Linked Life Data

10763806

Source:http://linkedlifedata.com/resource/pubmed/id/10763806

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-6-23
pubmed:abstractText
Specialized domains, displaying a peculiar lipid and protein composition, are present within the plasma membrane of mammalian cells and play a pivotal role in fundamental membrane-associated events. Among lipids, sphingolipids (in particular glycolipids and sphingomyelin) are characteristically enriched within such domains. Moreover, a series of functionally related proteins is present, suggesting the involvement of these membrane structures in the mechanism of signal transduction and lipid/protein sorting. An increasing body of evidence suggests that domains are dynamic structures, and that their dynamic fluctuations can modulate the activity of domain-associated proteins through changes of glycolipid protein interaction. Even if a large body of experimental investigation has been carried out on eukaryotic cells, only little attention has been paid to the neuron. The purpose of the present review is to summarize the observations implying a functional role of glycolipid-enriched domains in cultured rat cerebellar granule cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0144-8463
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
385-95
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Involvement of glycolipid-enriched domains in the transduction mechanism of neurotrophins in cultured neurons.
pubmed:affiliation
Department of Medical Chemistry and Biochemistry, Medical School, University of Milano-Bicocca, Italy.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't