Human Aldehyde Dehydrogenase 3A1 (ALDH3A1) Exhibits Chaperone-Like Function

Voulgaridou, Georgia-Persephoni, Tsochantaridis, Ilias, Mantso, Theodora, Franco, Rodrigo, Panagiotidis, Mihalis and Pappa, Aglaia (2017) Human Aldehyde Dehydrogenase 3A1 (ALDH3A1) Exhibits Chaperone-Like Function. The International Journal of Biochemistry & Cell Biology, 89. pp. 16-24. ISSN 1357-2725

[img] Text (Article)
1-s2.0-S1357272517301073-main.pdf - Accepted Version
Restricted to Repository staff only until 16 May 2018.

Download (1MB)
Official URL: https://doi.org/10.1016/j.biocel.2017.05.017

Abstract

Aldehyde dehydrogenase 3A1 (ALDH3A1) is a metabolic enzyme that catalyzes the oxidation of various aldehydes. Certain types of epithelial tissues in mammals, especially those continually exposed to environmental stress (e.g., corneal epithelium), express ALDH3A1 at high levels and its abundance in such tissues is perceived to help to maintain cellular homeostasis under conditions of oxidative stress. Metabolic as well as non-metabolic roles for ALDH3A1 have been associated with its mediated resistance to cellular oxidative stress. In this study, we provide evidence that ALDH3A1 exhibits molecular chaperone-like activity further supporting its multifunctional role. Specifically, we expressed and purified the human ALDH3A1 in E. coli and used the recombinant protein to investigate its in vitro ability to protect SmaI and citrate synthase (from precipitation and/or deactivation) under thermal stress conditions. Our results indicate that recombinant ALDH3A1 exhibits significant chaperone function in vitro. Furthermore, over-expression of the fused histidine-tagged ALDH3A1 confers host E. coli cells with enhanced resistance to thermal shock, while ALDH3A1 over-expression in the human corneal cell line HCE-2 was sufficient for protecting them from the cytotoxic effects of both hydrogen peroxide and tert-butyl hydroperoxide. These results further support the chaperone-like function of human ALDH3A1. Taken together, ALDH3A1, in addition to its primary metabolic role in fundamental cellular detoxification processes, appears to play an essential role in protecting cellular proteins against aggregation under stress conditions.

Item Type: Article
Uncontrolled Keywords: Aldehyde dehydrogenase 3A1, corneal crystallin, molecular chaperone
Subjects: C700 Molecular Biology, Biophysics and Biochemistry
Department: Faculties > Health and Life Sciences > Applied Sciences
Depositing User: Ay Okpokam
Date Deposited: 23 May 2017 09:52
Last Modified: 28 Oct 2017 14:00
URI: http://nrl.northumbria.ac.uk/id/eprint/30791

Actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics


Policies: NRL Policies | NRL University Deposit Policy | NRL Deposit Licence