Linked Life Data

3081505

Source:http://linkedlifedata.com/resource/pubmed/id/3081505

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1986-4-4
pubmed:abstractText
The effects of alpha-D-mannopyranosylmethyl-p-nitrophenyltriazene (alpha-ManMNT) on the degradation and biosynthesis of oligosaccharide chains on alpha 1-acid glycoprotein (AGP) were studied. Addition of the triazene to a perfused liver prevented the complete degradation of endocytosed N-acetyl[14C]glucosamine-labeled asialo-AGP and caused the accumulation of Man2GlcNAc1 fragments in the lysosome-enriched fraction of the liver homogenate. This compound also reduced the reincorporation of lysosomally derived [14C]GlcNAc into newly secreted glycoproteins. Cultured hepatocytes treated with the inhibitor synthesized and secreted fully glycosylated AGP. However, the N-linked oligosaccharide chains on AGP secreted by the alpha-ManMNT-treated hepatocytes remained sensitive to digestion with endoglycosidase H, were resistant to neuraminidase, and consisted of Man9-7GlcNAc2 structures as analyzed by high resolution Bio-Gel P-4 chromatography. As measured by their resistance to cleavage by endoglycosidase H, the normal processing of all six carbohydrate chains on AGP to the complex form did not completely resume until nearly 24 h after triazene treatment. Since alpha-ManMNT is likely to irreversibly inactivate alpha-D-mannosidases, the return of normal AGP secretory forms after 24 h probably resulted from synthesis of new processing enzymes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3457-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Effect of alpha-D-mannopyranosylmethyl-p-nitrophenyltriazene on hepatic degradation and processing of the N-linked oligosaccharide chains of alpha 1-acid glycoprotein.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't