Linked Life Data

2828285

Source:http://linkedlifedata.com/resource/pubmed/id/2828285

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1988-3-14
pubmed:abstractText
High amount of N-acetyl-D-galactosamine specific lectin binding sites were detected on the canalicular membranes of human parietal cells. Our present model investigations on mice showed that the intracellular distribution of the terminal N-acetyl-D-galactosamine containing glycoprotein highly depends on the actual functional state of the parietal cells. In the normal gastric mucosa 40%-60% of parietal cells react positively after staining with horseradish peroxidase or biotin labelled Dolichos biflorus lectin. Ultrastructurally lectin binding sites occur mainly on the basolateral membrane infoldings in fed animals, while they are present exclusively on the canalicular membranes of fasting mice, suggesting that the alternative appearance of lectin binding sites on the opposite membrane areas of parietal cells is tightly coupled to their main function, to H+ secretion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0301-5564
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
479-82
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Alternative ultrastructural localization of Dolichos biflorus lectin binding sites in proton secreting parietal cells of mice.
pubmed:affiliation
Department of Pathology, University Medical School of Pécs, Hungary.
pubmed:publicationType
Journal Article