Aldehyde dehydrogenase 2 activation and coevolution of its εPKC-mediated phosphorylation sites
详细信息 查看全文
- 作者：Aishwarya Nene ; Che-Hong Chen ; Marie-Hélène Disatnik…
- 关键词：ALDH2 ; Aldehyde dehydrogenase 2 ; εPKC ; Phosphorylation ; Coevolution ; 4HNE
- 刊名：Journal of Biomedical Science
- 出版年：2017
- 出版时间：December 2017
- 年：2017
- 卷：24
- 期：1
- 全文大小：3532KB
- 刊物类别：Biomedical and Life Sciences
- 刊物主题：Biomedicine, general;
- 出版者：BioMed Central
- ISSN：1423-0127
- 卷排序：24
文摘
BackgroundMitochondrial aldehyde dehydrogenase 2 (ALDH2) is a key enzyme for the metabolism of many toxic aldehydes such as acetaldehyde, derived from alcohol drinking, and 4HNE, an oxidative stress-derived lipid peroxidation aldehyde. Post-translational enhancement of ALDH2 activity can be achieved by serine/threonine phosphorylation by epsilon protein kinase C (εPKC). Elevated ALDH2 is beneficial in reducing injury following myocardial infarction, stroke and other oxidative stress and aldehyde toxicity-related diseases. We have previously identified three εPKC phosphorylation sites, threonine 185 (T185), serine 279 (S279) and threonine 412 (T412), on ALDH2. Here we further characterized the role and contribution of each phosphorylation site to the enhancement of enzymatic activity by εPKC.