Редактирование: FAHD1

Acylpyruvase FAHD1, mitochondrial precursor (EC 3.7.1.5) (Fumarylacetoacetate hydrolase domain-containing protein 1) (FAH domain-containing protein 1) (Oxaloacetate decarboxylase) (EC 4.1.1.112) (OAA decarboxylase) (YisK-like protein) [C16orf36] [YISKL]

==Publications==

{{medline-entry
|title=Oxaloacetate decarboxylase [[FAH]]D1 - a new regulator of mitochondrial function and senescence.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/30055189
|abstract=[[FAH]]D1, a member of the [[FAH]] superfamily of enzymes, was identified in a proteomic screen for mitochondrial proteins with differential expression in young versus senescent human endothelial cells. [[FAH]]D1 acts as oxaloacetate decarboxylase, and recent observations suggest that [[FAH]]D1 plays an important role in regulating mitochondrial function. Thus, mutation of the nematode homolog, fahd-1, impairs mitochondrial function in Caenorhabditis elegans. When [[FAH]]D1 gene expression was silenced in human cells, activity of the mitochondrial electron transport (ETC) system was reduced and the cells entered premature senescence-like growth arrest. These findings suggest a model where [[FAH]]D1 regulates mitochondrial function and in consequence senescence. These findings are discussed here in the context of a new concept where senescence is divided into deep senescence and less severe forms of senescence. We propose that genetic inactivation of [[FAH]]D1 in human cells induces a specific form of cellular senescence, which we term senescence light and discuss it in the context of mitochondrial dysfunction associated senescence (MiDAS) described by others. Together these findings suggest the existence of a continuum of cellular senescence phenotypes, which may be at least in part reversible.
|mesh-terms=* Animals
* Caenorhabditis elegans
* Cellular Senescence
* Endothelial Cells
* Humans
* Hydrolases
* Mitochondria
|keywords=* FAHD1
* Mitochondria
* Oxaloacetate (OAA)
* Oxaloacetate decarboxylase (ODx)
* Senescence
* Senescence light
|full-text-url=https://sci-hub.do/10.1016/j.mad.2018.07.007
}}
{{medline-entry
|title=Depletion of oxaloacetate decarboxylase [[FAH]]D1 inhibits mitochondrial electron transport and induces cellular senescence in human endothelial cells.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/28286170
|abstract=In this study we report the identification of [[FAH]] domain containing protein 1 ([[FAH]]D1), a recently described member of the fumarylacetoacetate hydrolase ([[FAH]]) superfamily of metabolic enzymes, as a novel player in the regulation of cellular senescence. [[FAH]]D1 was found in a proteomic screen searching for mitochondrial proteins, which are differentially regulated in mitochondria from young and senescent human endothelial cells, and subsequently identified as oxaloacetate decarboxylase. We report here that depletion of [[FAH]]D1 from human endothelial cells inhibited mitochondrial energy metabolism and subsequently induced premature senescence. Whereas senescence induced by [[FAH]]D1 depletion was not associated with DNA damage, we noted a reduction of mitochondrial ATP-coupled respiration associated with upregulation of the cdk inhibitor p21. These results indicate that [[FAH]]D1 is required for mitochondrial function in human cells and provide additional support to the growing evidence that mitochondrial dysfunction can induce cellular senescence by metabolic alterations independent of the DNA damage response pathway.
|mesh-terms=* Cell Line
* Cellular Senescence
* Cyclin-Dependent Kinase Inhibitor p21
* DNA Damage
* Electron Transport
* Endothelial Cells
* Energy Metabolism
* Humans
* Hydrolases
* Mitochondria
|keywords=* DNA damage
* Energy metabolism
* FAHD1
* Mitochondria
* Oxaloacetate decarboxylase
* Premature senescence
|full-text-url=https://sci-hub.do/10.1016/j.exger.2017.03.004
}}