand of neurotensin receptors. Preparation, biological activity, and binding properties to rat brain synaptic membranes.

Mazella, Jean; Poustis, Claudine; Labbé, Catherine; Checler, Frédéric; Kitabgi, Patrick; Granier, Claude; Rietschoten, J Van; Vincent, Jean‐Pierre

doi:10.1016/s0021-9258(18)32686-3

Cited by 112 publications

(13 citation statements)

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“…Association kinetics of low affinity sites were examined employing 2.9 nM of 125I-ST, wherein >95% of the observed binding was contributed by low affinity compared to high affinity sites (Figure 2B). Over the time course of these experiments, free labeled ST varied less than 10% and association performed under these conditions fulfilled the criteria for being pseudo first order (Molinoff et al, 1981;Mazella et al, 1983). 125I-ST bound in a time-dependent fashion to low affinity sites in membranes prepared from COS-7 cells transfected with rat GCC, achieving equilibrium after about 30 min at 37 °C (Figure 2B).…”

Section: Resultsmentioning

confidence: 93%

“…where B represents ligand bound at equilibrium, Bmax, the maximum number of binding sites of the family of receptors being studied, L, the ligand concentration, and , the dissociation constant of the ligand-receptor complex (Mazella et al, 1983). Employing 10 pM labeled ligand, >75% of the observed binding in these studies was contributed by high affinity compared to low affinity sites.…”

Section: Resultsmentioning

confidence: 99%

“…Over the time course of these experiments, free labeled ST varied less than 30%. Association performed under these conditions fulfilled the criteria for being pseudo first order since ligand concentrations remained essentially constant and only a single class of receptors was visualized at a given ligand concentration (Molinoff et al, 1981;Mazella et al, 1983). 125I-ST bound in a time-dependent fashion to high affinity sites in membranes prepared from COS-7 cells transfected with rat GCC, achieving equilibrium after approximately 60 min at 37 °C (Figure 2A).…”

Section: Resultsmentioning

confidence: 99%

“…(D) Determination of Association Rate Constants of High and Low Affinity ST Binding Sites and Comparison of Kinetic and Equilibrium Binding Parameters. Once &0bs-H , kobs-u, fcobs-L2, kd.h, and, kd.L were defined, the second order rate constants of association of labeled ST with high affinity sites and with the high and low affinity states of low affinity sites were calculated using the relationship: (2) where ka and kd represent the second order rate constant of association and first order rate constant of dissociation of the complex formed between 125I-ST and receptors (Table 1; Mazella et al, 1983;Hugues et al, 1991). These rate constants for rat GCC expressed in COS-7 cells were closely comparable to those exhibited by native GCC in membranes obtained from rat intestine (Hugues et al, 1991;.…”

Section: Resultsmentioning

confidence: 99%

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Rat Guanylyl Cyclase C Expressed in COS-7 Cells Exhibits Multiple Affinities for Escherichia coli Heat-Stable Enterotoxin

Deshmane

Carrithers²,

Parkinson³

et al. 1995

Biochemistry

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Intestinal cells exhibit binding sites with different affinities for Escherichia coli heat-stable enterotoxin (ST) and guanylin, suggesting the existence of different receptors for these peptides. Guanylyl cyclase C from intestinal cells has been identified as one receptor for these peptides. Equilibrium and kinetic binding characteristics of rat guanylyl cyclase C expressed in COS-7 cells were examined, employing ST, to determine if this receptor exhibited multiple affinities. Scatchard analysis of equilibrium binding yielded curvilinear isotherms consistent with the presence of high (pM) and low (nM) affinity sites. Kinetic analysis of binding demonstrated that these sites exhibited similar dissociation but different association kinetics. In addition, two distinct affinity states of low affinity sites were identified with dissociation constants of 0.15 and 5.85 nM. Association of ST and low affinity sites was biphasic, while dissociation from these sites was unimodal. Close agreement of equilibrium and kinetic dissociation constants suggested that low affinity sites were in the lowest affinity state at equilibrium. Comparison of the ligand dependence of guanylyl cyclase activity (EC50 = 110 nM) with receptor occupancy revealed that binding of ST to the lowest affinity state of low affinity sites (EC50 = 80 nM) is directly coupled to catalytic activation. These studies suggest that binding sites with different affinities for ST exhibited by intestinal cells reflect the expression of a single gene product, guanylyl cyclase C, rather than different receptors for the ligand. The shift in affinity state of low affinity sites and its correlation with catalytic activation suggest a central role for this phenomenon in mechanisms mediating receptor-effector coupling of membrane guanylyl cyclases.

