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dc.contributor.authorFreeman, TCen_US
dc.contributor.authorPlayford, RJen_US
dc.contributor.authorQuinn, Cen_US
dc.contributor.authorBeardshall, Ken_US
dc.contributor.authorPoulter, Len_US
dc.contributor.authorYoung, Jen_US
dc.contributor.authorCalam, Jen_US
dc.date.accessioned2010-04-28T10:59:12Z
dc.date.accessioned2010-05-19T09:39:55Z
dc.date.accessioned2010-05-25T14:23:38Z
dc.date.accessioned2010-07-21T09:17:39Z
dc.date.issued1990-11en_US
dc.identifier.issn0017-5749en_US
dc.identifier.urihttps://qmro.qmul.ac.uk/xmlui/handle/123456789/175
dc.description.abstractWe studied the distribution of pancreatic secretory trypsin inhibitor (PSTI) in the epithelia of the gastrointestinal tract and determined whether PSTI is secreted into gastric juice. PSTI was measured by a specific radioimmunoassay in biopsy specimens taken from the upper (n = 8) and lower (n = 7) gastrointestinal tract of patients with normal endoscopies. PSTI was present in the stomach, small intestine, and colon. Concentrations (micrograms/g protein) were highest in the stomach, and significantly higher in the antrum (1240, 670-1700, median and range) than in the gastric body (370, 350-570) (p less than 0.01). Concentrations were similar in the duodenum (180, 80-210) and colon (160, 130-360). PSTI determined by immunohistochemistry was present in mucus secreting gastric foveolar cells, duodenal Paneth cells, and colonic non mucus cells. PSTI was present in gastric juice. The median (range) concentration of PSTI in basal gastric juice from 13 patients with duodenal ulcers was 9 (3-21) micrograms/l and did not change during stimulation with pentagastrin. The rate of secretion, however, did increase significantly (p less than 0.05) from 1430 (180-2810) ng/h to 4500 (1250-12,770) ng/h during pentagastrin stimulation. PSTI was labile in acid pepsin but stable in the neutral conditions present in the mucus layer. The presence of pancreatic secretory trypsin inhibitor throughout the gut and its secretion into the lumen suggests a hitherto unrecognised mechanism protecting gastrointestinal epithelia against luminal proteases.en_US
dc.format.extent1318 - 1323en_US
dc.languageengen_US
dc.relation.ispartofGuten_US
dc.relation.replaceshttps://qmro.qmul.ac.uk/jspui/handle/123456789/175
dc.relation.replaces123456789/148
dc.relation.replaceshttps://qmro.qmul.ac.uk/jspui/handle/123456789/175
dc.relation.replaces123456789/152
dc.relation.replaceshttps://qmro.qmul.ac.uk/jspui/handle/123456789/175
dc.relation.replaces123456789/156
dc.subjectAdulten_US
dc.subjectBiopsyen_US
dc.subjectChromatography, High Pressure Liquiden_US
dc.subjectColonen_US
dc.subjectDuodenumen_US
dc.subjectEpitheliumen_US
dc.subjectFemaleen_US
dc.subjectGastric Juiceen_US
dc.subjectGastric Mucosaen_US
dc.subjectHumansen_US
dc.subjectImmunohistochemistryen_US
dc.subjectIntestinal Mucosaen_US
dc.subjectMaleen_US
dc.subjectMiddle Ageden_US
dc.subjectPyloric Antrumen_US
dc.subjectTrypsin Inhibitor, Kazal Pancreaticen_US
dc.titlePancreatic secretory trypsin inhibitor in gastrointestinal mucosa and gastric juice.en_US
dc.typeArticle
dc.identifier.doi10.1136/gut.31.11.1318en_US
pubs.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/2253919en_US
pubs.issue11en_US
pubs.notesNot knownen_US
pubs.publication-statusPublisheden_US
pubs.volume31en_US


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