Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

When maintained in organ culture, rabbit gastric mucosal biopsies incorporated [14tc]leucine into tissue protein and secreted labeled protein into culture medium steadily for 24 hr. Incorporation of radioactivity was abolished by cycloheximide. When examined by sodium dodecyl sulfate gel electrophoresis, dextran gel filtration, and ion exchange chromatography, 65 to 90% of macromolecular radioactivity secreted into culture medium migrated coincidentally with enzymatically assayed pepsinogen. Pepsin activity in cultured biopsies did not decrease during 24 hr of organ culture. Nevertheless, pepsin activity increased linearly in culture medium during this period. Acetylcholine markedly stimulated secretion of labeled protein and pepsinogen by cultured biopsies. In the presence of a subthreshold concentration (10(-10) M) of acetylcholine, pentagastrin, secretin, and the octapeptide of cholecystokinin, all stimulated protein secretion. Over-all incorporation of [14C]leucine into protein by cultured biopsies was stimulated by 10(-9) M pentagastrin. These results directly demonstrate: (1) synthesis and secretion of protein and pepsinogen by isolated gastric mucosa, (2) stimulation of gastric secretion of protein by acetylcholine and polypeptide hormones, and (3) stimulation of gastric synthesis of protein by pentagastrin.
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PMID:Synthesis and secretion of protein and pepsinogen by rabbit gastric mucosa in organ culture. 109 89

Valosin, a novel 25-amino acid gastrointestinal peptide with N-terminal valine and C-terminal tyrosine, has recently been isolated from porcine upper gut extracts. Its physiologic role is unknown and it does not belong to one of the structurally related gut peptide families. Assuming that valosin may influence gastrointestinal functions, we investigated the effect of high-performance liquid chromatography-pure valosin on gastric and exocrine pancreatic secretion and on the intestinal myoelectric activity in conscious dogs. Intravenous injection of valosin (0.125-1 microgram/kg) dose-dependently increased gastric acid secretion 80-fold over basal, corresponding to 18% of the maximal pentagastrin-induced effect. Pepsin output increased 10-fold over basal (30% of the pentagastrin-stimulated secretion). Half-maximal stimulation by pentagastrin could be further increased dose-dependently by simultaneous administration of valosin. Pancreatic bicarbonate secretion was stimulated 11-fold over basal at 1.0 microgram/kg, reaching about 6% of the secretin-induced maximal output, whereas protein secretion increased 12-fold over basal, corresponding to about 55% of the cholecystokinin-induced maximal output. In fasted dogs, spontaneously occurring migrating myoelectric complexes were substantially delayed during infusion of valosin at a dose of 0.2 microgram/kg. These experiments indicate that valosin may represent a novel member of the regulatory gastrointestinal peptides.
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PMID:Valosin stimulates gastric and exocrine pancreatic secretion and inhibits fasting small intestinal myoelectric activity in the dog. 310 27

In eight volunteers the effect of pentagastrin (0.15, 1.0 and 6.0 microgram/kg body weight/h), secretin (0.5 and 1.0 clinical units/kg b.w./h), and cholecystokinin (CCK) (0.5 and 1.0 Ivy dog units/kg b.w./h) on the gastric secretion of pepsin was investigated to ascertain whether interaction occurred. A high intraindividual variation was found, and also a significant washout of pepsin in the initial period after stimulation. Pepsin secretion was stimulated after pentagastrin (50% above basal level) and even more after secretin (75%-200% above basal level), whereas no stimulation but a tendency for depression was seen after CCK. With the doses of gastrointestinal hormones used in this investigation, no interaction between secretin and CCK on gastric secretion of pepsin in man was demonstrated.
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PMID:Effect of Pentagastrin, secretin, and cholecystokinin on gastric secretion of pepsin in man. 679 45

Pepsin stored in the stomach mucosa of the Atlantic salmon (Salmo salar L.) increases within two days of the onset of starvation. Trypsin and chymotrypsin in the pyloric caeca/pancreas behave similarly, indicating that when no food is present in the gut, digestive enzymes accumulate in the secretory tissues. As a corollary, trypsin and chymotrypsin activities in the gut contents fell during starvation, indicating that secretion is greatly reduced when food is not present. At the onset of feeding, pepsin is rapidly synthesised in the mucosal tissues and then secreted. Twenty four hours after feeding, the pepsin levels of the mucosa are still low, suggesting that synthesis may be a rapid response to the presence of food in the stomach. Secretion of trypsin and chymotrypsin appears to take place as soon as digesta enters the intestine, between 4 and 14h after feeding, and resynthesis of enzyme precursors appears to be complete again within a further 11h. It is suggested that both synthesis and release may be under the control of cholecystokinin.
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PMID:The effect of feeding on the secretion of pepsin, trypsin and chymotrypsin in the Atlantic salmon,Salmo salar L. 2419 4