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Effects of acrolein, a natural occurring aldehyde, on the anticoagulant serpin antithrombin
Author(s) -
Martínez-Martínez I.,
Ordóñez A.,
Guerrero J.A.,
Pedersen S.,
Miñano A.,
Teruel R.,
Velázquez L.,
Kristensen S.R.,
Vicente V.,
Corral J.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.062
Subject(s) - acrolein , serpin , antithrombin , aldehyde , chemistry , anticoagulant , biochemistry , organic chemistry , medicine , heparin , catalysis , gene
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.