Localization and pharmacological characterization of high affinity binding sites for vasopressin and oxytocin in the rat brain by light microscopic autoradiography

Tribollet, Eliane; Barberis, Claude; Jard, Serge; Dubois‐Dauphin, Michel; Dreifuss, J. J.

doi:10.1016/0006-8993(88)91437-0

Cited by 439 publications

(213 citation statements)

References 21 publications

Supporting

Mentioning

199

Contrasting

Unclassified

Order By: Relevance

“…AVP-induced responses of SCN cells in slices of the hamster hypothalamus and mediated by Vla receptors [20]. Vla receptors and transcripts have been demonstrated in the SCN by receptor autoradiography and in situ hybridization, respectively [18,32,33,46,53]. Stimulation of Via receptors results in phosphoinositol turnover and the subsequent activation of protein kinase C (PKC) [38,43].…”

Section: Introductionmentioning

confidence: 99%

Distribution of AVP and Ca2+-dependent PKC-isozymes in the suprachiasmatic nucleus of the mouse and rabbit

Zee

Bult

1995

Brain Research

View full text Add to dashboard Cite

Citation for published version (APA): Zee, E. A. V. D., & Bult, A. (1995). Distribution of AVP and Ca2+-dependent PKC-isozymes in the suprachiasmatic nucleus of the mouse and rabbit. Brain Research, 701(1), 99-107. https://doi.org/10.1016/0006-8993(95)00968-1 Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. AbstractThe suprachiasmatic nucleus (SCN) is the circadian pacemaker in mammals and contains a network of argimne-vasopressin-immunoreactive (AVP-ir) neurons. AVP-recipient cells contain the Vla class of receptors linked to phosphoinositol turnover and protein kinase C (PKC). The present study describes the localization of AVP and the four Ca2+-dependent PKC-isoforms in the mouse and rabbit SCN. An estimate of the numerical density of AVP-ir neurons at the rostral, medial, and caudal level of the SCN revealed that the mouse SCN contains more than twice the number of AVP-ir neurons than the rabbit SCN. Neurons immunostained for AVP or PKC dominated in the dorsomedial and ventrolateral aspects of the mouse SCN, while the central area of the SCN revealed only weakly stained neurons. The rabbit SCN was characterized by a more homogeneous distribution of AVP-ir and PKC-ir neurons. PKCa was the most abundantly expressed isozyme in both species, whereas the presence of the other isoforms differed (mouse: PKC a > PKC/31 > > PKC/3 II > PKCT: rabbit: PKC~ > PKC/3II > PKC7 > PKC/3I). Clear PKCy-positive neurons were only observed in the rabbit SCN, while the mouse SCN predominantly contained immunolabeled fiber tracts for this PKC isozyme. Astrocytes immunoreactive for each PKC isoform were frequently encot, ntered in the rabbit SCN, but were absent in mice. Immunofluorescence double labeling showed that numerous AVP-recipient cells in the mouse SCN were immunopositive for PKCo~, and that nearly all AVP-ir neurons express PKCo~ abundantly. These results substantiate the putative role for PKC a in vasopressinergic signal transduction in the SCN. The differential expression in degree and cell lype of the CaZ+-dependent PKC-isoforms in the mouse and rabbit SCN may be related to the differences observed in circadian timekeeping between the two species.

show abstract

Section: Introductionmentioning

confidence: 99%

Distribution of AVP and Ca2+-dependent PKC-isozymes in the suprachiasmatic nucleus of the mouse and rabbit

Zee

Bult

1995

Brain Research

View full text Add to dashboard Cite

show abstract

“…The CAI/subicuhtm of the ventral hippocampus is one of the brain structures in which vasopressin (VP)-and oxytocin (OT)-containing fibers [8,16] and specific binding sites for these hormones have been found [23,24,34,63]. Centrally administered VP improves avoidance behavior, stimulates the maintenance of tolerance to alcohol, and affects the regulation of the body temperature and many other physiological parameters (for review see [20]).…”

