SEARCH · PubMed Health

Results for “Vasoactive Intestinal Peptide”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 145 records · Page 8Linked to original sources

PubMed1985

Effect of resection of small intestine on the interaction of vasoactive intestinal peptide with rat colonic epithelial cells.

Vasoactive intestinal peptide (VIP) receptors and VIP-dependent cyclic AMP production were studied in rat colonic epithelial cells 3 days after a 60% resection of the small intestine. Basal cyclic AMP levels were similar in both control and resected animals. The potency, but not the efficiency, of the peptide on the stimulation of cyclic AMP production was diminished in cells from resected rats. Accordingly, the affinity of VIP receptors, but not the binding capacity, decreased as a consequence of the loss of a part of the small intestinal mucosa. These observations are consistent with the known inhibitory role of cyclic AMP on cell proliferation in colonic epithelium and other tissues and suggest a participation of VIP acting through the cyclic nucleotide in the compensatory hyperproliferative response of the colon following massive resection of the small intestine.

Animals↗

PubMed1989

Peptide histidine methionine and vasoactive intestinal peptide: occurrence and relaxant effect in the human female reproductive tract.

The occurrence of the neuropeptides peptide histidine methionine (PHM) and vasoactive intestinal peptide (VIP) in the human female genital tract was studied by means of immunochemistry and radioimmunoassay in combination with gel chromatography. In addition, the effect of PHM and VIP on smooth muscle activity was investigated in vitro. The regional distribution of PHM as determined by radioimmunoassay correlated with that of VIP. This finding agreed with the immunohistochemical data, which, in addition, provided evidence for colocalization of the two peptides in nerve fibers. These fibers were most abundant in the vagina and the uterine cervix, where they seemed to innervate blood vessels, smooth muscle, and epithelial cells. The concentrations of immunoreactive PHM and VIP were found to be similar in all areas except in the vagina, where the PHM concentration was fourfold that of VIP. Gel chromatography of vaginal extract revealed a high concentration of a C-terminally extended form of PHM, suggesting differential processing pathways of the VIP precursor. Both PHM and VIP inhibited, in a dose-dependent manner, the smooth muscle activity in strips from the Fallopian tube and the myometrium. Administered in combination, PHM and VIP had an additive effect and displayed the same efficacy as VIP alone, indicating that the peptides act via a common receptor.

Adult↗

PubMed1989

Disruption of the optic pathway during development affects vasoactive intestinal peptide mRNA expression.

Vasoactive intestinal polypeptide (VIP) is a regulatory peptide widely distributed in the central and peripheral nervous systems. To understand the activities of VIP it is necessary to study the mechanisms governing its production. The highest concentration of VIP-producing cells occurs in the suprachiasmatic nucleus (SCN) of the hypothalamus. Because the SCN is directly innervated by the optic nerve, we decided to investigate the effect of visual input on VIP gene expression. By means of Northern blot hybridization, we measured VIP mRNA levels in the hypothalami of 36-day-old normal rats and rats that had been enucleated at birth. The concentration of VIP mRNA in the hypothalami of enucleated rats was approximately double that in the hypothalami of normal rats. In contrast, the concentration of VIP mRNA in the cerebral cortex significantly decreased after enucleation. The concentrations of VIP mRNA were also measured by in situ hybridization to brain sections. The hypothalamic VIP mRNA was located mainly in the SCN. Enucleation resulted in an increase of VIP transcripts in the SCN. These results indicate that visual input may participate in the regulation of VIP production.

Animals↗

PubMed1989

Characterization and regional distribution of peptides derived from the vasoactive intestinal peptide precursor in the normal human brain.

