Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20366 (substance P)
 21,176 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. We have used micropuncture techniques to study the regulation of fluid secretion by interlobular ducts isolated from the pancreas of copper-deficient rats. 2. Ducts isolated from different strains of Wistar rats exhibited quantitative differences in basal fluid secretion; however, secretion rates measured in the presence of secretin were similar. 3. Vasoactive intestinal peptide had no effect on fluid transport. 4. Bombesin stimulated fluid secretion, and this effect was abolished by removal of extracellular bicarbonate. 5. Substance P inhibited basal secretion, and that stimulated by bombesin and secretin. These inhibitory effects were partially reversed by spantide. 6. Substance P also inhibited fluid secretion stimulated by dibutyryl cyclic AMP and forskolin. This places the site of inhibition mediated by substance P at a point in the secretory mechanism distal to the generation of cyclic AMP. 7. We conclude that rat pancreatic duct cells possess receptors for bombesin and substance P, in addition to 'secretin-preferring' receptors. Since VIP had no effect on fluid transport, it is unlikely that 'VIP-preferring' receptors are present on rat duct cells.
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PMID:Effect of vasoactive intestinal peptide, bombesin and substance P on fluid secretion by isolated rat pancreatic ducts. 169 81

Gastrin-releasing peptide (GRP) and bombesin can stimulate pepsinogen release by both gastrin-dependent and -independent mechanisms. Using isolated guinea pig gastric chief cells, we determined that GRP can act directly on the guinea pig chief cell to cause pepsinogen release. GRP and bombesin stimulated a 2.5- to 3-fold increase in pepsinogen release above basal release. Substance P also stimulated a small but significant increase in pepsinogen release. No gastrin immunoreactivity was detected in the supernatants of cells stimulated with up to 1 microM GRP or bombesin or 1 mM carbachol. GRP-stimulated pepsinogen release was completely inhibited by GRP/bombesin receptor agonists as well as substance P receptor antagonist but not by antagonists to receptors for gastrin, the octapeptide of cholecystokinin (CCK-8), secretin, vasoactive intestinal peptide (VIP), or muscarinic agents. Substance P-stimulated pepsinogen release was completely inhibited by substance P receptor antagonist but not by GRP/bombesin receptor antagonists. An additive effect on pepsinogen release was seen when GRP was combined with maximally effective concentrations of adenosine 3',5'-cyclic monophosphate (cAMP)-mediated agents (VIP, secretin, 8-BrcAMP) but not with calcium-mediated agents (carbachol, CCK-8, gastrin). These results indicate that GRP can directly stimulate pepsinogen release from guinea pig chief cells by a specific GRP receptor that mobilizes intracellular calcium.
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PMID:Gastrin-releasing peptide directly releases pepsinogen from guinea pig chief cells. 170 Jun 25

The ability to assess the importance of secretin in various physiological processes is limited by the lack of specific potent antagonists. Recently, reduced peptide bond (psi) analogues of bombesin or substance P in which the -CONH- bond is replaced by -CH2NH- are reported to be receptor antagonists. To attempt to develop a new class of secretin receptor antagonists, we have adopted a similar strategy with secretin and sequentially altered the eight NH2-terminal peptide bonds, the biological active portion of secretin. In guinea pig pancreatic acini, secretin caused a 75-fold increase in cyclic AMP (cAMP). Secretin inhibited 125I-secretin binding with a half-maximal effect at 7 nM. Each of the psi analogues inhibited 125I-secretin binding. [psi 4,5]Secretin was the most potent, causing the half-maximal inhibition at 4 microM, and was 2-fold more potent than the [psi 1,2]secretin; 7-fold more than [psi 3,4]secretin, [psi 5,6]secretin, and [psi 8,9]secretin; 9-fold more than [psi 7,8]secretin; 13-fold more potent [psi 6,7]secretin, and 17-fold more than [psi 2,3]secretin. Secretin caused a half-maximal increase in cAMP at 1 nM. At concentrations up to 10 microM, [psi 2,3]secretin, [psi 4,5]secretin, and [psi 8,9]secretin did not alter cAMP whereas [psi 1,2]secretin and [psi 6,7]secretin caused a detectable increase in cAMP at 10 nM, [psi 7,8]secretin at 300 nM, [psi 5,6]secretin at 1 microM, and [psi 3,4]secretin at 10 microM. The [psi 4,5], [psi 2,3], and [psi 8,9] analogues of secretin each inhibited 1 nM secretin-stimulated cAMP as well as [psi 3,4]secretin, which functioned as a partial agonist. [psi 4,5]Secretin was the most potent, causing half-maximal inhibition at 3 microM whereas [psi 8,9]secretin was 6-fold less potent, and [psi 2,3]secretin and [psi 3,4]secretin were 17-fold less potent. [psi 4,5]Secretin inhibited secretin-stimulated cAMP and binding of 125I-secretin in a competitive manner. [psi 4,5]Secretin did not interact with cholecystokinin, bombesin, calcitonin gene-related peptide, or cholinergic receptors but did interact with receptors for vasoactive intestinal peptide, causing half-maximal inhibition at 72 microM and thus had a 18-fold higher affinity for secretin than vasoactive intestinal peptide receptors. These results indicate that reduced peptide bond analogues of the NH2 terminus of secretin represent a new class of secretin receptor antagonists. It is likely that in the future even more potent members of this class can be developed which may be useful to investigate the role of secretin in various physiological processes.
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PMID:Reduced peptide bond pseudopeptide analogues of secretin. A new class of secretin receptor antagonists. 170 23

