Linked Life Data

12890998

Source:http://linkedlifedata.com/resource/pubmed/id/12890998

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-7-31
pubmed:abstractText
Previously we have demonstrated inhibitory effects of the plant lectin wheat germ agglutinin (WGA) on (125)I-CCK-8 binding to pancreatic AR42J cells as well as on CCK-8-stimulated Ca(2+) release and alpha-amylase secretion of rat pancreatic acini or acinar cells. Therefore, it is entirely conceivable that alpha-amylase having several lectin-like carbohydrate recognition domains can modulate the CCK-8 stimulated lipase secretion. Human alpha-amylase, purified from pancreatic juice by affinity chromatography to homogeneity, and commercial porcine pancreatic alpha-amylase inhibit CCK-8-stimulated lipase secretion of rat pancreatic acini in a concentration-dependent manner. Acarbose, a specific inhibitor of alpha-amylase, was without effect on CCK-8-induced cellular lipase secretion. The data presented here provide evidence for a regulatory function of alpha-amylase in CCK-8-stimulated pancreatic secretion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1424-3903
pubmed:author
pubmed:copyrightInfo
Copyright 2003 S. Karger AG, Basel and IAP
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
342-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Inhibitory effects of human and porcine alpha-amylase on CCK-8-stimulated lipase secretion of isolated rat pancreatic acini.
pubmed:affiliation
Department of Pathology, Faculty of Medicine, University of Rostock, Germany. ludwig.jonas@med.uni-rostock.de
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't