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Results for “Vasoactive Intestinal Peptide”

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PubMed1991

Isolation of a low molecular mass vasoactive intestinal peptide binding protein.

A vasoactive intestinal peptide (VIP) binding protein was purified in active form by detergent solubilization of lung membranes, gel filtration, VIP-Sepharose affinity chromatography, reverse phase high performance liquid chromatography, and anion exchange chromatography. The mass of this protein was estimated at 18 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 17 kDa by gel filtration. The binding of VIP by this protein was inhibited by Mg2+, covalent cross-linking of [Tyr10-125I]VIP to the protein produced two radioactive bands at 22 and 26 kDa identified by electrophoresis, and the purified protein exhibited saturable and high affinity binding of VIP and the related neuropeptide, rat growth hormone releasing factor.

Animals↗

PubMed1986

Interaction of a bovine thymic peptide extract with vasoactive intestinal peptide (VIP) receptors.

Bovine thymic peptide extract (1-100 micrograms/ml) is shown to completely inhibit the binding of [125I]VIP to rat blood mononuclear cells, lymphoid cells of spleen, and liver plasma membranes. In the three models, the bovine thymic peptide extract inhibits [125I]VIP binding with a potency that is 4000-7000 times lower than that of the native VIP, on a weight basis. In rat liver plasma membranes, the bovine thymic peptide extract stimulates adenylate cyclase with a maximal efficiency that is similar to that of VIP. At maximal doses, VIP and thymic peptide extract do not exert an additive effect on adenylate cyclase, suggesting that the activation of the enzyme by the bovine thymic peptide extract occurs through VIP receptors. Finally, no VIP-like immunoreactivity was detected in the thymic peptide extract using an antiserum raised against mammalian VIP. All these data suggest the presence in the bovine thymic peptide extract of a new substance which behaves as a VIP agonist in rat.

Adenylyl Cyclases↗

PubMed1990

[Chemical neuro-anatomy of the thalamus: an example of the co-expression of 2 neuropeptides, cholecystokinin and intestinal vasoactive peptide].

Recent studies using hybridization histochemistry have demonstrated the presence of cholecystokinin (CCK) gene expression in thalamocortical and thalamo-striatal neurons. To further understand the chemical anatomy of the thalamus, we used the same method to study the coexpression of CCK and vasoactive intestinal peptide (VIP) genes in the same neurons. Most of the neurons expressing the VIP gene in the rat dorsal thalamus (found especially in the ventrolateral nucleus) also expressed the CCK gene, as demonstrated by autoradiography on emulsion-coated adjacent sections studied with probes recognizing either mRNA. Some further neurons, located in the reticular nucleus, had VIP mRNA at lower levels of expression but did not appear to contain CCK mRNA.

Animals↗

PubMed1999

[Prenatal inhibition of intestinal vasoactive peptide and cerebral excitatory lesions in the newborn mouse].

The glutamatergic agent ibotenate induces cortical plate and white matter lesions in the newborn mouse, mimicking brain lesions of the human neonate. In this model, co-treatment with ibotenate and a vasoactive intestinal peptide antagonist (VA) aggravates the excitotoxic lesions, suggesting a protective role of endogenous VIP. On the other hand, prenatal injection of VA is followed by a dramatic depletion of astrocytes in the neocortex. Since astrocytes produce numerous neuronotrophic agents, we studied the consequences of a decreased astrocytic density by prenatal VIP blockade on the excitotoxic brain lesions in newborn mice. Pregnant females were pre-treated with VA during the last 2 days of gestation and ibotenate was intracerebrally injected on postnatal day (P) 2 or P5. When compared to controls, pups pre-treated with VA and injected with ibotenate at P2 displayed a significant reduction of the white matter lesion size while cortical plate lesion was not affected. This protective effect disappeared when ibotenate was injected at P5. White matter protection by VA pre-treatment did not seem to be linked to the decreased astrocytic density since, i) this astrocytic paucity concerns only superficial cortical layers and does not affect white matter, ii) protective effects are only observed at P2 while astrocytic density reduction is observed at P2 and P5. This white matter protection could be secondary to an up-regulation of VIP receptors: an increased density of VIP receptors, which was described in other developmental models following VA treatment, could increase the efficacy of the endogenous VIP after an excitotoxic insult.

Animals↗

PubMed1990

Protein secretion in salivary glands of cats in vivo and in vitro in response to vasoactive intestinal peptide.

In anaesthetized cats exogenous vasoactive intestinal peptide failed to elicit any secretion of saliva from the submandibular and parotid glands. However, protein release from both glands occurred in response to VIP in the presence of alpha- and beta-adrenoceptor blocking agents and was dose-dependent. This response was revealed by means of a subsequent washout flow of saliva evoked by intravenous injections of methacholine or stimulations of the parasympathetic innervation. The submandibular glands responded to vasoactive intestinal peptide at a lower dose than the parotid glands. In the presence of atropine (but in the absence of adrenoceptor blockers), stimulation of the parasympathetic chorda-lingual nerve, which of itself elicited no secretion of saliva, contributed to the release of protein within the submandibular gland, since the output of protein in response to a subsequent stimulation of the sympathetic innervation was increased. Vasoactive intestinal peptide administered in combination with methacholine or during ongoing parasympathetic nerve-induced salivary secretion revealed positive interactions, particularly with respect to protein release. In-vitro protein release in response to vasoactive intestinal peptide was also demonstrated by perfusing small pieces of the two glands in the presence of muscarinic and adrenoceptor blockers. As in vivo, submandibular tissue responded at a lower concentration of vasoactive intestinal peptide than the parotid tissue. One to two weeks after combined parasympathetic and sympathetic denervation of the parotid glands, the glands were sensitized to vasoactive intestinal peptide when tested in vitro. It is concluded that vasoactive intestinal peptide or a structurally related peptide is a potential transmitter in the parasympathetic control of protein secretion in salivary glands of cats.

Animals↗

PubMed1988

Photoaffinity labelling of the vasoactive-intestinal-peptide-binding site on intact human colonic adenocarcinoma cell line HT29-D4. Synthesis and use of photosensitive vasoactive-intestinal-peptide derivatives.

N-Hydroxysuccinimidyl 4-azidobenzoate, a u.v.-sensitive heterobifunctional reagent, was used to synthesize photoreactive derivatives of the vasoactive intestinal peptide (VIP). Products of the reaction were purified by reverse-phase h.p.l.c. Three 4-azidobenzoyl-VIP (4-AB-VIP) derivatives were able to compete with monoiodinated 125I-VIP with an apparent KD of 2.5, 6.3 and 12.5 nM compared with 0.6 nM for native VIP. H.p.l.c.-purified mono[125I]iodinated VIP was used to synthesize 4-AB-125I-VIP derivatives. They were used to photoaffinity-label the VIP-binding site of HT29-D4 cells, a clone derived from the human colonic adenocarcinoma cell line HT29. Only one polypeptide, of Mr 70,000 +/- 5000 (mean +/- S.D.) was specifically labelled. The Mr of the component thus characterized was slightly higher than that of the major species (Mr 67,000) labelled after cross-linking experiments using 125I-VIP, conventional homobifunctional reagents and HT29 cells. Nevertheless, the specificity and extent of glycosylation of these two components were identical. These new photosensitive VIP derivatives should be useful tools with which to investigate further VIP-receptor structure and metabolism.

Affinity Labels↗

PubMed1991

Molecular characterization and peptide specificity of two vasoactive intestinal peptide (VIP) binding sites in the chicken pineal.

Here we report that chicken pineal membranes express high affinity receptors for Vasoactive Intestinal Peptide (VIP), as revealed by competitive displacement analysis of [3-iodotyrosyl-125I]-VIP by native VIP. These binding sites were further characterized by covalent cross-linking of radioiodinated VIP to chicken pineal cell membranes, using dithiobis(succinimidylpropionate) as a cross-linking reagent. Sodium dodecyl sulfate electrophoresis after solubilization of the cross-linked membranes, reveals the existence of two polypeptides, P1 and P2, with a similar labelling intensity and apparent molecular weights of Mr = 57,000 and Mr = 70,000 respectively. These two components behave like high affinity binding sites for VIP.

