Linked Life Data

6793421

Source:http://linkedlifedata.com/resource/pubmed/id/6793421

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1981-12-22
pubmed:abstractText
Simultaneous or sequential treatment of rat adipocytes with neuraminidase plus beta-galactosidase decreased insulin binding by 43%. No modification was observed with either enzyme individually. alpha-Mannosidase enhanced insulin binding (38%), whereas beta-N-acetylglucosaminidase and alpha-L-fucosidase were ineffective. Lectins that interact with galactose (Ricinus communis I, RCAI), mannose, Lens culinaris agglutinin (LCA), Concanavalin A (Con A) or N-acetylglucosamine (wheat-germ agglutinin, WGA) decreased insulin binding by 43, 57, 59 and 85% respectively. Lectin inhibition was dose-dependent, saturable and prevented by specific monosaccharides. RCAI, LCA, Con A and WGA decreased the insulin dissociation process by 45, 90, 78 and 84% respectively. Lectins specific for sialic acid, terminal galactose, N-acetylgalactosamine or fucose (Limulus polyphemus, peanut, soybean and Ulex I agglutinins) did not modify either insulin binding or dissociation. These results indicate involvement of penultimate D-galactose, internal N-acetyl-D-glucosamine and D-mannose residues in both processes. They suggest that, in rat adipocytes, a glycosidic moiety participates in the insulin-receptor interaction through N-linked oligosaccharides of the 'complex type'.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
297-310
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Further characterization of the insulin receptor glycosidic moiety in rat adipocytes.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't