Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P61278 (somatostatin)
 22,083 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The new long-acting somatostatin analogue octreotide (SMS 201-995) was investigated for its influence on secretagogue-stimulated human exocrine pancreatic secretion. Eighteen healthy volunteers participated in the study. During duodenal intubation with a background stimulation of either secretin 1 U.kg/h or secretin 1 U.kg/h + ceruletide, 120 ng.kg/h, octreotide was infused at doses of 5, 20 and 80 micrograms/h in a placebo-controlled randomized double-blind crossover trial. Duodenal juice samples were collected in 10-min intervals, and amylase, trypsin, chymotrypsin, and bicarbonate were measured in the individual fractions. During secretin stimulation, amylase was inhibited between 41 and 59%, trypsin between 28 and 72%, chymotrypsin between 55 and 70%, and bicarbonate between 0 and 31% with 5, 20 and 80 micrograms/h octreotide. During secretin and ceruletide stimulation, amylase was significantly inhibited by 84%, 78%, 81%, trypsin by 76%, 55%, 52%, chymotrypsin by 77%, 55%, 60%, and bicarbonate by 25%, 11%, 19% with 5, 20, and 80 micrograms/h octreotide, respectively (all decreases P less than 0.05). The long-acting somatostatin analogue octreotide was confirmed to be a potent inhibitor of stimulated human exocrine pancreatic secretion. The near maximal inhibitory potency of octreotide was achieved at a dose of only 5 micrograms/h. This finding may be of value in the planning of therapeutic studies with octreotide.
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PMID:Inhibition of human exocrine pancreatic secretion by the long-acting somatostatin analogue octreotide (SMS 201-995). 137 38

An endopeptidase was isolated from Xenopus laevis skin secretions. This enzyme, which has an apparent molecular mass of 100 kDa, performs a selective cleavage at the Xaa-Phe, Xaa-Leu, or Xaa-Ile bond (Xaa = Ser, Phe, Tyr, His, or Gly) of a number of peptide hormones, including atrial natriuretic factor, substance P, angiotensin II, bradykinin, somatostatin, neuromedins B and C, and litorin. The peptidase exhibited optimal activity at pH 7.5 and a Km in the micromolar range. No cleavage was produced in vasopressin, ocytocin, minigastrin I, and [Leu5]enkephalin, which include in their sequence an Xaa-Phe, Xaa-Leu, or Xaa-Ile motif. The endopeptidase activity was inhibited by divalent cation chelators and by phosphoramidon only at high concentrations (IC50 = 50 microM), whereas it was insensitive to classical inhibitors of chymotrypsin, angiotensin convertase, and serine and cysteine peptidases, as well as carboxypeptidases. It is hypothesized that this enzyme, which is distinct from neutral endopeptidase (EC 3.4.24.11), constitutes the prototype of a family of related metalloendopeptidases that inactivate peptide substrates by cleavage at the Xaa-Phe, Xaa-Leu, or Xaa-Ile bond.
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PMID:A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion. 172 23

Somatostatin (SS) is found in the endocrine pancreas and has been reported in the pure pancreatic juice (PPJ) of different species. Characterization by gel filtration of immunoreactive SS (irSS) in the rat PPJ (rPPJ) results in a single peak corresponding to 23kDa molecular weight. Incubation of the 23kDa fraction with labeled or synthetic SS results in time dependent degradation of both peptides. This degradation is inhibitable by PMSF, calcium and by heat, whereas specific inhibitors of trypsin and chymotrypsin are without effect. These data suggest that irSS previously measured in rPPJ samples by RIA without confirmation of radioactive tracer stability may lead to false positive results. Indeed, our study indicates the presence of a 23kDa enzyme in the rPPJ degrading radiolabeled somatostatin during the RIA procedure. This putative new enzyme found into the rPPJ may thus be partially responsible for the apparent irSS presence.
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PMID:Evidence of a new serine protease in the rat pure pancreatic juice that degrades somatostatin. 197 13

