Linked Life Data

904973

Source:http://linkedlifedata.com/resource/pubmed/id/904973

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10 Pt 2
pubmed:dateCreated
1977-11-25
pubmed:abstractText
Ectoglycosyltransferase activities were measured in cultured normal and mucolipidosis II fibroblasts using endogenous glycoproteins and glycolipids and whole cells. Nucleotide pyrophosphatase, known to interfere with glycosyltransferases, was completely inhibited with 6 mM 5' AMP. Since preliminary experiments have shown multiple abnormalities of ectoglycosyltransferases in mucolipidosis II fibroblasts (Di Donato, unpublished results), galactosyl (Gal)-and N-acetylglucosaminyl (GluNac)-transferase were studied in further detail in confluent and nonconfluent cultures of normal and patient fibroblasts. Activities of both transferases on glycoproteins were higher in nonconfluent cultures. A 50% reduced activity of Gal-transferase was measured in confluent mucolipidosis II cultures and of GluNac-transferase in nonconfluent mucolipidosis II cultures towards incorporation of sugar precursors into glycoproteins. Substrate saturation kinetics of both transferases in mucolipidosis II fibroblasts revealed an abnormal Km for Gal incorporation into endogenous glycoproteins. Glycosylation of glycolipids in mucolipidosis fibroblasts was normal.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0031-3998
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1094-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Multiple abnormalities of ectoglycosyltransferases in cultured fibroblasts from patients with mucolipidosis II: Possible indication for abnormal plasma membrane glycoproteins.
pubmed:publicationType
Journal Article, In Vitro