Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2004-2-3
pubmed:abstractText
When human platelets are chilled below 20 degrees C, they undergo cold-induced activation. We have previously shown that cold activation correlates with the main phospholipid phase transition (10-20 degrees C) and induces the formation of large raft aggregates. In addition, we found that the glycoprotein CD36 is selectively enriched within detergent-resistant membranes (DRMs) of cold-activated platelets and is extremely sensitive to treatment with methyl-beta-cyclodextrin (MbetaCD). Here, we further studied the partitioning of downstream signaling molecules within the DRMs. We found that the phospholipase Cgamma2 (PLCgamma2) and the protein tyrosine kinase Syk do not partition exclusively within the DRMs, but their distribution is perturbed by cholesterol extraction. In addition, PLCgamma2 activity increases in cold-activated cells compared to resting platelets and is entirely inhibited after treatment with MbetaCD. The Src-family protein tyrosine kinases Src and Lyn preferentially partition within the DRMs and are profoundly affected by removal of cholesterol. These kinases are non-redundant in cold-activation. CD36, active Lyn, along with inactive Src and PLCgamma2 co-localize in small raft complexes in resting platelets. Cold-activation induces raft aggregation, resulting in changes in the activity of these proteins. These data suggest a crucial role of raft aggregation in the early events of cold-induced platelet activation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
1660
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-15
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Important role of raft aggregation in the signaling events of cold-induced platelet activation.
pubmed:affiliation
Center for Biostabilization, University of California, Davis, CA 95616, USA. kgousset@jhu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.