To study the biosynthetic processing of the precursor for vasoactive intestinal peptide (prepro-VIP) in the human brain, we have developed antisera against the five functional domains of the precursor molecule: prepro-VIP 22-79, peptide histidine methionine (PHM), prepro-VIP 111-122, VIP, and prepro-VIP 156-170. The antisera were used in radioimmunoassays in combination with HPLC to identify and quantify the peptides in regions of the human brain. All five peptides were expressed, but mainly in nonequimolar ratios. In only three regions were the same amounts of VIP and PHM found; in the remaining areas the concentration of PHM was two-thirds that of VIP. The concentrations of prepro-VIP 22-79, prepro-VIP 111-122, and prepro-VIP 156-170 were considerably lower than the corresponding VIP concentrations, and the relative concentration of prepro-VIP 111-122 differed between cortical and subcortical areas. A small proportion of the VIP precursor followed a pathway in which the dibasic conversion site after PHM is not cleaved, as evidenced by the presence of a C-terminally extended form of PHM. Finally, it was found that the C-terminal lysine residue of prepro-VIP is not removed during processing. The findings indicate that differences in the posttranslational processing of prepro-VIP exist in subpopulations of neurons in the human brain.

Aged↗

PubMed1985

Effect of vasoactive intestinal peptide on isolated perfused rat kidney.

Vasoactive intestinal peptide, a polypeptide neurotransmitter, stimulates salt secretion by the mammalian intestine and the rectal gland of the dogfish shark. Because of the recent identification of vasoactive intestinal peptide in renal nerves, the present study was undertaken to investigate its effects on the isolated perfused rat kidney. The addition of vasoactive intestinal peptide to the recirculating perfusate produced a significant increase in urine volume, fractional excretion of sodium, chloride, and potassium, as well as osmolar clearance when compared with control kidneys. These changes associated with addition of vasoactive intestinal peptide occurred without any significant changes in perfusion flow, renal vascular resistance, or inulin clearance. These experiments strongly suggest an action of vasoactive intestinal peptide on renal tubular reabsorption.

Animals↗

PubMed1990

Selectivity for binding of peptide analogs to vascular receptors for vasoactive intestinal peptide.

The structure-activity relationships for vasoactive intestinal peptide (VIP) receptor binding were studied using N-terminally modified VIP analogs. VIP fragments, and VIP receptor antagonists. Tissue sources included bovine coronary artery, rat mesenteric artery, rat pituitary, rat brain synaptosomes, and rat liver. Experimental conditions for receptor binding were maintained as near to identical as possible. The competitive binding curves for VIP analogs were similar in the bovine and rat vascular preparations. However, appreciable differences were observed between the vascular and other preparations. The vascular receptors discriminated between [D-His1]VIP and [Phe1]VIP, whereas the receptors in other tissues did not. The greatest selectivity was found for [D-Ala4]VIP, which was among the lowest affinity analogs tested on the vasculature but among the highest affinity analogs in the other preparations. The rank orders of analog potencies were comparable for the rat brain and pituitary receptors. The rat liver VIP receptor differed from its counterpart in brain and pituitary predominantly by discriminating between [D-Phe2]VIP and [D-Arg2]VIP. The two VIP receptor antagonists bound weakly and nonselectively to all receptor preparations. Integrity of the full VIP molecule was necessary for full potency of binding to the vascular receptor. We conclude that the vascular VIP receptor possesses recognition properties that are distinct from those for VIP receptors in liver, pituitary, or brain.

Animals↗

PubMedDate not supplied

NMR study of five N-terminal peptide fragments of the vasoactive intestinal peptide: crucial role of aromatic residues.

Five peptides related to the N-terminal sequence of the vasoactive intestinal peptide (VIP) have been synthesized. Two-dimensional nuclear magnetic resonance (2D-NMR) experiments (i.e., correlated spectroscopy [COSY]) and low temperature coefficient measurements for particular NH chemical shifts suggest the presence of hydrogen bondings in both VIP (1-7, and VIP (1-11) fragments. Nuclear Over-hauser enhancement spectroscopy (NOESY) show that aromatic interactions stabilize a preferred conformation. The crucial role of the first histidine residue, which is a determinant for the biological activity, is explained by specific interactions with the aromatic protons of Phe6 and Tyr10.