A bland procedure, conducted in ice, is described for the extraction with HCl of smooth-muscle-contracting substances from plexus-containing ileal longitudinal muscle (l.m.) sheets obtained mainly from rabbits and some guinea-pigs. The spasmogenic activity in rabbit extracts was distinguished from acetylcholine, histamine and 5-hydroxytryptamine by antagonists; and from prostaglandins, by its insolubility in ether at acid pH and by pretreatment of the animals with indomethacin. The fact that it contracts the separated l.m. of the guinea-pig ileum, whether plexus-containing or plexus-free, and in atropine distinguishes it also from methionine-enkephalin, somatostatin, 13-norleucine motilin, bombesin, and cholecystokinin octapeptide (CCK8). This activity was partially purified, first by several partitions with ether at pH 1.4-2.2 and then by treatment at pH 4.5-5 with lead acetate. The virtual absence of ATP was confirmed by the firefly bioluminescence technique. The guinea-pig-ileum-contracting component in the partially purified extracts was destroyed by pepsin, chymotrypsin and DPCC-treated trypsin, indicating its peptide nature and distinguishing it from oxytocin, vasopressin, bradykinin, etc. In parallel assays the partially purified rabbit extracts were considerably more active than Substance P on jird or rat ascending colons than on the guinea-pig l.m., suggesting the presence of a second spasmogenic component in the extracts. In guinea-pig extracts the partially purified activity was 8-16 times greater when plexus-containing than when plexus-free, pointing to Auerbach's plexus as the source of the activity.
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PMID:Extraction and partial purification of spasmogenic substances in Auerbach's plexus. 242 21

The current study examines the effects of somatocrinin (GRF) and somatostatin antiserum (ASS) alone and in combination on pancreatic growth. Twenty-four-day-old rats were injected daily s.c. at 10:00 and 16:30 h for 14 days with either saline or GRF (4 and 20 micrograms X kg-1). ASS was given i.p. every other day. Pancreatic weights and DNA, RNA, protein, amylase, and chymotrypsin total contents and concentrations were evaluated at the end of treatment. GRF alone was associated with significant decreases in pancreatic weight and contents of protein, amylase, and chymotrypsin but with significant increases in total DNA content indicating pancreatic atrophy and hyperplasia. ASS alone has a slight effect on DNA content but potentiates GRF given at the dose of 4 micrograms X kg-1. Even though ASS reduced protein and enzyme contents, it prevented the large decreases observed with increasing doses of GRF. These data present for the first time effects of GRF and ASS on pancreatic growth and describe a strong interaction between the two products. It is yet too early to determine how these two substances work on the pancreatic acinar cells, but hypotheses on their possible mode of action are proposed.
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PMID:Effect of somatocrinin with or without a somatostatin antiserum on pancreatic growth. 243 58

Mice were injected 3 times a day for 12 days with 8 micrograms/kg of somatostatin 14 which caused a hypoplasia of parietal and goblet cells, a hypotrophy and hypofunctionality of pancreatic acinar cells with a decrease in lipase and chymotrypsin activities, a decrease in the secretory fuction of the Brunner gland and in the number of dark granules of G cells. Neither villous and microvillous areas nor brush border hydrolase activities were affected. The number of peptic cells and Paneth cells increase as the level of pepsin and lysozyme. Mice were injected 4 times per hour with 2 micrograms/kg of somatostatin. 2 h after the first injection of somatostatin and 90 min after a single injection of tritiated thymidine, fundic, antral, jejunal and ileal labelling indexes strongly decrease (maximal effect in ileum). The inhibitory effect of somatostatin on the digestive epithelial cell proliferation compared to its long-term action only directed on specific cell types evokes probable compensatory mechanisms induced to maintain the equilibrium of the digestive epithelia.
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PMID:Long-term effect of somatostatin 14 on mouse stomach, antrum, intestine and exocrine pancreas. 285 47

The aim of this study was to determine the effect of wheat bran consumption on exocrine pancreas secretion in pigs. Sixteen Large-White pigs were divided into two groups. The first group (control) was fed a diet without wheat bran and the second one (experimental) a diet containing 40% wheat bran. After one week the animals were fitted with two permanent fistulae (in the pancreatic duct and the duodenum) and/or with a catheter in a carotid artery. After an 8-day recovery period, pancreatic secretion (volume, protein content and output, chymotrypsin, trypsin, lipase and amylase activities) and plasma levels of some gastro-intestinal peptides [secretin, cholecystokinin (CCK), vasoactive intestinal peptide (VIP), somatostatin and pancreatic polypeptide (PP)] were measured over an experimental period of 5 days. The results show that wheat bran intake induced an increase in the volume (+ 115%) and protein output (+ 36%) of the pancreatic juice secreted in a 24-hour period, whereas protein concentration decreased. All enzyme activities were enhanced by wheat bran. The plasma levels of secretin, VIP, somatostatin and PP were higher in the experimental than in the control group. On the contrary, plasma CCK levels were not affected by wheat bran consumption.
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PMID:Effects of wheat bran on exocrine pancreas secretion in the pig. 289 Nov 62

