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AGEs and methylglyoxal induce apoptosis and expression of Mac-1 on neutrophils resulting in platelet-neutrophil aggregation.

Abstract：

INTRODUCTION:Diabetes mellitus is characterised by hyperglycaemia that plays an important role in the pathogenesis of diabetic complications including accumulation of methylglyoxal (MG), a highly reactive alpha-dicarbonyl metabolite of glucose degradation pathways and increased generation of advanced glycation end products (AGEs). The aim of this study was to investigate the impact of AGE-BSA, the model substance for AGEs, and MG on cellular haemostasis. MATERIALS AND METHODS:Isolated peripheral blood mononuclear cells (PBMCs) or whole blood was incubated with AGE-BSA and MG. Markers of cellular haemostasis were monitored by flow cytometry. RESULTS:Exposure of PBMCs to AGE-BSA and MG resulted in a dose- and time-dependent increase of TF-expression by monocytes. AGE-BSA and MG induced enhanced platelet-neutrophil aggregation. Examination of platelet activation showed that AGE-BSA induces no direct effect on the expression of P-selectin. However, stimulation with MG resulted in a dose-dependent expression of P-selectin by platelets. Stimulation with AGE-BSA or MG markedly increased dose-dependent expression of Apo2.7 on the neutrophil mitochondria. In addition the analysis demonstrated for the first time that both AGE-BSA and MG induce a dose-dependent expression of the adhesion molecule Mac-1 on the surface of neutrophils. CONCLUSIONS:AGE-BSA as well as MG induced apoptosis of neutrophils and enhanced expression of the adhesion molecule Mac-1 resulting in increased formation of platelet-neutrophil aggregates. These findings may contribute to better understand the mechanism of diabetic thrombosis and the associated high cardiovascular risk of diabetic patients.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Gawlowski T,Stratmann B,Stirban AO,Negrean M,Tschoepe D

doi

10.1016/j.thromres.2007.03.002

subject

Has Abstract

pub_date

2007-01-01 00:00:00

pages

117-26

issue

1

eissn

0049-3848

issn

1879-2472

pii

S0049-3848(07)00083-7

journal_volume

121

pub_type

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