Amides↗

PubMed1993

Peptide histidine methionine and vasoactive intestinal peptide levels in human cerebrospinal fluid: age-related changes and absence of a correlation with serum prolactin.

Serum levels of prolactin (PRL), peptide histidine methionine (PHM) and vasoactive intestinal peptide (VIP) were measured in 97 subjects and cerebrospinal fluid (CSF) levels of PHM and VIP were measured in 50 subjects by specific radioimmunoassays to investigate correlations between them. The chromatographic studies revealed that PHM and C-terminal extended form of PHM, peptide histidine valine occurred in human serum and CSF. Significant age-related increases of CSF PHM (P < 0.02) were observed in both males and females, whereas an age-related decrease of serum PRL level was found in females (P < 0.01). In contrast, neither serum VIP, serum PHM nor CSF VIP changed significantly with age. There was a significant positive correlation (P < 0.002) between VIP and PHM in serum, but not in CSF. The close relation between VIP and PHM in serum meets one's expectation because of their derivation from a common precursor. In CSF, these two peptides did not change in parallel with each other. These results may reflect the alteration in metabolism of PHM in CSF. Finally, there was no correlation between serum PRL concentrations and either serum or CSF levels of the peptides, suggesting that neither VIP nor PHM levels in CSF as well as in serum can influence the basal PRL secretion in subjects without endocrine disorders.

Adolescent↗

PubMed1985

Molecular forms of peptide histidine isoleucine-like immunoreactivity in the gastrointestinal tract. Nonequimolar levels of peptide histidine isoleucine and vasoactive intestinal peptide in the stomach explained by the presence of a big peptide histidine isoleucine-like molecule.

Regional specific antibodies and chromatography were used to analyze the distributions and molecular forms of peptide histidine isoleucine (PHI) and vasoactive intestinal peptide (VIP) in the porcine intestine. Both peptides were present along the entire length of the intestine, the highest concentrations occurring in the colon. Concentrations of PHI immunoreactivity, measured with three different antisera, and VIP immunoreactivity were approximately equal in all parts of the gastrointestinal tract except in the stomach. In the stomach, the concentration of PHI immunoreactivity, measured with the N-terminally directed antibody R8403, although equal to the corresponding VIP concentration, was two to four times higher than the PHI immunoreactivity detected with the two C-terminally directed PHI antisera T33 and T41. Chromatographic analysis on Sephadex G-50 superfine of gastric extracts revealed only one VIP immunoreactive peak that eluted in the same position as the porcine VIP standard, at Kav 0.53. A PHI immunoreactive peak was also detected with the C-terminally directed PHI antisera in the same position as porcine PHI standard. However, with the N-terminally directed PHI antiserum R8403, an additional PHI immunoreactive peak was detected in gastric extracts constituting the predominant form present, and this peak eluted earlier at Kav 0.37. The PHI immunoreactive material that eluted earlier was present in the rest of the intestine in only small amounts. As VIP and PHI are believed to be derived from a common precursor, it is suggested that in the stomach the posttranslational enzymic processing of the precursor is different from that in the other parts of the intestine.

Animals↗

PubMed1997

Anally projecting neurons exhibiting immunoreactivity to galanin, nitric oxide synthase and vasoactive intestinal peptide, detected by confocal laser scanning microscopy, in the intestine of the Atlantic cod, Gadus morhua.

The projections of enteric neurons showing immunoreactivity for vasoactive intestinal peptide (VIP), nitric oxide synthase (NOS) and galanin were investigated in the myenteric plexus of the intestine of the Atlantic cod, Gadus morhua. Quantification of immunoreactive material on the proximal and distal side of a myotomy was performed by means of confocal laser scanning microscopy. NOS immunoreactivity was reduced anal to the myotomy, whereas there was an accumulation of immunoreactivity for VIP and for galanin oral to the cut. These results suggest the presence of VIP, NOS and galanin in neurons with oral-to-anal projections along the intestine of the cod. Since descending neurons in the myenteric plexus of many other vertebrates also contain these substances, we conclude that the oral-to-anal projections of neurons containing VIP, NOS and galanin are highly conserved features and important for the descending phase of intestinal peristalsis on an evolutionary basis.

Anal Canal↗

PubMed1998

An improved method to obtain a single recombinant vasoactive intestinal peptide (VIP) analog.

The vasoactive intestinal peptide (VIP) is an ubiquitous peptide of great potential for applications. Development of new bioactive VIP analogs using production in recombinant E coli has been carried out in our laboratory. This work presents a new multimeric fusion protein expressing several VIP units separated by factor Xa cleavage site linkers. The steps leading from the affinity purification of the fusion protein and its processing by the factor Xa to the full characterization of the new bioactive improved VIP analog are also described.

Base Sequence↗

PubMed1983

In vivo bronchodilator activity of vasoactive intestinal peptide in the cat.

Vasoactive intestinal peptide (VIP) is an octacosapeptide that occurs widely in the animal kingdom, is distributed in many organs and tissues, and has a broad range of biologic actions. We evaluated the ability of VIP to produce bronchodilation in anesthetized, mechanically ventilated, atropinized, closed chest cats. Boluses of VIP injected intravenously (0.1 to 10 micrograms X kg-1) reversed in a dose-dependent manner the increase in lung resistance (RL) and the decrease in dynamic lung compliance (Cdyn) induced by an intravenously administered infusion of 5-hydroxytryptamine (5HT) (5 to 30 micrograms X kg-1 X min-1). Distribution of bronchodilator activity was assessed by using RL as an index of central airways caliber and dynamic elastance (Edyn; the inverse of Cdyn) as an index of tone in peripheral airways and lung parenchyma. Although all levels of the tracheobronchial tree responded to VIP, the predominant site of action appeared to be in central airways. A similar distribution and magnitude of relaxant effects were observed after the intravenous administration of prostaglandin E2 (PGE2) (0.1 to 10 micrograms X kg-1). Prostaglandin E2 also was effective in reversing 5HT-induced bronchoconstriction when given by ultrasonic nebulization, whereas VIP was not. Bronchodilation mediated by VIP persisted after pretreatment with indomethacin or propranolol. We conclude that VIP is a potent relaxant of feline airways smooth muscle in vivo and that this effect of the peptide occurs independent of prostaglandin production or beta adrenergic receptor activation.

Animals↗

PubMed1988

Opiate modulation of the stress-induced increase of vasoactive intestinal peptide (VIP) in plasma.

Vasoactive intestinal peptide (VIP) has a variety of extra-intestinal actions which are typical of the body's reaction to stress, such as lipolysis, glycogenolysis and modulation of anterior pituitary hormone secretion. Serial VIP plasma concentrations in patients undergoing major laparotomies were determined. The influence of the mu-receptor agonist, fentanyl, on intra-operative changes was investigated and compared to a control group receiving halothane anesthesia. Plasma levels of typical "stress hormones" cortisol and catecholamines were also monitored for additional information on the extent of perioperative stress. VIP levels increased intraoperatively in the halothane group from 5.9 +/- 4.6 to 15.3 +/- 5.3 pmol/l. Cortisol and catecholamine levels showed a similar increase. The intraoperative VIP increase in the fentanyl group was significantly smaller: 3.5 +/- 1.9 to 7.3 +/- 3.6 pmol/l. Anesthesia itself did not affect VIP concentrations as shown by constant levels during a 30 minute preoperative control period. The observed increases of VIP plasma concentration are thought to reflect a possible role for VIP in the hormonal metabolic response to stress. The attenuation of the increase by fentanyl might be due to a direct opiate action on VIP release.

Anesthesia, Inhalation↗

PubMed1989

Solubilization of active and stable receptors for vasoactive intestinal peptide from rat liver.