The effect of sepsis on plasma levels of various gut peptides was studied in rats. Sepsis was induced by cecal ligation and puncture (CLP); control animals underwent sham operation. Sixteen hours after CLP or sham operation, portal and systemic blood was drawn, and plasma levels of gastrin, vasoactive intestinal peptide (VIP), secretin, peptide YY (PYY), gastrin-releasing peptide (GRP), and substance P were determined by radioimmunoassay. Plasma levels of gastrin, VIP, PYY, and secretin were elevated in septic rats compared with nonseptic animals, with the highest levels noted in portal blood. There was no effect of sepsis on GRP or substance P levels. In other experiments, human recombinant interleukin 1 alpha (IL-1 alpha) or recombinant tumor necrosis factor alpha (TNF alpha) was injected intraperitoneally (300 micrograms/kg body weight in 3 divided doses over 16 hours). There was no change in plasma levels of gut peptides after IL-1 alpha injection. TNF alpha induced elevation of PYY levels in portal plasma with no change in other gut peptide levels. The results suggest that sepsis stimulates release of certain gut peptides and that TNF, but not IL-1, may be partly responsible for this response. The mechanism of the release of gut peptides and its significance in the pathophysiologic changes induced by sepsis remain to be determined.
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PMID:Effect of sepsis or cytokine administration on release of gut peptides. 173 67

1. Corticotropin-stimulated lipolysis in adipocytes of rats, mice, hamsters, guinea pigs and rabbits. Melanotropins elicited high lipolytic activity only in guinea pig and rabbit adipocytes. Opiate peptides were active only in rabbit adipocytes. Pituitary and chorionic gonadotropins and somatotropin were lipolytic in guinea pig adipocytes. Other hormones tested including prolactin, somatostatin, substance P, neurotensin, angiotensin II, thyrotropin releasing hormone and pancreatic polypeptide were devoid of lipolytic activity in all of the adipocytes studied. 2. In the rabbit adipocytes gamma-melanotropin was lipolytic only at high doses. At these doses the peptide inhibited the lipolytic response to a high dose of corticotropin. 3. Lipolysis stimulated by vasoactive intestinal peptide and epinephrine in rat adipocytes was antagonized by insulin. The lipolytic hormones corticotropin, epinephrine, vasoactive intestinal peptide and secretin suppressed basal and insulin-stimulated lipogenesis.
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PMID:Studies on hormonal regulation of lipolysis and lipogenesis in fat cells of various mammalian species. 196 44

The proximal duodenum of eight marsupial species, (koala, common brushtail possum, ring-tailed possum, common wombat, great grey kangaroo, parma wallaby, short-nosed bandicoot and tiger cat) were investigated immunohistochemically using 12 specific antisera for gut hormones. Several types of immunoreactive cells were seen on the intestinal villi and in crypts of these species: 9 types in the koala; 8 types in the common brushtail possum; 7 types in the common wombat; 6 types in the short-nosed bandicoot and 5 types in the ringtailed possum, great grey kangaroo, parma wallaby and tiger cat. Gastrin-, somatostatin-, motilin- and serotonin-immunoreactive cells were seen in all species examined. A few BPP-, enteroglucagon-, CCK-, secretin-, GIP- and neurotensin-immunoreactive cells were seen but only in few species. A few substance P-immunoreactive cells were detected only in the koala. Immunoreactive cells were also seen in Brunner's glands: 5 types in the parma wallaby; 3 types in the great grey kangaroo and tiger cat; 2 types in the koala and common wombat; 1 type in the short-nosed bandicoot. No immunoreactive cells were found in Brunner's glands of the common brushtail possum.
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PMID:An immunohistochemical study of endocrine cells in the proximal duodenum of eight marsupial species. 218 87

