Linked Life Data

2765666

Source:http://linkedlifedata.com/resource/pubmed/id/2765666

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1989-9-25
pubmed:abstractText
Covalent attachment of fatty acid to proteins plays an important role in association of certain proteins with hydrophobic membrane structures. In platelets, the structure of many membrane glycoproteins (GPs) has been examined in detail, but the question of fatty acid acylation of platelet proteins has not been addressed. In this study, we wished to determine (a) whether platelet proteins could be fatty acid acylated; and, if so, (b) whether these modified proteins were present in isolated platelet membranes and cytoskeletal fractions; and (c) if the pattern of fatty acid acylated proteins changed on stimulation of the platelets with the agonist thrombin. We observed that in platelets allowed to incorporate 3H-palmitate, a small percentage (1.37%) of radioactivity incorporated into the cells became covalently bound to protein. Selective cleavage of thioester, thioester plus O-ester, and amide-linked 3H-fatty acids from proteins, and their subsequent analysis by high-performance liquid chromatography (HPLC) indicated that the greatest part of 3H-fatty acid covalently bound to protein was thioester-linked 3H-palmitate. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fluorography, at least ten major radiolabeled proteins were detected. Activation of platelets by thrombin greatly increased the quantity of 3H-palmitoylated proteins associated with the cytoskeleton. Nearly all radiolabeled proteins were recovered in the membrane fraction, indicating that these proteins are either integral or peripheral membrane proteins or proteins tightly associated to membrane constituents. Components of the GPIIb-IIIa complex were not palmitoylated. Thus, platelet proteins are significantly modified posttranslationally by 3H-palmitate, and incorporation of palmitoylated proteins into the cytoskeleton is a prominent component of the platelet response to thrombin stimulation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1339-47
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2765666-Acylation, pubmed-meshheading:2765666-Chromatography, High Pressure Liquid, pubmed-meshheading:2765666-Cytoskeletal Proteins, pubmed-meshheading:2765666-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:2765666-Humans, pubmed-meshheading:2765666-Hydrochloric Acid, pubmed-meshheading:2765666-Hydrolysis, pubmed-meshheading:2765666-Hydroxylamine, pubmed-meshheading:2765666-Hydroxylamines, pubmed-meshheading:2765666-Mercaptoethanol, pubmed-meshheading:2765666-Methanol, pubmed-meshheading:2765666-Molecular Weight, pubmed-meshheading:2765666-Palmitic Acid, pubmed-meshheading:2765666-Palmitic Acids, pubmed-meshheading:2765666-Platelet Aggregation, pubmed-meshheading:2765666-Platelet Membrane Glycoproteins, pubmed-meshheading:2765666-Subcellular Fractions, pubmed-meshheading:2765666-Tritium
pubmed:year
1989
pubmed:articleTitle
Covalent modification of platelet proteins by palmitate.
pubmed:affiliation
Department of Pathology and Laboratory Medicine, University of Pennsylvania, School of Medicine, Philadelphia 19104.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.