Vasoactive intestinal peptide (VIP) receptors were solubilized from rat liver using the zwitterionic detergent CHAPS. Optimal conditions of solubilization were obtained with 5 mM CHAPS and 2.5 mg protein/ml. The binding of 125I-VIP to CHAPS extracts was time- and pH-dependent, saturable and reversible. The following order of potency of unlabeled VIP-related peptides for inhibiting 125I-VIP binding was observed: VIP greater than helodermin greater than peptide histidine isoleucine amide (PHI) greater than rat growth hormone releasing factor (rGRF) greater than secretin. This peptide specificity is identical to that of rat liver membrane-bound receptors. VIP binding activity in the CHAPS extract was destroyed by trypsin or dithiothreitol in accordance with the known sensitivity of membrane-bound receptors to these agents. VIP receptors in CHAPS extracts were stable for at least 5 days at 4 degrees C. Scatchard analysis of equilibrium binding data indicated the presence in CHAPS extracts of high (H) and low (L) affinity binding sites with the following characteristics: KdH = 0.27 nM and BmH = 34 fmol/mg protein; KdL = 51 nM and BmL = 1078 fmol/mg protein. The guanine nucleotide GTP inhibited 125I-VIP binding to soluble receptors and enhanced the dissociation of soluble VIP-receptor complexes, suggesting that GTP-binding proteins were functionally associated with VIP receptors in solution. Gel filtration of solubilized VIP receptors on Sephacryl S-300 revealed a single binding component with a Stokes radius of 6.1 nm. It is concluded that active VIP receptors can be extracted from liver membranes by CHAPS. The availability of this CHAPS-soluble, stable and functional receptor from a tissue which can be obtained in large amounts represents a major step toward the purification of VIP receptors.

Animals↗

PubMed1996

Nitrergic inhibition of migrating myoelectric complex in the rat is mediated by vasoactive intestinal peptide.

The role of vasoactive intestinal peptide (VIP) for the action of nitric oxide (NO) as a nonadrenergic noncholinergic inhibitory mediator was investigated regarding effects on migrating myoelectric complex (MMC) in rat. Animals were supplied with implanted bipolar electrodes at 5, 15 and 25 cm distal to pylorus for electromyography of small intestine. First, basal recordings with saline were followed by intravenous infusions of glyceryl trinitrate or VIP at different infusion rates to achieve dose-response relationships. Second, effects of different doses of the nitric oxide synthase inhibitor, N omega-nitro-L-arginine (L-NNA) were studied. Third, the action of L-NNA (1 mg kg-1) on the effect of VIP (500 pmol kg-1 min-1), and of the VIP receptor antagonist (4-Cl-D-Phe6, Leu17), VIP (45 nmol 20 min-1), on the action of glyceryl trinitrate (44 nmol kg-1 min-1) was investigated. Glyceryl trinitrate prolonged the MMC cycle length from 16.3 +/- 1.3 to 44.9 +/- 8.0 min (P < 0.001), while VIP completely disrupted the MMC for the whole infusion period (P < 0.05). Higher doses of either compound induced quiescence. L-NNA shortened MMC cycle length from 14.7 +/- 1.2 to 8.6 +/- 1.4 min (P < 0.05), increased its propagation velocity from 2.0 +/- 0.4 to 18.3 +/- 8.4 cm min-1 (P < 0.01) and increased calculated length from 6.3 +/- 1.0 to 55.4 +/- 18.4 cm (P < 0.01). Pretreatment with (4-Cl-D-Phe6, Leu17) VIP blocked the inhibitory action of glyceryl trinitrate and preserved MMC pattern (P < 0.05). In contrast, L-NNA had no effect on the inhibition of MMC caused by VIP. Our results indicate that inhibition of MMC is related to production of NO, which may mediate its actions through VIP.

Animals↗

PubMed1999

Targeting of embryonic and postnatal autonomic and enteric neurons with a vasoactive intestinal peptide transgene.

