Coagulation protein function. IV. Effect of acetaldehyde upon factor X and factor Xa, the proteins at the gateway to the common coagulation pathway

Alcohol
Arthur S BrecherM H Basista

Abstract

Acetaldehyde (AcH) (447 mM) exerts an inhibition on Factor Xa, as followed by a clotting assay, but does not inhibit the hydrolysis of the synthetic fluorogenic substrate, N-tBOC-Ile-Glu-Gly-Arg-7-amido-4-methylcoumarin. These data suggest that AcH, although not reacting at the catalytic site of Factor Xa nor at the binding site for the synthetic substrate, does interact with the functional groups on the enzyme that bind to its natural substrate, prothrombin. As a consequence of such interaction, the charge and conformation of Factor Xa is altered, thereby limiting effective activation of prothrombin. Additionally, alkylation of factor Xa may also affect its capacity to associate with Factor Va for the activation of prothrombin. AcH also reacts with Factor X, prolonging clotting times when the zymogen is activated with Russell's viper venom (RVV). It also reduces the rate of hydrolysis of the fluorogenic substrate after activation of the alkylated zymogen by RVV. These data lead to the considerations that AcH-modified Factor X is no longer as effectively activated by RVV due to an alteration of its charge/conformation. Additional possibilities include a likely alkylation of the Factor Xa moiety of Factor X by AcH such that the ...Continue Reading

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Citations

Oct 26, 2010·Analytical and Bioanalytical Chemistry·Vanessa Castro-LópezAnthony J Killard
Jul 20, 2007·International Journal of Legal Medicine·T FracassoH Pfeiffer
Apr 18, 2002·Alcohol·Arthur S Brecher, Mohammed T Adamu
Nov 15, 2002·Canadian Journal of Physiology and Pharmacology·Arthur S Brecher, Eric L Hommema
Apr 17, 2007·Digestive Diseases and Sciences·Elizabeth A Suchocki, Arthur S Brecher
May 18, 2005·Canadian Journal of Physiology and Pharmacology·Arthur S Brecher, Mohammed T Adamu
Feb 10, 2018·Trends in Molecular Medicine·Helen M HeymannEric R Gross

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