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Section: Resultsmentioning

confidence: 93%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Rat Guanylyl Cyclase C Expressed in COS-7 Cells Exhibits Multiple Affinities for Escherichia coli Heat-Stable Enterotoxin

Deshmane

Carrithers²,

Parkinson³

et al. 1995

Biochemistry

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“…For diagnosis of such type of cancers, the NT (8-13) sequence: [55] also found that a radiohalogenated analogue of neurotensin (8)(9)(10)(11)(12)(13), may be useful for the diagnosis of several tumors like small cell lung carcinoma, colon and pancreas carcinoma. Radioiodination and selective radioiodination at Tyr" were performed and studied [56,57].…”

Section: Neurokininsmentioning

confidence: 99%

The Importance of Amino Acid and Peptide Chemistry in the Treatment of the Major Diseases: Neuropeptides

Moustafa

Shalaby

2021

Egypt. J. Chem.

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During this review, from the reality of the previously published articles, we explained how the peptide bond is formed. This review was divided and different peptide groups were distinguished according to the mode of action of the various peptides, whether they were linear or cyclic peptides, as well as according to the path from hormonally active cells to the target organ, in addition to their peptide analogs that can develop different treatments. Alternatively, an extensive reference survey was conducted for the peptides family "Neuropeptides" and some examples for this family that are chemically composed of various amino acids and peptides were studied.

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Cellular distribution of neurotensin receptors in rat brain: Immunohistochemical study using an antipeptide antibody against the cloned high affinity receptor

et al. 1996

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Receptors for the neuropeptide, neurotensin, were localized by immunohistochemistry in the rat brain by using an antibody raised against a sequence of the third intracellular loop of the cloned high affinity receptor. Selective receptor immunostaining was observed throughout the brain and brainstem. This immunostaining was totally prevented by preadsorbing the antibody with the immunogenic peptide. The regional distribution of the immunoreactivity conformed for the most part to that of [3H]- or [125I]-neurotensin binding sites previously identified by autoradiography. Thus, the highest levels of immunostaining were observed in the islands of Calleja, diagonal band of Broca, magnocellular preoptic nucleus, pre- and parasubiculum, suprachiasmatic nucleus, anterodorsal nucleus of the thalamus, substantia nigra, ventral tegmental area, pontine nuclei and dorsal motor nucleus of the vagus, all of which had previously been documented to contain high densities of neurotensin binding sites. There were, however, a number of regions reportedly endowed with neurotensin binding sites, including the central amygdaloid nucleus, periaqueductal gray, outer layer of the superior colliculus and dorsal tegmental nucleus, which showed no or divergent patterns of immunostaining, suggesting that they might be expressing a molecularly distinct form of the receptor. At the cellular level, neurotensin receptor immunoreactivity was predominantly associated with perikarya and dendrites in some regions (e.g., in the basal forebrain, ventral midbrain, pons and rostral medulla) and with axons and axon terminals in others (e.g., in the lateral septum, bed nucleus of the stria terminalis, neostriatum, paraventricular nucleus of the thalamus and nucleus of the solitary tract). These data indicate that neurotensin may act both post- and presynaptically in the central nervous system and confirm that some of its effects are exerted on projection neurons. There were also areas, such as the cerebral cortex, nucleus accumbens and para- and periventricular nucleus of the hypothalamus, which contained both immunoreactive perikarya/dendrites and axon terminals, consistent with either a joint association of the receptor with afferent and efferent elements or its presence on interneurons. Taken together, these results also suggest that the neurotensin high affinity receptor protein is associated with a neuronal population that is more extensive than originally surmised from in situ hybridization studies.

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Monoiodo-[Trp11]neurotensin, a highly radioactive ligand of neurotensin receptors. Preparation, biological activity, and binding properties to rat brain synaptic membranes.

Cited by 112 publications

References 30 publications

Rat Guanylyl Cyclase C Expressed in COS-7 Cells Exhibits Multiple Affinities for Escherichia coli Heat-Stable Enterotoxin

Rat Guanylyl Cyclase C Expressed in COS-7 Cells Exhibits Multiple Affinities for Escherichia coli Heat-Stable Enterotoxin

The Importance of Amino Acid and Peptide Chemistry in the Treatment of the Major Diseases: Neuropeptides

Cellular distribution of neurotensin receptors in rat brain: Immunohistochemical study using an antipeptide antibody against the cloned high affinity receptor

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