Reaction of acetaldehyde with human platelets.
Details
Serval ID
serval:BIB_751F7D78DA1D
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Reaction of acetaldehyde with human platelets.
Journal
Thrombosis and haemostasis
ISSN
0340-6245 (Print)
ISSN-L
0340-6245
Publication state
Published
Issued date
23/01/1992
Peer-reviewed
Oui
Volume
67
Number
1
Pages
126-130
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Publication Status: ppublish
Abstract
Platelet function defects observed in chronic alcoholics are not wholly explained by the inhibitory action of ethanol on platelet aggregation; they are not completely reproduced either in vivo by short-term ethanol perfusion into volunteers or in vitro by the addition of ethanol to platelet-rich plasma. As acetaldehyde (AcH) binds to many proteins and impairs cellular activities, we investigated the effect of this early degradation product of ethanol on platelets. AcH formed adducts with human platelets at neutral pH at 37 degrees C which were stable to extensive washing, trichloracetic acid hydrolysis and heating at 100 degrees C, and were not reduced by sodium borohydride. The amount of platelet adducts formed was a function of the incubation time and of the concentration of AcH in the reaction medium. At low AcH concentrations (less than 0.2 mM), platelet bound AcH was directly proportional to the concentration of AcH in the reaction medium. At higher concentrations (greater than or equal to 0.2 mM), AcH uptake by platelets tended to reach a plateau. The amount of adducts was also proportional to the number of exposures of platelets to pulses of 20 microM AcH. AcH adducts formation severely impaired platelet aggregation and shape change induced by ADP, collagen and thrombin. A positive correlation was established between platelet-bound AcH and inhibition of aggregation. SDS-PAGE analysis of AcH adducts at neutral pH demonstrated the binding of [14C]acetaldehyde to many platelet proteins. AcH adduct formation with membrane glycoproteins, cytoskeleton and enzymes might interfere with several steps of platelet activation and impair platelet aggregation.(ABSTRACT TRUNCATED AT 250 WORDS)
Keywords
Acetaldehyde/blood, Acetaldehyde/pharmacology, Alcoholism/blood, Binding Sites, Blood Platelets/drug effects, Blood Platelets/metabolism, Ethanol/blood, Humans, In Vitro Techniques, Platelet Aggregation/drug effects, Platelet Aggregation Inhibitors/pharmacology, Platelet Membrane Glycoproteins/metabolism
Pubmed
Web of science
Create date
25/01/2008 16:31
Last modification date
25/05/2024 7:12