Linked Life Data

8155721

Source:http://linkedlifedata.com/resource/pubmed/id/8155721

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-5-19
pubmed:abstractText
The role of processing of the oligosaccharide chains in the affinity of lipoprotein lipase (LPL) for heparin was examined in 3T3-L1 adipocytes. 43% of 35S-labeled LPL subunits in tunicamycin (TUN)-treated cells did not bind to a heparin-Sepharose column and 46% was eluted with 0.6 M NaCl. 11% of LPL subunits in castanospermine (CSTP)-treated cells did not bind to the column and 38% was eluted with 0.6 M NaCl. In contrast, as in untreated cells, LPL subunits in 1-deoxymannojirimycin (dMM)-treated and swainsonine (SW)-treated cells almost all bound to the column and over 93% of the subunits bound were eluted with 1.5 M NaCl. Thus, core glycosylation and subsequent removal of the distal glucose residue from oligosaccharide chains of LPL in the endoplasmic reticulum (ER) is required for acquisition of a higher affinity for heparin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
1212
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Role of processing of the oligosaccharide chains in the affinity of lipoprotein lipase for heparin.
pubmed:affiliation
Department of Medical Biochemistry, School of Medicine, Ehime University, Japan.
pubmed:publicationType
Journal Article