Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases
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Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases. / Bootorabi, Fatemeh; Jänis, Janne; Hytönen, Vesa P.; Valjakka, Jarkko; Kuuslahti, Marianne; Vullo, Daniela; Niemelä, Onni; Supuran, Claudiu T.; Parkkila, Seppo.
In: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, Vol. 26, No. 6, 12.2011, p. 862-870.Research output: Contribution to journal › Article › Scientific › peer-review
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TY - JOUR
T1 - Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases
AU - Bootorabi, Fatemeh
AU - Jänis, Janne
AU - Hytönen, Vesa P.
AU - Valjakka, Jarkko
AU - Kuuslahti, Marianne
AU - Vullo, Daniela
AU - Niemelä, Onni
AU - Supuran, Claudiu T.
AU - Parkkila, Seppo
PY - 2011/12
Y1 - 2011/12
N2 - 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.
AB - 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.
KW - Acetaldehyde
KW - Adduct
KW - Alcohol
KW - Mass spectrometry
KW - Modification
UR - http://www.scopus.com/inward/record.url?scp=81355149286&partnerID=8YFLogxK
U2 - 10.3109/14756366.2011.588227
DO - 10.3109/14756366.2011.588227
M3 - Article
VL - 26
SP - 862
EP - 870
JO - JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
JF - JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
SN - 1475-6366
IS - 6
ER -