Unconjugated bilirubin inhibits C1 esterase activity.

Autor: Arriaga SM; Area Bioquímica Clínica y Fisiopatología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina. sarriaga@fbioyf.unr.edu.ar, Basiglio CL, Mottino AD, Almará AM
Jazyk: angličtina
Zdroj: Clinical biochemistry [Clin Biochem] 2009 Jun; Vol. 42 (9), pp. 919-21. Date of Electronic Publication: 2009 Jan 03.
DOI: 10.1016/j.clinbiochem.2008.12.015
Abstrakt: Objective: To evaluate if unconjugated bilirubin (UB) inhibits C1 esterase activity.
Design and Methods: Esterase activity was evaluated by C1-mediated hydrolysis of N-acetyl-L-tyrosine ethyl ester, and binding of UB to C1r and C1s was assessed by dot-blot analysis.
Results: UB inhibited C1 enzymatic activity. C1r, C1s and human serum albumin bound [(14)C]-UB to a similar extent.
Conclusions: UB inhibits C1 esterase activity, apparently due to a direct pigment-protein interaction. This could explain the inhibitory action of UB on complement activation.
Databáze: MEDLINE
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