ALDH1A3
Aldehyde dehydrogenase 1 family, member A3, also known as ALDH1A3 or retinaldehyde dehydrogenase 3 (RALDH3), is an enzyme that in humans is encoded by the ALDH1A3 gene,[5]
Function
Aldehyde dehydrogenase isozymes are thought to play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. The enzyme encoded by this gene uses retinal as a substrate, either in a free or a cellular retinol-binding protein form.[6]
Cancer
ALDH1A3 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. [7] For this reason, ALDH1A3 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression. [7]
References
- GRCh38: Ensembl release 89: ENSG00000184254 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000015134 - Ensembl, May 2017
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- Hsu LC, Chang WC, Hiraoka L, Hsieh CL (November 1994). "Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6". Genomics. 24 (2): 333–41. doi:10.1006/geno.1994.1624. PMID 7698756.
- "Entrez Gene: ALDH1A3".
- Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. PMID 25205602.
External links
- Human ALDH1A3 genome location and ALDH1A3 gene details page in the UCSC Genome Browser.
Further reading
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Wan C, Shi Y, Zhao X, et al. (2009). "Positive association between ALDH1A2 and schizophrenia in the Chinese population". Prog. Neuropsychopharmacol. Biol. Psychiatry. 33 (8): 1491–5. doi:10.1016/j.pnpbp.2009.08.008. PMID 19703508.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Nishimura M, Yoshitsugu H, Naito S, Hiraoka I (2002). "Evaluation of gene induction of drug-metabolizing enzymes and transporters in primary culture of human hepatocytes using high-sensitivity real-time reverse transcription PCR". Yakugaku Zasshi. 122 (5): 339–61. doi:10.1248/yakushi.122.339. PMID 12040753.
- Cañestro C, Catchen JM, Rodríguez-Marí A, et al. (2009). Gojobori T (ed.). "Consequences of lineage-specific gene loss on functional evolution of surviving paralogs: ALDH1A and retinoic acid signaling in vertebrate genomes". PLoS Genet. 5 (5): e1000496. doi:10.1371/journal.pgen.1000496. PMC 2682703. PMID 19478994.
- Saito A, Kawamoto M, Kamatani N (2009). "Association study between single-nucleotide polymorphisms in 199 drug-related genes and commonly measured quantitative traits of 752 healthy Japanese subjects". J. Hum. Genet. 54 (6): 317–23. doi:10.1038/jhg.2009.31. PMID 19343046.
- Rexer BN, Zheng WL, Ong DE (2001). "Retinoic acid biosynthesis by normal human breast epithelium is via aldehyde dehydrogenase 6, absent in MCF-7 cells". Cancer Res. 61 (19): 7065–70. PMID 11585737.
- Yoshida A, Rzhetsky A, Hsu LC, Chang C (1998). "Human aldehyde dehydrogenase gene family". Eur. J. Biochem. 251 (3): 549–57. doi:10.1046/j.1432-1327.1998.2510549.x. PMID 9490025.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.