Animals↗

PubMed1999

Functional characterization of a receptor for vasoactive-intestinal-peptide-related peptides in cultured dermal melanophores from Xenopus laevis.

A receptor for vasoactive-intestinal-peptide (VIP)-related peptides was functionally characterized in a cell line derived from Xenopus melanophores using a recently described microtiter-plate-based bioassay. Activation of the melanophore VIP receptor by VIP or the peptides pituitary-adenylate-cyclase-activating polypeptide (PACAP 38), PACAP 27, and helodermin stimulated intracellular 3'-5' cyclic adenosine monophosphate (cAMP) accumulation and pigment dispersion in the cells. Helodermin, with an EC50 (concentration of peptide inducing half-maximal melanosome dispersion) of 46.5 pM, was the most potent activator of pigment dispersion, followed by PACAP 38 > VIP > PACAP 27. A similar order of potencies was observed for the peptides to induce cAMP accumulation. The responses to VIP agonists were selectively inhibited by the VIP antagonists PACAP-(6-27) and (N-Ac-Tyr(1)-D-Phe2)-growth-hormone-releasing factor[GRF](1-29)-NH2. Taken together, the results suggest that the melanophores express a VIP receptor that shares certain characteristics of, but also differs significantly from, other previously identified VIP receptors.

Animals↗

PubMed1994

Inhibitory transmission in tenia coli mediated by distinct vasoactive intestinal peptide and apamin-sensitive pituitary adenylate cyclase activating peptide receptors.

Inhibitory transmission in tenia coli involves both vasoactive intestinal peptide (VIP) and an apamin-sensitive transmitter. The present study examined whether pituitary adenylate cyclase activating peptide (PACAP) is released from tenia coli and accounts for the apamin-sensitive component of neurally mediated relaxation. Electrical field stimulation (0.25-4 Hz) elicited frequency-dependent relaxation and PACAP release; earlier studies had shown a similar pattern for VIP release and an absence of nitric oxide generation in this tissue. A combination of specific PACAP-27 and PACAP-38 monoclonal antibodies (each 100 micrograms/ml), the PACAP antagonist PACAP6-38 and desensitization with PACAP inhibited relaxation induced by all frequencies of stimulation. The magnitude of inhibition elicited by each treatment (38 +/- 3%-41 +/- 3% at 4 Hz) was similar to that elicited by apamin (44 +/- 11%) and was not augmented by apamin. VIP antibody (1:60), the VIP antagonist, VIP10-28 and VIP desensitization also inhibited relaxation (33 +/- 2%-35 +/- 5% at 4 Hz). Inhibition by each treatment was augmented additively by apamin (76 +/- 3%-85 +/- 3%) as well as by combination with PACAP antibody, PACAP antagonist and PACAP desensitization (76 +/- 6%-80 +/- 3%). Measurements in muscle strips and dispersed tenia coil muscle cells showed that VIP10-28 inhibited relaxation induced by VIP only, and PACAP6-38 inhibited relaxation mediated by PACAP-27 or PACAP-38 only, implying interaction of VIP and PACAP with distinct receptors.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1994

Role of vasoactive intestinal peptide in the control of prolactin-induced turkey incubation behavior. II. Chronic infusion of vasoactive intestinal peptide.

