Format

Send to

Choose Destination
J Enzyme Inhib Med Chem. 2011 Dec;26(6):862-70. doi: 10.3109/14756366.2011.588227. Epub 2011 Jun 16.

Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases.

Author information

1
Institute of Biomedical Technology, University of Tampere and Tampere University Hospital, Tampere, Finland.

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.

PMID:
21679053
DOI:
10.3109/14756366.2011.588227
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Taylor & Francis
Loading ...
Support Center