Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01350 (gastrin)
 9,683 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Twelve gastric-cannulated litter-mate pigs were used to study secretion and proteolytic activity in the stomach of suckling and early-weaned pigs in relation to age and food intake. 2. Results demonstrate that from the first observation at day 8, piglets were able to secrete acid. pH and acid concentration did not change during the first 4 weeks of life. 3. Proteolytic activity was low during the first 2--3 weeks of life and rapidly increased thereafter. 4. Two phenomena differentiated suckling pigs from pigs given dry cow's milk: (1) a low buffering capacity the gastric contents, beginning 1 hr after feeding the dry cow's-milk formula, results in a low total acid concentration in the weaned pigs and (2) the increase in proteolytic activity in relation to the age is much more pronounced in the artificially-reared pigs. 5. These two phenomena are discussed and related to the formation of a hard casein clot in the stomach of the cow's-milk-fed pigs, which has a long retention time and stimulates gastrin release.
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PMID:Gastric secretion in suckling pigs and early-weaned pigs given a dry cow's-mild formula ad lib. 2 7

In tests on dogs with innervated and vagus denervated miniature stomaches and gastric fistula the action of secretin on the gastric secretion provoked by food stimulants-pentagastrin, histamine and parenteral introduction of casein hydrolysate was studied. Experiments showed the secretin to produce an inhibiting action only on the 2nd phase of the gastric secretion after feeding on 100 g of meat, depresses secretion, called forth with pentagastrin, but it does not affect the secretion induced by sham feeding, histamine and intravenous administration of casein hydrolysate. Hence, secretin displays specific properties, by arresting only the action of gastrin on the gastric glands.
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PMID:[Action of secretin on the gastric secretion induced by food stimuli, pentagastrin, histamine and the parenteral administration of casein hydrolysate]. 10 52

Experiments carried out on dogs helped ascertain the casein hydrolysate capable of provoking gastric secretion both with retained gastric innervation and without preservation of the vagal and sympathetic innervation. As this been shown earlier the effect of nitrous substances on the gastric secretion is realized mainly through the agency of the nervous mechanism. The observed secretion in dogs with denervated isolated pouches, however, occuring in response to administration of casein hydrolysate may be explained by mobilization of gastrin under the effect of nervous impulses and its action on the gastric glands. This assumption has been confirmed by tests carried out with the inhibitorglycomacropeptide which inhibits mainly the action of gastrin on the gastric glands.
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PMID:[Effect of a parenterally administered casein hydrolysate on the secretory activity of the stomach with different degrees of gastric gland denervation]. 40 21

The aim of this study was to look for a difference in fasting serum gastrin levels or in serum gastrin response to oral feeding between infants with hypertrophic pyloric stenosis and normal controls. Fasting serum gastrin levels were measured by radioimmunoassay in 10 patients with pyloric stenosis, before pyloromyotomy and 7 and 15 days after it, and in 11 controls. In addition, the serum gastrin responses to a casein hydrolysate meal were studied in both groups (in the patients, 7 days after operation). The fasting serum gastrin levels in the patients did not differ from those in the controls before operation, but they did so after it. The serum gastrin response to feeding in patients after pyloromyotomy was no greater than in controls.
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PMID:Serum gastrin levels in hypertrophic pyloric stenosis of infancy. Response to a gastrin secretion test. 43 7

Amino acids and peptides release gastrin and stimulate gastric acid secretion. However, the relation between gastrin release and acid secretory response is unclear. An isotonic mixed amino acid solution (casein hydrolysate) was continuously infused into the stomach of eight healthy human subjects. Acid secretion, measured by in vivo intragastric titration, increased 12.8 meq/h over the response to intragastric infusion of isotonic saline. Plasma gastrin heptadecapeptide (G-17) concentration, measured by specific radioimmunoassay, increased 13 pmol/liter during intragastric amino acid infusion. To determine whether this rise in plasma G-17 concentration could account for some or all of the acid secretory response, several doses of synthetic human G-17-I were infused intravenously into the same subjects. During i.v. G-17-I infusion, the stomach was continuously infused with isotonic saline. By graphically relating plasma G-17 concentration during i.v. G-17 infusion to concomitant acid secretion, it was determined that a 13-pmol/liter rise in plasma G-17 concentration could increase acid secretion 14.8 meq/h. Therefore, the rise in plasma G-17 concentration during intragastric amino acid infusion could have produced all of the observed acid secretory response. This suggests that gastrin heptadecapeptide is the major physiologic mediator of the human acid secretory response to meals containing mixed amino acids.
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PMID:Role of gastrin heptadecapeptide in the acid secretory response to amino acids in man. 62 Dec 75

The gastric emptying kinetics of peptides derived from milk protein were studied in vivo in preruminant calves by collecting and characterizing the whole effluent leaving the stomach for 12 h after ingestion of crude skim milk. Peptides were isolated by reversed-phase HPLC and identified. Particular attention was paid to biologically active peptides and to peptides that could be precursors of biologically active sequences. A gastrin inhibitor, the caseinomacropeptide, was emptied from the stomach only during the first 0.5 h of digestion and rapidly hydrolysed. Precursors of immunostimulatory peptides from alpha s1- and beta-caseins were emptied throughout digestion in the gastric effluent. A precursor of beta-casomorphins (peptide 58-93 of beta-casein) was emptied from the stomach 3.5 h after the meal when it was taken on an empty stomach. From this precursor, peptides that may be resistant to hydrolysis by intestinal peptidase were obtained after in vitro hydrolysis by pancreatic enzymes. A phosphopeptide (fragment 110-142 of alpha s1-casein) was also found in digesta after a few hours of digestion. When the meal was not taken on an empty stomach, these peptides were emptied in the first digesta at a low concentration. The potential activity of these peptides is discussed. The results support the hypothesis that active sequences could still be present in the gut after the action of pancreatic enzymes.
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PMID:Characterization and kinetics of gastric emptying of peptides derived from milk proteins in the preruminant calf. 145 29