Hyperprolactinemia is associated with incubation behavior in avian species. Increased nesting activity is a major indication of incubation behavior. Vasoactive intestinal peptide (VIP) stimulates prolactin (PRL) secretion from the anterior pituitary. The goal of this study was to induce incubation behavior by stimulating PRL through chronically infusing VIP into the third ventricle of turkey brains. In experiment 1, porcine VIP (pVIP) was infused into the median eminence at a rate of 60 ng/min for 7 days by means of osmotic pumps implanted s.c.. Plasma PRL increased significantly in the pVIP-treated turkeys (p < 0.001). Although egg laying was not affected by the pVIP infusion, the mean oviduct weight decreased (p < 0.057). In experiment 2, saline or pVIP (30 or 60 ng/min) was infused into the third ventricle of laying turkeys for 12 days. Both pVIP treatments increased plasma PRL for 9 days (p < 0.05). The 30-ng pVIP/min infusion decreased nesting activity, plasma LH, ovary and oviduct weight, hypothalamic GnRH I, and anterior pituitary VIP receptors (p < 0.1). However, ovine PRL infusion (20.8 ng/min) into the same turkey flock increased nesting activity (p < 0.01). In conclusion, pVIP does not induce incubation behavior in laying turkeys.

Animals↗

PubMed1976

Interaction of porcine vasoactive intestinal peptide with dispersed pancreatic acinar cells from the guinea pig. Structural requirements for effects of vasoactive intestinal peptide and secretin on cellular adenosine 3':5'-monophosphate.

Secretin and vasoactive intestinal peptide (VIP), but not glucagon, stimulate accumulation of cyclic AMP in dispersed guinea pig pancreatic acinar cells. Secretin stimulated cellular accumulation of cyclic AMP by interacting with a single class of high affinity receptors. On the other hand, the dose-response curve for VIP-stimulated cellular cyclic AMP was biphasic and reflected interaction of this peptide with two classes of receptors. Results obtained with synthetic fragments of VIP and secretin indicate that the receptor having a high affinity for VIP has a low affinity for secretin, interacts with, but does not distinguish among, secretin, secretin 5-27 and [6-tyrosine] secretin or among secretin 14-27, VIP 14-28, VIP 15-28, and increases cellular cyclic AMP when occupied by VIP, but not when occupied by secretin, [6-tyrosine] secretin, or secretin 1-14. The receptor having a low affinity for VIP has a high affinity for secretin, interacts with and distinguishes among secretin, secretin 5-27, and [6-tyrosine] secretin, interacts with secretin 14-27 but not with VIP 14-28 or VIP 15-28, and increases cellular cyclic AMP when occupied by VIP, secretin, [6-tyrosine] secretin, or secretin 1-14.

Animals↗

PubMed1990

Characterization of vasoactive intestinal peptide receptors in retina.

Vasoactive intestinal peptide (VIP) is a neuropeptide having a wide range of effects on a large number of tissues. To gain insight into the role VIP plays in retinal function, VIP receptors in bovine retinal membranes were analyzed in competition binding assays and by affinity labeling studies and compared to VIP receptors in rat liver membranes. In both membrane preparations, high affinity VIP binding sites (KD approximately 1 nM) were detected. Secretin and glucagon, each having close structural homology to VIP, were found to have negligible effects on [125I]VIP binding in retina. In contrast, secretin (KD = 70 nM) was modestly effective in inhibiting [125I]VIP binding to rat liver membranes. Affinity labeling analysis revealed a VIP binding site of 59 kDa in both bovine retinal and rat liver membranes. Digestion of affinity-labeled receptor proteins with endoglycosidase F generated final cleavage products of approx. 45 kDa for both receptors. These results indicate that the retina expresses a high affinity, highly selective VIP receptor thereby supporting a specific function for VIP in this tissue.

Affinity Labels↗

PubMed2002

Inhibition of PC-3 human prostate cancers by analogs of growth hormone-releasing hormone (GH-RH) endowed with vasoactive intestinal peptide (VIP) antagonistic activity.

