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Hydroxyacid oxidase 2

Hao-2, long chain alpha-hydroxy acid oxidase, hydroxyacid oxidase 3, HAOX2
This gene is one of three related genes that have 2-hydroxyacid oxidase activity yet differ in encoded protein amino acid sequence, tissue expression and substrate preference. Subcellular location of the encoded protein is the peroxisome. Specifically, this gene is expressed predominantly in liver and kidney and has the highest activity toward the substrate 2-hydroxypalmitate. Two alternatively spliced variants encoding the same isoform have been described. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, HAD, glycolate oxidase, Kv2.1, Monarch
Papers on Hao-2
The metabolic gene HAO2 is down regulated in mouse, rat and human hepatocellular carcinoma and correlates with metastasis and poor survival.
New
Columbano et al., Cagliari, Italy. In J Hepatol, Dec 2015
We investigated the role of HAO2, a member of this family, in rat, mouse and human hepatocarcinogenesis. METHODS: We evaluated HAO2 expression by qRT-PCR in the following rodent models of hepatocarcinogenes: the Resistant-Hepatocyte, the CMD and the chronic DENA rat models and the TCPOBOP/DENA and TCPOBOP only mouse models.
Discovery of pyrazole carboxylic acids as potent inhibitors of rat long chain L-2-hydroxy acid oxidase.
Singh et al., Pune, India. In Bioorg Med Chem Lett, 2012
Long chain L-2-hydroxy acid oxidase 2 (Hao2) is a peroxisomal enzyme expressed in the kidney and the liver.
Potent and Selective Inhibitors of Long Chain l-2-Hydroxy Acid Oxidase Reduced Blood Pressure in DOCA Salt-Treated Rats.
Cai et al., Pune, India. In Acs Med Chem Lett, 2012
l-2-Hydroxy acid oxidase (Hao2) is a peroxisomal enzyme with predominant expression in the liver and kidney.
Fetal hemoglobin in sickle cell anemia: genetic determinants of response to hydroxyurea.
Steinberg et al., Boston, United States. In Pharmacogenomics J, 2007
Both methods revealed that SNPs in genes within the 6q22.3-23.2 and 8q11-q12 linkage peaks, and also the ARG2, FLT1, HAO2 and NOS1 genes were associated with the HbF response to HU. Polymorphisms in genes regulating HbF expression, HU metabolism and erythroid progenitor proliferation might modulate the patient response to HU.
Reversible cysteine-targeted oxidation of proteins during renal oxidative stress.
Shattock et al., London, United Kingdom. In J Am Soc Nephrol, 2003
These included the LDL receptor-related protein 2, ATP synthase alpha chain, heat shock protein 90 beta, hydroxyacid oxidase 3, serum albumin precursor, triose phosphate isomerase, and lamin.
Use of a panel of congenic strains to evaluate differentially expressed genes as candidate genes for blood pressure quantitative trait loci.
Cicila et al., Toledo, United States. In Hypertens Res, 2003
Seven out of 37 differentially expressed genes were mapped to congenic regions carrying BP QTLs, but only one of these genes, L-2 hydroxy acid oxidase (Hao2), showed the congenic strain-specific pattern of differential kidney gene expression predicted by its chromosomal location.
Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases.
Gould et al., Baltimore, United States. In J Biol Chem, 2000
Computer-based approaches identified three distinct human 2-hydroxy acid oxidase genes, HAOX1, HAOX2, and HAOX3, that encode proteins with significant sequence similarity to plant glycolate oxidase, a prototypical 2-hydroxy acid oxidase.
L-lactate oxidase and L-lactate monooxygenase: mechanistic variations on a common structural theme.
Massey et al., Tokushima, Japan. In Biochimie, 1994
From its cDNA sequence the amino acid sequence has been derived and shown to have high similarity with those of other enzymes catalyzing oxidation of L-alpha-hydroxy acids, including flavocytochrome b2, lactate monooxygenase, glycolate oxidase, mandelate dehydrogenases and a long chain alpha-hydroxy acid oxidase.
Chromosomal mapping in the mouse of eight K(+)-channel genes representing the four Shaker-like subfamilies Shaker, Shab, Shaw, and Shal.
Jockusch et al., Bielefeld, Germany. In Genomics, 1993
The following localizations were determined: Chr 2, cen-Acra-Kcna4-Pax-6-a-Pck-1-Kras-3-Kcn b1 (corresponding human Chrs 11p and 20q, respectively); Chr 3, cen-Hao-2-(Kcna2, Kcnc4)-Amy-1 (human Chr 1); and Chr 6, cen-Cola-2-Met-Kcnd2-Cpa-Tcrb-adr/Clc-1-Hox-1.1-Myk - 103-Raf-1-(Tpi-1, Kcna1, Kcna5, Kcna6) (human Chrs 7q and 12p, respectively).
Amino acid sequence of long chain alpha-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent alpha-hydroxy acid-oxidizing enzymes.
Lederer et al., Paris, France. In J Biol Chem, 1991
The complete amino acid sequence of rat kidney long chain alpha-hydroxy acid oxidase has been determined by microsequencing, using a number of standard enzymatic and chemical cleavages.
Genetics of hydroxyacid oxidase isozymes in the mouse: localisation of Hao-2 on linkage group XVI.
Holmes, In Heredity (edinb), 1978
The structural gene loci for these isozymes (Hao-2 and Amy-1) are apparently linked (4.9 +/- 2.4 per cent recombinants) in this organism, which places Hao-2 on linkage group XVI, since previous studies by Eicher and co-workers (1976) have localised Amy-1 on this chromosome.
The genetics of alpha-hydroxyacid oxidase and alcohol dehydrogenase in the mouse: evidence for multiple gene loci and linkage between Hao-2 and Adh-3.
Holmes, In Genetics, 1977
The structural gene loci for those enzymes (Adh-3 and Hao-2, respectively) are apparently linked (17.6% recombinants) in this organism, whereas the multiple gene loci for HAOX, Hao-1 (encoding the A4 liver isozyme) and Hao-2, exhibited independent segregation and are unlinked (50% recombinants).
Immunochemical homologies among L-alpha-hydroxyacid oxidase isozymes.
Holmes et al., Australia. In Int J Biochem, 1976
This provides further evidence that loci (Hao-1 ; Hao-2) encoding these isozymes are products of a recent gene duplication event.
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