Hepatic and intestinal balances of amino acids, insulin, glucagon and gastrin were studied in 6 non-anaesthetized Large White pigs (mean body weight 64 +/- 4.8 kg) after ingestion of casein or rapeseed proteins. The animals were fitted with permanent catheters in the portal vein, the brachiocephalic artery and the right hepatic vein. In addition, 2 electromagnetic flow probes were implanted, one around the portal vein and the other around the hepatic artery. After a preliminary adaptation to each diet the animals received at 1-wk intervals and according to a double latin square design, 3 test meals of 800 g each, one containing 23.2% of rapeseed concentrate (diet RA 12) and the others 13.9 or 27.8% of hydrochloric casein (diets CA 12 and CA 24). Each observation period lasted 12 h. Amino acids from all diets were very well absorbed. In 12 h, the absorption of total amino acids as a percentage of the ingested quantities was 99% for CA 12, 102% for CA 24 and 104% for RA 12. Hepatic uptake of total amino acids in 12 h expressed as a percentage of the absorbed quantities was 13% for CA 12, 66% for CA 24 and 25% for RA 12. Differences in the hepatic extraction rate of essential amino acids appeared between the 2 levels of casein ingestion and for Arg between the 2 protein sources. Whatever the nature of the ingested protein or the level of casein, the liver showed a net production of Asp and Glu. The production and hepatic balance of insulin were the lowest after ingestion of RA 12. No differences were noted in the same parameters for glucagon and gastrin. Independently of the nutritional situation, the hepatic extraction rate of insulin appeared to be higher than those of glucagon and gastrin. Our results showed that the nature as well as the level of dietary proteins have large effects on the sequence and volume of absorptive phenomena, the hepatic metabolism of nutrients, the production of gastrointestinal hormones and the non-hepatic tissue disposal of absorbed nutrients.
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PMID:Hepatic and portal-drained viscera balances of amino acids, insulin, glucagon and gastrin in the pig after ingestion of casein or rapeseed proteins. 187 48

In preruminant calves total splanchnic production of immunoreactive somatostatin and gastrin did not change when casein was replaced by whey protein in the diet, but gastrin secretion was more rapid for the first 3 postprandial hours. Loss during passage through the liver was equivalent to splanchnic production for somatostatin, but was very low for gastrin.
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PMID:[Gastro-entero-pancreatic production and hepatic uptake of gastrin and somatostatin in the preruminant calf receiving milk proteins or milk serum]. 290 89

Binding of 125I-gastrin to the 270-30,000 g fraction from homogenized rat oxyntic mucosa was studied. 'Specific' binding was calculated by subtracting the binding at excess cold gastrin from the binding with labelled gastrin (250 pM) only. At 30 degrees C specific binding rose rapidly to a short-lived maximum before falling gradually, whereas at 15 degrees C and 0 degree C specific binding rose gradually to a higher plateau level. The reduced binding at 30 degrees C could be caused by degradation of either the tracer or the binding site or by a combination of these two events. Degradation of 125I-gastrin was evaluated by trichloroacetic acid (TCA) precipitation, fast protein liquid chromatography, and binding to a gastrin antibody (immunoreactivity). The effect of incubation on the binding site was evaluated by preincubation of the homogenate fraction before adding gastrin. In separate studies, the proteolytic activity of the homogenate fraction was studied by TCA precipitation of radioactive casein. Different enzyme inhibitors tested were virtually ineffective in preventing gastrin and casein degradation. Only lowering the incubation temperature to 15 degrees C or lower could prevent this degradation. The reduced and transient binding of 125I-gastrin at 30 degrees C most probably reflects tracer degradation. Accordingly, the gastrin binding experiments were performed at 15 degrees C. Only homogenates from the oxyntic area of the stomach bound 125I-gastrin specifically and with a Kd of 0.8 nM (Scatchard analysis). However, micromolar concentrations of unlabelled gastrin were required to inhibit half maximal binding of the tracer. The tracer binding was unaffected by secretin, slightly reduced by a CCK-9 analogue, and more markedly reduced by pentagastrin.
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PMID:Binding and degradation of 125I-gastrin by plasma membranes from homogenized rat gastric mucosa. 301 14

The inhibitory effect of peptides formed in a reaction of limited proteolysis on stimulated gastric acid secretion was studied in rats as well as the changes of gastrin level in the blood serum and antral gastric mucosa. The acid secretion decreased after intraluminal administration of the peptide by 51% in the rat isolated stomach, and gastrin level decreased by 8.3% in the blood serum. The mechanism of action of peptide derived from K-casein was discussed.
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PMID:[Mechanism of inhibition of acid secretion into the stomach by peptides of kappa-casein]. 373 56


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