Vasoactive intestinal peptide (VIP) stimulates the proliferation and invasiveness of malignant prostatic cells. Receptors for VIP and the closely related growth hormone-releasing hormone (GH-RH) show considerable homology and are found in prostatic and other carcinomas. Among various analogs of GH-RH synthesized, JV-1-52 is a non-selective VIP/GH-RH antagonist, whereas JV-1-53 is a VIP antagonist devoid of GH-RH antagonistic effect. In our study, nude mice bearing PC-3 human androgen-independent prostate carcinomas were treated with JV-1-52 or JV-1-53 (20 microg/day, s.c.) for 28 days. Both antagonists produced a similar reduction in tumor volume (62-67%, p < 0.01) and tumor weight (59-62%; p < 0.05) vs. controls and extended tumor doubling-time from 9.1 to about 16 days (p < 0.05). To investigate the mechanisms involved, in another study we compared the effects of JV-1-53 with those of somatostatin analog RC-160. VIP antagonist JV-1-53 reduced tumor weight by 67% (p < 0.01) and suppressed the expression of mRNA for c-fos and c-jun oncogenes by about 34% (p < 0.05), without affecting serum levels of insulin-like growth factor-I (IGF-I). In contrast, RC-160 (50 microg/day) reduced serum IGF-I by 19% (p < 0.05), but did not significantly decrease tumor weight. mRNA for VIP and high affinity receptors for VIP were detected on PC-3 tumors. Our results suggest that VIP/GH-RH antagonists can inhibit the growth of androgen-independent prostate cancer by abrogating the autocrine/paracrine mitogenic stimuli of VIP. The ability of GH-RH antagonists to block tumoral VIP receptors, in addition to GH-RH receptors, could be potentially beneficial for prostate cancer therapy.

Animals↗

PubMed1991

Pituitary adenylate cyclase-activating peptide (PACAP), a new vasoactive intestinal peptide (VIP)-like peptide in the respiratory tract.

Pituitary adenylate cyclase-activating peptide (PACAP) is a vasoactive intestinal peptide (VIP)-like peptide recently isolated from ovine hypothalami. Nerve fibers displaying PACAP immunoreactivity were found in the respiratory tract of rats, guinea pigs, ferrets, pigs, sheep and squirrel monkeys. A moderate supply of PACAP-immunoreactive fibers was seen in the nasal mucosa of guinea pigs. Few to moderate numbers of PACAP-containing fibers occurred in the tracheo-bronchial wall of rats, guinea pigs, ferrets, pigs, sheep and squirrel monkeys. The fibers were distributed beneath the epithelium, around blood vessels and seromucous glands, and among bundles of smooth muscle. In the lungs, the immunoreactive fibers were observed close to small bronchioli. A few PACAP-immunoreactive nerve cell bodies were seen in the sphenopalatine and otic ganglia of guinea pigs. Simultaneous double immunostaining of the respiratory tract of sheep and ferrets revealed that all PACAP-containing nerve fibers stored VIP. We suggest that neuronal PACAP may take part in the regulation of smooth muscle tone and glandular secretion.

Animals↗

PubMed1989

Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody.

Vasoactive intestinal peptide (VIP) labeled with 125I, [Tyr10-125I]VIP, can be hydrolyzed by immunoglobulin G (IgG) purified from a human subject, as judged by trichloroacetic acid precipitation and reversed-phase high-performance liquid chromatography (HPLC). The hydrolytic activity was precipitated by antibody to human IgG, it was bound by immobilized protein G and showed a molecular mass close to 150 kilodaltons by gel filtration chromatography, properties similar to those of authentic IgG. The Fab fragment, prepared from IgG by papain treatment, retained the VIP hydrolytic activity of the IgG. Peptide fragments produced by treatment of VIP with the antibody fraction were purified by reversed-phase HPLC and identified by fast atom bombardment-mass spectrometry and peptide sequencing. The scissile bond in VIP deduced from these experiments was Gln16-Met17. The antibody concentration (73.4 fmol per milligram of IgG) and the Kd (0.4 nM) were computed from analysis of VIP binding under conditions that did not result in peptide hydrolysis. Analysis of the antibody-mediated VIP hydrolysis at varying concentrations of substrate suggested conformity with Michaelis-Menton kinetics (Km). The values for Km (37.9 X 10(-9) M) and the turnover number kcat (15.6 min-1) suggested relatively tight VIP binding and a moderate catalytic efficiency of the antibody.

Amino Acid Sequence↗

PubMed1989

Coronary hemodynamic effects of intravenous vasoactive intestinal peptide in humans.