The neuropeptide vasoactive intestinal peptide (VIP) is expressed in several distinct sites in the CNS, in cholinergic and enteric ganglia, and in a small subpopulation of neurons within sympathetic ganglia. Previous studies on the human VIP gene indicate that transcription in neural crest-derived neuroblastoma and pheochromocytoma cell lines is controlled in part by multiple regulatory elements located along 4.5 kb of upstream 5' flanking sequence. In the current studies, transgenic mice were created with a chimeric gene consisting of 16.5 kb of the mouse VIP gene fused to the beta-galactosidase reporter. In situ hybridization analysis in adult mice indicated that reporter gene expression was correctly targeted to neurons in the esophagus, stomach, small intestine, and colon. No expression was observed in the brain, including regions that contain abundant VIP-expressing cells, such as the thalamus, amygdala, cerebral cortex, hippocampus, and suprachiasmatic nucleus. Analysis of transgene expression in neonatal and embryonic day 13.5 mice revealed a near perfect correlation between VIP and beta-galactosidase gene expression in cranial cholinergic ganglia and the superior cervical ganglia, and lack of transgene expression in sensory ganglia and in nonneuronal tissue. Potential ectopic transgene expression was observed in neonates, in the cerebellar external granule layer and in a small subpopulation of neurons in the olfactory epithelium. We conclude that the 16.5 kb of VIP gene used in these studies contains sequences sufficient for directing expression specifically to VIP neurons in the PNS, and that sequences located elsewhere on the gene are required for proper CNS expression. The VIP gene sequences used here should be capable of targeting other gene products to specific populations of embryonic and adult peripheral neurons without causing significant expression in the CNS.

Aging↗

PubMed1980

In vitro stimulation of prolactin release by vasoactive intestinal peptide.

The effect of vasoactive intestinal peptide (VIP) on anterior pituitary hormone release was examined in a variety of in vitro preparations. Synthetic VIP was capable of stimulating increased prolactin (PRL) release from male rat hemipituitaries in doses as low as 10-9M only when the enzyme inhibitor bacitracin was present in the incubation medium. Natural porcine VIP was similarly capable of stimulating PRL release, but only at higher doses (10-6M). Additionally, synthetic VIP was capable of stimulating PRL release from dispersed anterior pituitary cells harvested from adult male and lactating female rats and from an enriched population of lactotrophs obtained by unit gravity sedimentation of similar dispersed cells from infantile female rats. No effect of VIP on luteinizing hormone, growth hormone or thyroid stimulating hormone release was seen. These findings taken in concert with the presence of VIP in the hypothalamus, pituitary and hypophyseal portal plasma of the rat suggest a physiological role for VIP in the control of PRL secretion.

Animals↗

PubMed2001

Isolation, maintenance, and characterization of human pancreatic islet tumor cells expressing vasoactive intestinal peptide.

Tissue from a vasoactive intestinal peptide (VIP)-secreting human tumor has been used to establish and characterize human neuroendocrine primary cell cultures from which permanent, clone-derived cell lines have been established. Viable cells were obtained by enzymatic and mechanical dissociation of freshly resected pancreatic islet tumor and hepatic metastatic tumor tissues. Aliquots of tumor cells were established ex vivo under culture conditions including porous substrata coated with type IV collagen and laminin and a low serum, hormonally defined culture medium. The small (<10 microm) rounded, grape-like cells had a very slow growth rate of doubling times estimated at several weeks or more. After several passages, morphologically uniform cells were derived that strongly expressed neuroendocrine markers of synaptophysin and synaptobrevin. Although chromogranin A and VIP had somewhat weaker expression, both demonstrated phorbol ester-stimulated secretion. The morphologic and secretory properties were maintained by the cells for nearly 2 years in culture. The establishment of this novel VIP-secreting human neuroendocrine cell line (HuNET) makes available a culture model with which to study a transformed version of this pancreatic islet cell type and offers approaches by which to establish islet tumor cell lines.

Adult↗