Linked Life Data

1828806

Source:http://linkedlifedata.com/resource/pubmed/id/1828806

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1991-7-24
pubmed:abstractText
The lymphoma plasma membrane glycoprotein, GP85, is a transmembrane glycoprotein that binds directly to ankyrin, a molecule known to link the plasma membrane with the underlying cytoskeleton. In this study, we have demonstrated that palmitic acid is incorporated into GP85 in vivo and that the amount of palmitic acid incorporated is greatly stimulated during lymphoma cap formation. The majority of the incorporated palmitic acid appears to be strongly linked to GP85 since it is not dissociated by strong detergents (e.g. sodium dodecyl sulfate) or by chloroform/methanol extraction, but is labile to alkaline or acid hydrolysis. Furthermore, we have established that deacylation of GP85 (i.e. removal of the palmitic acid moiety from GP85 by 1 M hydroxylamine treatment) significantly reduces the binding affinity between GP85 and ankyrin, and reacylation of GP85 restores the binding affinity. These findings suggest that fatty acid acylation of GP85 by palmitic acid may be required for the stable attachment of the cytoskeleton to the lymphoma plasma membrane.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11761-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Acylation of the lymphoma transmembrane glycoprotein, GP85, may be required for GP85-ankyrin interaction.
pubmed:affiliation
Department of Cell Biology and Anatomy, School of Medicine, University of Miami, Florida 33101.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't