Section: Introductionmentioning

confidence: 99%

Long-lasting enhancement of synaptic excitability of CA1/subiculum neurons of the rat ventral hippocampus by vasopressin and vasopressin(4–8)

Chepkova¹,

French

Wied

et al. 1995

Brain Research

View full text Add to dashboard Cite

Vasopressin (VP) is axonally distributed in many brain structures, including the ventral hippocampus. Picogram quantities of VP injected into the hippocampus improve the passive avoidance response of rats, presumably by enhancing memory processes. Vasopressin is metabolized by the brain tissue into shorter peptides, such as [pGlu4,Cyt~']VP(4-9) and [pGlu4,Cyt~']VP(4-8), which preserve the behavioral activity but lose the peripheral activities of the parent hormone. Using brain slices, we investigated whether VP or VP(4-8) affects excitatory postsynaptic potentials (EPSPs) and/or membrane responses to depolarization in neurons of the CA 1/subiculum of lhe ventral hippocampus. The EPSPs were evoked by stimulating the stratum radiatum of the CAI field; the membrane responses were elicited by current injections. Exposure of slices for 15 min to 0.1 nM solution of these peptides resulted in an increase in the amplitude and slope of the EPSPs in 21 neurons (67%) tested. No consistent change in either the resting membrane potential or the input resistance of the neurons was observed. The peptide-induced increase in EPSPs reached a maximum 30-45 min after peptide application. In 14 of these neurons (66%), the peptide-induced increase in EPSPs remained throughout the entire 60-120 min washout period. In the remaining 7 neurons (33%1, the initial increase in EPSPs amplitude was followed by a gradual decline to the pre-adminislralion level. The increase in EPSP amplitude was often, but not always, associated with a decrease in the threshold and increase in the number of action potentials in response lo depolarizing current injection. Suppression of GABA a receptor-mediated inhibition and N-methyl-D-aspartate (NMDA) receptor-mediated excitation did not prevent the effects of VP and VP(4-8) on the EPSP amplitude or the threshold for action potentials. The results demonstrate that 0.1 nM concentrations of these neuropeptides can elicit a long-lasting enhancement of the excitability of CAl/subiculum neurons of the ventral hippocampus to excitatory, glutamatergic synaptic input. This novel action of VP and its metabolite in the ventral hippocampus may be the physiological action, mediating the memory-enhancing effect of these peptides.

show abstract

“…The V1, VPR subtype, expressed by vascular smooth muscle and hepatocytes, has been well characterized and is known to regulate blood pressure and liver function by stimulating phosphoinositidase C (Michell et al, 1979). The V,, VPR is also expressed by other cell types in the central nervous system and periphery (Jard et al, 1987;Maggi et al, 1988;Tribollet et al, 1988). The availability of V,,-selective ligands, particularly antagonists (Manning et al, 1987a), has greatly facilitated studies addressing the nature and function of the V,, VPR subtype.…”

mentioning

confidence: 99%

“…The V,, VPR is also expressed by other cell types in the central nervous system and periphery (Jard et al, 1987;Maggi et al, 1988;Tribollet et al, 1988).…”

mentioning

confidence: 99%

Fluorescent and biotinylated linear peptides as selective bifunctional ligands for the V_1a vasopressin receptor

Howl

Wang

Kirk

et al. 1993

European Journal of Biochemistry

View full text Add to dashboard Cite

We have designed and synthesized a linear peptide analogue of arginine vasopressin. This peptide, 11-phenylacetyl, 2-O-methyl-~-tyrosine, 6-arginine, 8-arginine, 9-lysinamide]vasopressin (PhAcALVP), has a lysinamide residue substituted for the more usual glycinamide at position 9. Derivatization of PhAcALVP at the NE-lysyl amino group with N-hydroxysuccinimide esters of aminomethylcoumarin (Mec) and biotin (Btn) produced the bifunctional ligands PhAcAL(Mec jVP and PhAcAL(Btn)VP, respectively. Pharmacological characterization of these peptides revealed that all were high-affinity V,,-selective antagonists. PhAcAL(BtnjVP can simultaneously bind to both the rat liver V,, receptor and avidin conjugates. Using this strategy, we were able to study the distribution of V,, receptors on the surface of the rat mammary tumour cell line, WRK-1. Routine epifluorescent microscopy and confocal image analysis were used to observe the distribution of avidin -Texas-Red associated with receptor-bound PhAcAL(Btn)VP. We conclude that PhAcALVP is a useful precursor for the production of hetero-bifunctional V,,-selective ligands. Both PhAcAL-(Mec)VP and PheAcAL(Btn)VP can be used selectively to probe the Vt, receptor and will be versatile tools for a variety of histocytochemical applications, including receptor localization and purification.[Args]vasopressin ([Arg'IVPj, a neurohypophyseal peptide hormone, regulates a plethora of physiological processes in mammals that include well-documented pressor (Hofbauer et al., 1984) and antidiuretic actions (reviewed by Handler and Orloff, 1981). To date, three pharmacologically distinct subtypes of vasopressin receptor (VPR) have been described and classified as Vla, V,, and V, (Michell et al., 1979;Jard et al., 1986). The V1, VPR subtype, expressed by vascular smooth muscle and hepatocytes, has been well characterized and is known to regulate blood pressure and liver function by stimulating phosphoinositidase C (Michell et al., 1979). The V,, VPR is also expressed by other cell types in the central nervous system and periphery (Jard et al., 1987;Maggi et al., 1988;Tribollet et al., 1988). The availability of V,,-selective ligands, particularly antagonists (Manning et al., 1987a), has greatly facilitated studies addressing the nature and function of the V,, VPR subtype. In this regard, the synthetic peptide [l -P-mercaptocyclopentamethylenepropionic acid, 2-O-methyltyrosine, Arg8]vasopressin [d(CH,j,Tyr(Me)2]AVP which is a V,, VPR antagonist (Kruszynski et al., 1980) has proved particularly useful for selectively blocking V,, VPR function. Like [d(CH,),Tyr(Me)2]AVP, the vast majority of potent structural analogues of [Arg8]VP have incorporated an intramolecular disulphide bond between positions 1 and 6 to mimic the cystine bond in [Arg'IVP. Manning and his co-workers (Manning et al., 1984 were also the first to demonstrate that the nature of the amino acid residue at position 9 does not greatly influence the potency of cyclic vasopressin antagonists. Indeed, all that may be required for high-a...

show abstract

Localization and pharmacological characterization of high affinity binding sites for vasopressin and oxytocin in the rat brain by light microscopic autoradiography

Cited by 439 publications

References 21 publications

Distribution of AVP and Ca2+-dependent PKC-isozymes in the suprachiasmatic nucleus of the mouse and rabbit

Distribution of AVP and Ca2+-dependent PKC-isozymes in the suprachiasmatic nucleus of the mouse and rabbit

Long-lasting enhancement of synaptic excitability of CA1/subiculum neurons of the rat ventral hippocampus by vasopressin and vasopressin(4–8)

Fluorescent and biotinylated linear peptides as selective bifunctional ligands for the V_1a vasopressin receptor

Contact Info

Product

Resources

About

Localization and pharmacological characterization of high affinity binding sites for vasopressin and oxytocin in the rat brain by light microscopic autoradiography

Cited by 439 publications

References 21 publications

Distribution of AVP and Ca2+-dependent PKC-isozymes in the suprachiasmatic nucleus of the mouse and rabbit

Distribution of AVP and Ca2+-dependent PKC-isozymes in the suprachiasmatic nucleus of the mouse and rabbit

Long-lasting enhancement of synaptic excitability of CA1/subiculum neurons of the rat ventral hippocampus by vasopressin and vasopressin(4–8)

Fluorescent and biotinylated linear peptides as selective bifunctional ligands for the V1a vasopressin receptor

Contact Info

Product

Resources

About

Fluorescent and biotinylated linear peptides as selective bifunctional ligands for the V_1a vasopressin receptor