Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-11-14
pubmed:abstractText
The dependence of CMP-N-acetylneuraminate:GM1 sialyltransferase (SAT IV) activity of rat liver Golgi apparatus on GM1 ganglioside ceramide composition was evaluated. SAT IV activity was assayed on GM1 molecular species carrying homogeneous ceramide moieties containing long chain bases of different length (18 or 20 C atoms) unsaturated or not, linked to 14:0, 16:0, 18:0 or 22:0 fatty acids. The results obtained in the presence of the detergent Triton CF-54, when enzyme and substrate are presumably part of the same supramolecular structure, show that either the long chain base or the fatty acid composition can affect enzyme activity. This feature was not displayed when GM1 was embedded in dipalmitoylphosphatidylcholine vesicles in the absence of detergent. Under the latter conditions, the enzyme was not sensitive to the lipid composition of GM1 but to the ganglioside/phospholipid ratio in the vesicles. These results indicate for the first time that SAT IV is affected by the lipid composition of the substrate and strengthen the hypothesis that glycosyltranferases may contribute to control the cellular glycosphingolipid ceramide pattern.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
383
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
223-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Dependence of rat liver CMP-N-acetylneuraminate:GM1 sialyltransferase (SAT IV) activity on the ceramide composition of GM1 ganglioside.
pubmed:affiliation
Department of Medical Chemistry and Biochemistry, University of Milan, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't