Disease relevance of Hao1

• Endothelial disruption and blebbing, elevated lung wet-to-dry ratio, and interstitial and alveolar edema indicated that anti-PECAM-GOX damaged pulmonary endothelium [1].

High impact information on Hao1

• Both types of conjugates had equally high pulmonary uptake after intravenous injection in mice, yet only small (200- to 250-nm), not large (600- to 700-nm), GOX conjugates caused profound oxidative vascular injury in the lungs, presumably owing to intracellular generation of H(2)O(2) [2].
• Ltk(-) and Cos-7 cells were transfected with vectors expressing a fusion protein of green fluorescence protein and Hao1, as well as mutants thereof [3].
• Recently, we have cloned a cDNA for the mouse hydroxyacid oxidase 1 (Hao1), a protein that seems to be localized in peroxisomes [3].
• Electrophoretic polymorphisms for stomach alcohol dehydrogenase (ADH-C2) and kidney L-alpha-hydroxyacid oxidase (HAOX-B4) have been identified in an Asian subspecies of mouse, Musmusculus castaneous [4].
• Coinjection of anti-PECAM/catalase protected against anti-TM/GOX-induced pulmonary oxidative stress, injury, and lethality, whereas polyethylene glycol catalase or IgG/catalase conjugates afforded only marginal protective effects [5].

Biological context of Hao1

• Genetics of hydroxyacid oxidase isozymes in the mouse: localisation of Hao-2 on linkage group XVI [6].
• The blind-sterile (bs) mutation in the mouse was localized on Chromosome 2 between Hao-1 and Emv-13 [7].

Anatomical context of Hao1

• After intravenous injection in mice, anti-TM/GOX binds to pulmonary endothelium and produces H2O2, which causes lung injury and 100% lethality within 7 h [5].
• To validate the strategy, we conjugated glucose oxidase (GOX) via streptavidin with antibodies to the endothelial cell surface antigen platelet endothelial cell adhesion molecule (PECAM) [1].

Associations of Hao1 with chemical compounds

• To test its protective effect, we employed a murine model of oxidative lung injury induced by glucose oxidase coupled with thrombomodulin antibody (anti-TM/GOX) [5].
• Peroxisomal glycolate oxidase and mitochondrial butyryl-CoA, octanoyl-CoA, and palmitoyl-CoA dehydrogenases were unaffected or increased [8].
• The protein has glycolate oxidase activity in vitro, as measured by the reduction of 2, 6-dichlorophenolindophenol in the presence of flavin mononucleotide and glycolate [9].

Other interactions of Hao1

• The enzyme locus (Dao) was shown to segregate independently of Hao-1, encoding the peroxisomal enzyme hydroxyacid oxidase (liver on A4 isozyme) [10].

Analytical, diagnostic and therapeutic context of Hao1

• Molecular cloning of mouse glycolate oxidase. High evolutionary conservation and presence of an iron-responsive element-like sequence in the mRNA [11].
• Previous work documented that 1) anti-PECAM-streptavidin carrier accumulates in the lungs after intravenous injection in animals and 2) anti-PECAM-GOX binds to, enters, and kills endothelium via intracellular H(2)O(2) generation in cell culture [1].
• The influence of immobilization chemistry was investigated with GOX [12].

References