Labelling of vasopressin and oxytocin receptors from the human uterus

Tencé, Martine; Guillon, Gilles; Bottari, Serge P.; Jard, Serge

doi:10.1016/0014-2999(90)94177-y

Cited by 28 publications

(18 citation statements)

References 22 publications

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“…The novel oxytocin-binding sites described here also had high affinity for the related neurohypophysial peptide AVP. This has been a consistent finding in studies of ovine oxytocin receptors (Ayad & Wathes 1989, Ayad et al 1990) and of this receptor in other species (Audigier & Barberis 1985, Elands et al 1988, Jard 1988, Maggi et al 1987, 1988, 1991, Tence et al 1990). However, in vivo studies have indicated that AVP does not have an oxytocic potency equal to that of oxytocin (Ayad et al 199A) and therefore actions of endogenous AVP on the ovine cervix cannot necessarily be predicted from the present study.…”

Section: Discussionsupporting

confidence: 64%

Characterization and localization of a putative oxytocin receptor in the cervix of the oestrous ewe

Matthews

Ayad²

1994

Journal of Endocrinology

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The purpose of the present study was to investigate the presence of high-affinity oxytocin-binding sites (putative oxytocin receptors) in the cervix of the non-pregnant ewe. [3H]Oxytocin binding to the peripheral layers of cervical tissue (comprising the serosal layer and the least dense collagenous and muscular layers) and the remaining dense collagenous cervical tissue were studied separately. [3H]Oxytocin-binding sites were detected in membrane fractions prepared from both of these regions, but binding to the peripheral cervix was variable and binding site concentrations were low, hence these were not characterized further. A high-affinity oxytocin-binding site, having a dissociation constant of 1.8 nmol/l, was characterized in the dense collagenous regions of the cervix of ewes killed during the oestrous period. Similar dissociation constants were determined for [Arg8]-vasopressin and the oxytocin-specific agonist [Thr4, Gly7]-oxytocin in competition studies. [3H]Oxytocin binding to peripheral cervical tissue and to the dense collagenous cervix was generally low or undetectable during the luteal phase, but increased in both tissues around the time of luteolysis. Although specific binding to both tissues was variable during the oestrous period, it was higher at this time than during the luteal phase. [3H]Oxytocin-binding site concentrations were also found to be higher within the inner dense collagenous cervix of oestrous ewes than of pregnant, ovariectomized or anoestrous animals.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionsupporting

confidence: 64%

Characterization and localization of a putative oxytocin receptor in the cervix of the oestrous ewe

Matthews

Ayad²

1994

Journal of Endocrinology

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“…Although specific physiological functions have been attributed to each hormone, such as vasopressor effect and urine concentration for AVP and uterotonic and milk-ejecting activities for OT, they both show relatively high affinity for the four receptor subtypes. Interestingly, V1aR and OTR are coexpressed in several tissues such as the myometre (19,20) and some regions of the central nervous system (21), whereas V1aR is found also with V2R in the collecting duct (22)(23)(24)(25). Taken with the high level of sequence homology between the receptor subtypes (40-50%), such colocalization would be compatible with the occurrence of heterodimerization in native tissues.…”

Section: G Protein-coupled Receptors (Gpcrs)mentioning

confidence: 66%

Oxytocin and Vasopressin V1a and V2 Receptors Form Constitutive Homo- and Heterodimers during Biosynthesis

Terrillon

Durroux

Mouillac

et al. 2003

Molecular Endocrinology

293

219

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G protein-coupled receptor (GPCR) oligomerization is a growing concept that has emerged from several studies suggesting that GPCRs can form both homo- and heterodimers. Using both coimmunoprecipitation and bioluminescence resonance energy transfer (BRET) approaches, we established that the vasopressin V1a, V2, and the oxytocin receptors exist as homo- and hetero-dimers in transfected human embryonic kidney 293T cells. Each receptor protomer had a similar propensity to form homo- and heterodimers, indicating that their relative expression levels may determine the homo-/heterodimer ratio. The finding that immature forms of the receptor can be immunoprecipitated as homo- and heterodimers and the detection by BRET of such oligomer in endoplasmic reticulum-enriched fractions suggest that the oligomerization processes take place early during biosynthesis. Treatment with agonists or antagonists did not modify the BRET among any of the vasopressin and oxytocin receptor pairs studied, indicating that the dimerization state of the receptors is not regulated by ligand binding once they have reached the cell surface. Taken together, these results strongly support the notion that GPCR dimerization is a constitutive process.

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“…We use in‐vitro receptor autoradiography with a high affinity, selective radioiodinated linear vasopressin analogue ( 16) to localize V 1a binding sites in the brain. Because there has been considerable species variability in the selectivity of oxytocin and vasopressin ligands ( 17), we use in‐situ hybridization with a cloned fragment of the rhesus V 1a receptor gene in adjacent sections to confirm the identity of these binding sites and to determine the sites of V 1a receptor synthesis.…”

mentioning

confidence: 99%

Localization of Vasopressin (V_1a) Receptor Binding and mRNA in the Rhesus Monkey Brain

Young

Toloczko

Insel

1999

J Neuroendocrinology

124

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Centrally released arginine vasopressin (AVP) has been associated with various behavioural and cognitive effects, such as scent marking, aggression, and memory, which are believed to be mediated by the V1a subtype of the vasopressin receptor. Although the distribution of V1a receptors is conserved in a few brain regions, the pattern of expression of this receptor is, in general, highly species-specific. We have used receptor autoradiography with the linear V1a receptor ligand (125I-Phenylacetyl-D-Tyr(Me)-Phe-Gln-Asn-Arg-Pro-Arg-Tyr-NH2) to characterize the pattern of receptor binding in the rhesus monkey brain. Brain sites of V1a receptor synthesis were defined using in-situ hybridization. The regions of highest V1a receptor density included the prefrontal, cingulate, pyriform, and entorhinal cortex, as well as the presubiculum and mamillary bodies. In addition, V1a receptor binding and mRNA were detected in several regions reported to have V1a receptor in most rodents, including the amygdala, bed nucleus of the stria terminalis, lateral septum, hypothalamus and the brainstem. The distribution is consistent with a role for vasopressin in higher cognitive functions, especially memory, in primates.

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Labelling of vasopressin and oxytocin receptors from the human uterus

Cited by 28 publications

References 22 publications

Characterization and localization of a putative oxytocin receptor in the cervix of the oestrous ewe

Characterization and localization of a putative oxytocin receptor in the cervix of the oestrous ewe

Oxytocin and Vasopressin V1a and V2 Receptors Form Constitutive Homo- and Heterodimers during Biosynthesis

Localization of Vasopressin (V_1a) Receptor Binding and mRNA in the Rhesus Monkey Brain

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Labelling of vasopressin and oxytocin receptors from the human uterus

Cited by 28 publications

References 22 publications

Characterization and localization of a putative oxytocin receptor in the cervix of the oestrous ewe

Characterization and localization of a putative oxytocin receptor in the cervix of the oestrous ewe

Oxytocin and Vasopressin V1a and V2 Receptors Form Constitutive Homo- and Heterodimers during Biosynthesis

Localization of Vasopressin (V1a) Receptor Binding and mRNA in the Rhesus Monkey Brain

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Localization of Vasopressin (V_1a) Receptor Binding and mRNA in the Rhesus Monkey Brain