Vasoactive intestinal polypeptide (VIP), a probable neurotransmitter, is present in the hearts of experimental animals and is a coronary vasodilator in dogs. We evaluated the coronary hemodynamic effects of intravenously infused VIP in 11 men at two rates that modestly raised circulating VIP concentrations. The decreases in coronary and systemic vascular resistances during the second infusion, 33 and 31%, respectively, were slightly but insignificantly greater than the 24% decrease in pulmonary vascular resistance. Coronary sinus levels of 6-keto-prostaglandin F1 alpha were not elevated during the infusions, and cyclooxygenase inhibition did not significantly blunt coronary vasodilation. However, myocardial oxygen uptake rose significantly during both infusions. To test for a direct coronary vasodilator effect, we infused VIP into the left coronary artery of four other men at four levels. The maximum decline in coronary vascular resistance was 46% and was not associated with an increase in myocardial oxygen uptake. We conclude that 1) intravenous administration of low to intermediate doses of VIP in humans is associated with substantial coronary vasodilation, 2) the coronary bed appears to be at least as responsive as other vascular beds, 3) the coronary vasodilation is due to both direct and indirect effects, and 4) the coronary vasodilation does not appear to be mediated by prostaglandins.

Blood Pressure↗

PubMed1992

A further study on the stimulatory effect of peptide histidine methionine on growth hormone secretion in acromegaly: a dose-related study and a comparison with vasoactive intestinal peptide.

We examined whether the GH-releasing effect of peptide histidine methionine (PHM) in acromegaly may be mediated by activation of pituitary receptors for vasoactive intestinal peptide (VIP), which is structurally similar to but more powerful than PHM in stimulating GH secretion in acromegaly. VIP (50 or 100 micrograms) or PHM (50, 100, or 200 micrograms) was given as an i.v. bolus to 11 patients with active acromegaly, and plasma GH levels were measured before and at intervals up to 120 min after the injection. A paradoxical GH response (> 50% and > 6 micrograms/l above the basal) to 50 or 100 micrograms of VIP was observed in 4 (36%) or 5 (45%) patients, respectively. 2 (18%) patients showed paradoxical GH responses to both 50 and 100 micrograms of PHM, and, interestingly, as many as 5 (45%) patients showed positive GH responses to 200 micrograms of PHM. 3 of these 5 responders to 200 micrograms of PHM were also responders to both doses of VIP. To add to, one of the responders to 100 micrograms of VIP did not show a positive GH response to even 200 micrograms of PHM. These results may suggest that in at least some acromegalics the PHM stimulation of GH secretion is mediated by activation of pituitary VIP receptors by PHM and/or by PHM binding to its specific receptors which may have appeared concomitantly with VIP receptors. However, the occasional heterogeneity of the VIP- and PHM-induced GH responses may suggest that on some somatotroph adenomas either VIP or PHM receptors may appear independently.

Acromegaly↗

PubMed1996

Production, analysis and bioactivity of recombinant vasoactive intestinal peptide analogs.

Recombinant vasoactive intestinal polypeptide (VIP) analogs were expressed in Escherichia coli as a fusion protein containing tandemly repeated multiple copies of a synthetic VIP gene joined to glutathione S-transferase. The encoded protein contains VIP units separated by a linker peptide, potentially excisable by a double cleavage with endoprotease factor Xa and hydroxylamine. Expression of different polyVIP genes, from 1 to 32 units, was detected and the production of a 16 VIP polymer was performed. MonoVIP analogs appended by 5 or 10 amino acids at their C terminus were released by factor Xa from this polymerized product. They were then submitted to hydroxylamine cleavage to remove the linker sequence to finally obtain a recombinant VIP analog devoid of any amino acid extension. The biological activity of the recombinant polyVIP and VIP analogs was tested. Although less efficient than the natural neuropeptide, some of these components bound to VIP receptor, activated adenylate cyclase in human colonic adenocarcinoma cells and displayed a relaxation activity on guinea pig tracheal rings.

Amino Acid Sequence↗