We have reported that the secretion of at least 17 distinct peptides [including rat (rGH)] GH by cultured rat pituitary cells was stimulated by GH-releasing hormone and inhibited by somatostatin, when analyzed by two-dimensional polyacrylamide gel electrophoresis. Three of these peptides (no. 23, 24, and 25) were not rGH immunoreactive. In order to determine whether these three peptides are fragments, degradation products or posttranscriptionally modified forms of rGH, rGH and peptide no. 23 were characterized structurally. From partial peptide maps of rGH and peptide no. 23 by V8 protease or chymotrypsin, it appeared that these peptides were not related to each other. By N-terminal microsequencing of two-dimensional polyacrylamide gel electrophoresis purified peptide, we have obtained the sequence of 24 N-terminal amino acid residues of peptide no. 23. This sequence has no significant homology with rGH or any other reported protein sequence. Antiserum was generated against a synthetic oligopeptide corresponding to amino acid residues 3-24 of peptide no. 23. The antiserum cross-reacted with peptides no. 23, 24, and 25 upon Western blot analysis. These results indicate that peptide no. 23 has a novel structure unrelated to other pituitary hormones. Since its secretion is influenced by GH-releasing hormone and somatostatin, peptide no. 23 may represent a previously unrecognized structurally unique growth factor.
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PMID:Growth hormone-releasing hormone stimulates and somatostatin inhibits the release of a novel protein by cultured rat pituitary cells. 290 40

Three cases of clinically benign pancreatic papillary cystic tumors in young female patients were studied by immunohistochemistry and electron microscopy in order to define the cellular nature of this type of neoplasm. Two of the tumors showed focal cytokeratin- and desmoplakin-positivity as evidence of focal epithelial differentiation, while the tumor cells were in all cases positive for vimentin--the intermediate filament protein typical of (but not specific for) mesenchymal cells. Electron microscopy showed some cell-cell junctions, but there was no evidence of acinar or islet cell differentiation. The tumors were at least focally positive for neuron-specific enolase, and small clusters of polypeptide hormone immunoreactive cells were present in all cases (glucagon 3/3, somatostatin 2/3, insulin 2/3). However, the tumors were negative for synaptophysin and neurofilament proteins, unlike most islet cell tumors. Trypsin and chymotrypsin immunoreactivity was found in all tumors, but because many nonpancreatic carcinomas were also positive, we doubt whether these two enzyme proteins can act as specific markers for pancreatic acinar cell differentiation. Two of the tumors that were studied immunohistochemically for the presence of nuclear estrogen receptors, were negative. Therefore no proof of the suggested hormone dependence of this tumor could be obtained. We conclude that papillary cystic tumor is a neoplasm of primitive pancreatic epithelial cells, that may exhibit focal endocrine cell differentiation.
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PMID:Papillary cystic tumor of the pancreas. An analysis of cellular differentiation by electron microscopy and immunohistochemistry. 367 83

The aim of the present study was to investigate the short-term (8-day) effects of feeding a raw soybean diet on exocrine pancreatic secretion and the plasma levels of gastrointestinal hormones in pigs. After adaptation to a heated soybean diet, 6 pigs (36.5 +/- 0.8 kg) were fitted with permanent fistulae of the pancreatic duct, the duodenum and a carotid artery. After post-surgical recovery of 8 days, the animals were submitted to two experimental periods, a 4-day period during which they were fed the heated soybean diet and an 8-day period during which they received the raw soybean diet. Exocrine pancreatic secretion and plasma levels of secretin, cholecystokinin, VIP, PP, somatostatin and gastrin were monitored each day of the two experimental periods. On the first day of raw soybean ingestion and till its end, the daily volume of pancreatic juice was higher than the mean volume measured during heated soybean ingestion. On the contrary, daily total protein output was unchanged. Specific activities of chymotrypsin, amylase and lipase were not modified by the raw soybean diet whereas, from the third day of the experimental period, that of trypsin was higher than the corresponding mean value determined during the first experimental period. Plasma levels of secretin and VIP were higher throughout raw soybean ingestion than the corresponding mean levels determined during the first experimental period. The plasma level of cholecystokinin increased only slightly and in the first days of the second experimental period only. The other gastrointestinal hormones studied were slightly (gastrin) or not (somatostatin, PP) affected by raw soybean feeding. It is suggested that feedback control of exocrine pancreatic secretion in pigs was the mechanism involved in the increase of pancreatic juice observed when raw soybean was fed. This volume increase would result from secretin release into the blood.
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PMID:Short-term (8-day) effects of a raw soybean diet on exocrine pancreatic secretion and plasma gastrointestinal hormone levels in the pig. 371 92


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