Effects of acrolein, a natural occurring aldehyde, on the anticoagulant serpin antithrombin |
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Authors: | I. Martí nez-Martí nez,J.A. Guerrero,A. Miñ ano,L. Velá zquez,V. Vicente |
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Affiliation: | a Centro Regional de Hemodonación, Universidad de Murcia, Ronda de Garay S/N, Murcia 30003, Spain b Department of Clinical Biochemistry, Cardiovascular Research Centre, Aalborg Hospital, Aarhus University Hospital, Denmark |
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Abstract: | We studied the effect of acrolein, an α,β-unsaturated aldehyde that causes adduct-modification of lysine, cysteine, and histidine residues, on antithrombin, a key anticoagulant serpin. Intrinsic fluorescence, functionality (anti-FXa and anti-IIa activity), heparin affinity and conformational features of plasma and purified antithrombin were evaluated. In vivo experiments were carried out in mice. Intrinsic fluorescence showed a two-step conformational change. Acrolein, even at low dose, impaired the anticoagulant function of purified antithrombin by affecting its heparin affinity. However, higher concentrations of acrolein and long incubations are required to cause mild functional effects on plasma antithrombin and mice. |
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Keywords: | Antithrombin Acrolein Aldehyde Heparin affinity Post-translational modification Adducts |
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