[1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid),2-(O-methyl)tyrosine]arginine-vasopressin and [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)]arginine-vasopressin, two highly potent antagonists of the vasopressor response to arginine-vasopressin

Kruszynski, Marian; Lammek, Bernard; Manning, Maurice; Seto, J.; Haldar, Jaya; Sawyer, Wilbur H.

doi:10.1021/jm00178a003

Cited by 463 publications

(176 citation statements)

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“…These results and the recenl finding of specific binding sites for VP (4)(5)(6)(7)(8) in synaptosomal membrane preparations from the anterior cortex [22] strongly suggest that many of the central effects of VP and its metabolites are mediated by specific receptor complex(es) distinct from the peripheral V l, V~ or OT receptors. The observation that many of the VP effects on the brain neurons are prevented by pretreatment of the neurons with d(CH2)5-Tyr(Me)-arg inines VP [38,45,47,67,70], shown to be a selective antagonist at the periheral V~ pressor VP receptor [36], might be misleading as this antagonist acts as a general neurodepressant agent [49]. Thus, further studies with various ligands for VP and for OT types of receptors might be a better approach for characterization of the receptors mediating the VP effect on EPSPs.…”

Section: Discussionmentioning

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

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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.

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Section: Discussionmentioning

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

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“…Therefore, the rats were considered to be water-replete. The vasopressin antagonist (VPA) employed in this study was [1-(3.mercapto-j3,j3-cyclo-pentamethylene propionic acid), 2-(O-methyl)tyrosine] arginine-vasopressin (KRUSZYNsKI et al, 1980). Under experimentally set different circumstances, while arterial pressure was being recorded, VPA was injected intravenously at a dose of 0.01 or 0.02 mg/kg to observe whether it induced the characteristic, almost step-wise decrease in arterial pressure (Fig.…”

Section: Methodsmentioning

confidence: 99%

Conditions for secretion of vasopressin in pressor amounts in water-replete rats.

Iriuchijima

1983

Jpn.J.Physiol

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Conditions for secretion of pressor amounts of vasopressin were sought in conscious, water-replete rats. The characteristic lowering of arterial pressure on injection of a vasopressin antagonist was used to detect vasopressin secretion in pressor amounts. The absence or marked abatement of both baroreceptor impulses and adrenomedullary secretion were found necessary for secretion of vasopressin in pressor amounts : the vasopressin antagonist lowered arterial pressure in rats with sinoaortic denervation and ganglion blockade or adrenalectomy. Besides baroreceptor activity and adrenomedullary secretion, anesthetics were also found inhibitory on vasopressin release in pressor amounts. The adrenomedullary hormone signaling the presence of adrenomedullary activity to the vasopressin releasing mechanism was identified as noradrenaline and not adrenaline. It is suggested that the vasopressin pressor mechanism is recruited to sustain arterial pressure when the sympathoadrenal system fails.

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“…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.…”

mentioning

confidence: 99%

“…PhAcAL(Btn)VP binds very selectively to the V1, VPR subtype, compared to the rat kidney V, VPR, and is shown to be a versatile probe for the V,, VPR. (Kruszynski et al, 1980;80.9 Ci/ mmol) were from NEN (Du Pont Ltd). My0-[2-~H]inositol (1 08.4 Ci/mmol) was from Amersham.…”

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

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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...

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[1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid),2-(O-methyl)tyrosine]arginine-vasopressin and [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)]arginine-vasopressin, two highly potent antagonists of the vasopressor response to arginine-vasopressin

Cited by 463 publications

References 10 publications

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

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

Conditions for secretion of vasopressin in pressor amounts in water-replete rats.

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

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[1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid),2-(O-methyl)tyrosine]arginine-vasopressin and [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)]arginine-vasopressin, two highly potent antagonists of the vasopressor response to arginine-vasopressin

Cited by 463 publications

References 10 publications

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

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

Conditions for secretion of vasopressin in pressor amounts in water-replete rats.

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

Contact Info

Product

Resources

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