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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 journalArticleScientificpeer-review

Harvard

Bootorabi, F, Jänis, J, Hytönen, VP, Valjakka, J, Kuuslahti, M, Vullo, D, Niemelä, O, Supuran, CT & Parkkila, S 2011, 'Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases', JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol. 26, no. 6, pp. 862-870. https://doi.org/10.3109/14756366.2011.588227

APA

Bootorabi, F., Jänis, J., Hytönen, V. P., Valjakka, J., Kuuslahti, M., Vullo, D., ... Parkkila, S. (2011). Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases. JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 26(6), 862-870. https://doi.org/10.3109/14756366.2011.588227

Vancouver

Bootorabi F, Jänis J, Hytönen VP, Valjakka J, Kuuslahti M, Vullo D et al. Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases. JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY. 2011 Dec;26(6):862-870. https://doi.org/10.3109/14756366.2011.588227

Author

Bootorabi, Fatemeh ; Jänis, Janne ; Hytönen, Vesa P. ; Valjakka, Jarkko ; Kuuslahti, Marianne ; Vullo, Daniela ; Niemelä, Onni ; Supuran, Claudiu T. ; Parkkila, Seppo. / Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases. In: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY. 2011 ; Vol. 26, No. 6. pp. 862-870.

Bibtex - Download

@article{ed0dddde2ba947bbb054aef1e3101f12,
title = "Acetaldehyde-derived modifications on cytosolic human carbonic anhydrases",
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.",
keywords = "Acetaldehyde, Adduct, Alcohol, Mass spectrometry, Modification",
author = "Fatemeh Bootorabi and Janne J{\"a}nis and Hyt{\"o}nen, {Vesa P.} and Jarkko Valjakka and Marianne Kuuslahti and Daniela Vullo and Onni Niemel{\"a} and Supuran, {Claudiu T.} and Seppo Parkkila",
year = "2011",
month = "12",
doi = "10.3109/14756366.2011.588227",
language = "English",
volume = "26",
pages = "862--870",
journal = "JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY",
issn = "1475-6366",
publisher = "Informa Healthcare",
number = "6",

}

RIS (suitable for import to EndNote) - Download

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 -