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)

26 children were investigated on an average 11.5 years after partial (n = 13) and total (n = 13) colonic resection. Total colectomy was followed by an increased frequency of gastrointestinal symptoms such as recurrent abdominal pain, flatulence, attacks of diarrhoea, frequent and pasty or liquid stools with strange smell. An increased salt or fluid intake was observed in one half of these patients. Their height and bone age was slightly but significantly reduced. Laboratory investigations revealed no significant deficiencies of electrolyts, vitamins or trace elements. However Renin (mean and 2s-range = 5.2; 2.7-6.8 ng/ml.h, normal values (NV) 1.3; 0.5-4.0 ng/ml.h, p less than 0.02), aldosterone (242.1; 168.4-357.8 pg/ml, NV 78.9; 39.4-168.4 pg/ml, *p less than 0.02), conjugated bile acids (11.3; 5.2-20.0 mumol/1, NV 4.2; 1.5-7.0 mumol/1, p less than 0.01) and serum urea concentration (32.5; 20.8-48.7 mg/dl, NV 14.6; 6.0-22.5 mg/dl, p less than 0.01) were significantly elevated. Three postprandial plasma levels of gastrin, VIP and neurotensin were within normal limits. In patients with partial large bowel resection all signs were less pronounced. According to our results a special diet in children years after colectomy seems not to be required.
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PMID:[Late results following partial and total colectomy in infancy]. 328 87

The conformation of several naturally occurring peptide hormones and bioactive oligopeptides in phospholipid solutions was studied by circular dichroism. Phosphatidylcholine induced a partial helix in human gastrin I at neutral pH, but phosphatidylserine did not unless the five consecutive glutamic acid residues in gastrin were protonated. Reduced somatostatin with two lysines and substance P with one arginine and one lysine were partially helical in phosphatidylserine, but not phosphatidylcholine, solution. Both lipids induced a helical conformation in glucagon and its COOH-terminal fragment (19-29) probably because the helical segment is primarily located at the uncharged COOH terminus. Thus, polypeptides with a helix-forming potential can have the helical conformation only when the peptides carry no charge or charges opposite to those on the polar head of the lipid. Renin substrate, which has potentials for the beta form and beta turn, seemed to form a mixture of the two conformations in phosphatidylserine solution. Angiotensin I with a strong probability for the beta form adopted the beta form in phosphatidylserine solution and sleep peptide with no structure-forming potential remained unordered in lipid solutions. The helix usually predominated over the beta form in lipid solutions if the peptide has potentials for both conformations. This could account for the preponderance of helices in bacteriorhodopsin of the purple membrane, which according to its amino acid sequence would have favored the beta form.
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PMID:Lipid-induced ordered conformation of some peptide hormones and bioactive oligopeptides: predominance of helix over beta form. 618 2