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pubmed-article:9392498pubmed:abstractTextA modified platelet response to aggregating stimuli is supposed to play a role in the pathogenesis of diabetic macroangiopathy. We studied the fluidity and microheterogeneity of the external surface of the platelet membrane and the activities of the plasma membrane Na+-K+-ATPase and Ca2+-ATPase in 21 men with type 1 diabetes and in 20 control subjects before and after in vitro thrombin addition. In the resting state, platelets from type 1 diabetic patients showed an increased fluidity and microheterogeneity of the platelet membrane, a higher Ca2+-ATPase activity, and a reduced Na+-K+-ATPase activity in comparison with platelets from healthy subjects. The fatty acid composition was also modified, with increased C 16:1 and decreased C 18:0 content. Control cells incubated with thrombin showed a modification of the membrane parameters opposite to the response observed in type 1 cells after the stimulation. The incubation of control platelets in the resting state with high concentrations of glucose modified the fluidity of the plasma membrane Na+-K+-ATPase and Ca2+-ATPase activities in an opposite way in comparison with the alterations observed in type 1 platelets. This study suggests that in type 1 diabetic patients, the platelet membrane responds to activation with a molecular remodeling different from the response of healthy subjects. The abnormal organization of the membrane might contribute to the altered platelet functions in type 1 diabetic patients, but acute exposure to high glucose levels does not seem able to modify the platelet membrane in the way observed in type 1 diabetes.lld:pubmed
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pubmed-article:9392498pubmed:authorpubmed-author:MazzantiLLlld:pubmed
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pubmed-article:9392498pubmed:pagination2069-74lld:pubmed
pubmed-article:9392498pubmed:dateRevised2010-11-18lld:pubmed
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pubmed-article:9392498pubmed:year1997lld:pubmed
pubmed-article:9392498pubmed:articleTitleAltered platelet membrane dynamic properties in type 1 diabetes.lld:pubmed
pubmed-article:9392498pubmed:affiliationInstitute of Biochemistry, University of Ancona, INRCA, Italy. mazzanti@popcsi.unian.itlld:pubmed
pubmed-article:9392498pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9392498pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed