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Abstract
Acetaldehyde can generate modifications in several proteins, such as carbonic anhydrase (CA) II. In this study, we extended in vitro investigations on acetaldehyde adduct formation by focusing on the other human cytosolic CA enzymes I, III, VII, and XIII. High-resolution mass spectrometric analysis indicated that acetaldehyde most efficiently formed covalent adducts with CA II and XIII. The binding of up to 19 acetaldehydes in CA II is probably attributable to the high number of lysine residues (n = 24) located mainly on the surface of the enzyme molecule. CA XIII formed more adducts (up to 25) than it contains lysine residues (n = 16) in its primary structure. Acetaldehyde treatment induced only minor changes in CA catalytic activity in most cases. The present study provides the first evidence that acetaldehyde can bind to several cytosolic CA isozymes. The functional consequences of such modifications will be further investigated in vivo by using animal models.
Acknowledgements
This study was funded by the European Union DeZnIT project, the Academy of Finland, the Sigrid Juselius Foundation, and by Competitive Research Funding of the Tampere University Hospital (9L071, 9M075, 9L112). The authors thank Ritva Romppanen, Marianne Kuuslahti, and Aulikki Lehmus for their skilful technical assistance.
Declaration of interest
The authors report no conflict of interest. The authors alone are responsible for the content and writing of the article.