Although the histological features and endocrine cells of the gastro-intestinal tract of the chicken have been well studied, little is known about these features of the gut of the ostrich. The present study was undertaken to elucidate the histology and peptide-storing endocrine cells of the ostrich. As a rule the histological features of the gastro-intestinal tract of the ostrich corresponded to that of the fowl. However, certain differences were observed. The superficial proventricular glands were simple, branched tubular glands, while the deep proventricular glands were restricted to a slipper-shaped area and extended into the muscularis mucosae. The gizzard had a variably developed muscularis mucosae, a feature that seems to be unique to the ostrich. The villi of the small intestine were long and branched profusely, forming a labyrinthine surface. No Paneth cells were observed. The mucosa of the ceca and the first part of the rectum was thrown in large circular folds, forming a compressed spiral. Numerous melanocytes were seen in the submucosa and the connective tissue around the bloodvessels of the muscle layers at the tips of the ceca. A well developed subserosa was present throughout the gastro-intestinal tract. Endocrine cells immunoreactive to somatostatin, glucagon, gastrin, bombesin, neurotensin, substance P and pancreatic polypeptide were detected in the gastro-intestinal tract of the ostrich. The topographical distribution of those endocrine cells immunoreactive to glucagon, bombesin, neurotensin and substance P differed from that of the chicken. The results of this investigation inferred that at least one of the gut peptides of the ostrich (secretin) to be structurally different from its counterparts in mammal and chicken. Molecular heterogeneity of somatostatin was observed in endocrine cells situated in the deep ventricular glands of the ostrich.
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PMID:A light microscopic and immunocytochemical study of the gastrointestinal tract of the ostrich (Struthio camelus L.). 233 97

The regional distribution and relative frequency of argyrophil cells, and of cells immunoreactive for 5-hydroxytryptamine (5-HT), substance P (SP), somatostatin, glicentin, glucagon, bovine pancreatic polypeptide (BPP), gastrin, leucine-enkephalin, gastric inhibitory polypeptide (GIP), cholecystokinin, secretin, motilin, and neurotensin were studied in 9 segments from the gastrointestinal tract of cows (greater than 1 year old) and calves (less than 3 months old). Argyrophil cells, 5-HT-immunoreactive cells, and somatostatin-immunoreactive cells were distributed throughout the gastrointestinal tract, whereas the other immunoreactive cells were more restricted in distribution. Most endocrine cells were more numerous in the calf than in the cow. This feature was most conspicuous in the abomasum. In the abomasum, argyrophil cells in the cow and calf and 5-HT-immunoreactive cells in the calf were found predominantly in the fundic region, whereas somatostatin-immunoreactive cells and gastrin-immunoreactive cells in the cow and calf and 5-HT-immunoreactive cells in the cow were most numerous in the pyloric region. Substance P-, glucagon-, BPP-, and leucine-enkephalin-immunoreactive cells were rarely detected. In the small intestine, argyrophil cells, 5-HT-, SP-, somatostatin-, gastrin-, GIP-, cholecystokinin-, secretin-, and motilin-immunoreactive cells were most numerous in the duodenum. Neurotensin-, glicentin-, glucagon-, and BPP-immunoreactive cells were detected with the highest frequency in the ileum. In the large intestine, argyrophil cells and 5-HT-, glicentin-, BPP-, somatostatin-, glucagon-, and SP-immunoreactive cells occurred with the highest frequency in the rectum.
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PMID:Histologic and immunocytochemical study of endocrine cells in the gastrointestinal tract of the cow and calf. 241 Nov 74

A whole mount immunofluorescence method was used for the localization of immunoreactivity (IR) to four regulatory peptides and the bioamine serotonin in the nervous system of Stenostomum leucops (Turbellaria, Platyhelminthes). The flatworm S. leucops belongs to the taxon Catenulida which, according to the new phylogenetic system by Ax [2], forms a key group between the coelenterates and more advanced flatworm species. Positive IR was obtained using antisera against FMRF-amide, beta-endorphin, growth hormone releasing factor (GRF), substance P, and serotonin. The distribution patterns of these neuropeptide-like immunoreactivities differ significantly from each other. Antisera against Leu-enkephalin, bovine pancreatic polypeptide (BPP), bombesin, cholecystokinin (CCK-8), neurotensin, somatostatin, growth hormone (GH), secretin, and neurophysin II gave negative results. This primitive flatworm shows similarities with hydra in the lack of IR to anti-somatostatin, anti-Leu-enkephalin, and anti-BPP. These antisera give positive IR in more advanced flatworm species, indicating a later convergent evolution of vertebrate-like peptides within the phylum Platyhelminthes.
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PMID:Neuropeptides in a microturbellarian--whole mount immunocytochemistry. 242 Dec 67

The contractile effect of various neuropeptides was examined by pressure ejecting these agents from a pipette onto single smooth muscle cells freshly dissociated from the stomach of Bufo marinus. Substance P, cholecystokinin-octapeptide, and bombesin caused contraction, whereas vasoactive intestinal peptide, secretin, and dopamine inhibited acetylcholine-induced contractions. Acetylcholine and the three peptides which produced contraction were found in some instances to act on the same cell, suggesting that receptors for these agents exist on one and the same cell.
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PMID:Multiple neuropeptides exert a direct effect on the same isolated single smooth muscle cell. 242 49


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