Linked Life Data

1898016

Source:http://linkedlifedata.com/resource/pubmed/id/1898016

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-10-24
pubmed:abstractText
Kifunensine is an alkaloid that is produced by the actinomycete Kitasatosporia kifunense and resembles the cyclic oxamide derivative of 1-aminodeoxymannojirimycin in structure. We previously showed that this compound was a potent inhibitor of the purified glycoprotein processing enzyme, mannosidase I, and caused an almost complete inhibition in the formation of complex types of oligosaccharides with the concurrent accumulation of N-linked oligosaccharides having Man9(GlcNAc)2 structures in influenza virus-infected Madin Darby canine kidney cells. Kifunensine, at concentrations of 1 microgram/ml or higher in the culture medium, caused an almost complete inhibition in the formation of complex types of oligosaccharides by human skin fibroblasts or aortic endothelial cells, with the resulting accumulation of Man9(GlcNAc)2 oligosaccharides on the cell surface N-linked glycoproteins, and more specifically on the scavenger-LDL receptor. When endothelial cells were grown in the presence of 1 microgram/ml of kifunensine, there was a 75% inhibition in the ability of these cells to degrade 125I-labeled acetyl-LDL, but this inhibitor appeared to have little or no effect on the ability of either endothelial cells or fibroblasts to degrade 125I-labeled LDL, even at kifunensine concentrations of 10 micrograms/ml. Kifunensine also decreased the binding of the labeled acetyl-LDL by the scavenger receptor of the endothelial cells, but the amount of this inhibition relative to controls was significantly less than that of the degradation, suggesting that kifunensine affects two different steps of acetyl-LDL metabolism in these cells. Endothelial cells grown in the presence of 10 micrograms/ml of kifunensine had only half the activity of the lysosomal enzymes, beta-hexosaminidase, and proteases, as did control cells, although kifunensine did not affect [3H]leucine incorporation into protein. Thus, kifunensine apparently affects the activity of (some) lysosomal enzymes in an as yet undefined manner.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
288
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-84
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Kifunensine inhibits glycoprotein processing and the function of the modified LDL receptor in endothelial cells.
pubmed:affiliation
Department of Biochemistry and Pathology, University of Texas Health Science Center, San Antonio 78284.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.