Molecular cloning of the cDNA coding for mouse aldehyde oxidase: tissue distribution and regulation in vivo by testosterone

The cDNA coding for mouse aldehyde oxidase (AO), a molybdoflavoprotein. has been isolated and characterized. The cDNA is 4347 nt long and consists of an open reading frame predicting a polypeptide of 1333 amino acid residues, with 5' and 3' untranslated regions of 13 and 335 nt respectively. The app arent molecular mass of the translation product in vitro derived from the c orresponding cRNA is consistent with that of the monomeric subunit of the A O holoenzyme. The cDNA codes for a catalytically active form of AO, as demo nstrated by transient transfection experiments conducted in the HC11 mouse mammary epithelial cell line. The deduced primary structure of the AO prote in cell line. The deduced primary structure of the AO protein contains cons ensus sequences Tor two distinct 2Fe-2S redox centres and a molybdopterin-b inding site. The amino acid sequence of the mouse AO has a high degree of s imilarity with the human and bovine counterparts. and a significant degree of relatedness to AO proteins of plant origin. Northern blot and in 6-week- old mice once a day for 11 days at a dosage of 50 mg/kg. At the end of the experiment, animals were killed and tissues were explanted. Procedures invo lving animals and their care were conducted in conformity with the institut ional guidelines that are in compliance with national(D.L. n. 116, G.U., su ppl. 40, 18 February 1992) and international laws and policies (EEC Council Directive 86/609, OJ L 358, 1, 12 December 1987; NIH Guide for the Care an d Use of Laboratory Animals, NIH Publication No. 85-23, 1985).