title: The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter.
abstract: The amiloride binding protein (ABP) is detected in many epithelium-rich and/or hematopoietic tissues (Lingueglia, E., Renard, S., Voilley, N., Waldmann, R., Chassande, O., Lazdunski, M., and Barbry, P. (1993) Eur. J. Biochem. 216, 679-687). The protein binds amiloride and some of its derivatives, such as phenamil, benzamil, and ethylpropylamiloride. These properties have previously suggested that ABP might be associated with an amiloride-sensitive Na+ channel. It corresponds in fact to an amiloride-sensitive diamine oxidase (DAO) that catalyzes the degradation of compounds such as putrescine or histamine. The analysis of the organization of the sequence of the human ABP/DAO gene reveals that the 2.4-kilobase messenger RNA is transcribed from two close origins identifying the proximal promoter. After sequencing, some corrections within the initial cDNA sequence have been made. Human ABP/DAO corresponds to a 751-residue polypeptide. The promoter activity of 1800 base pairs upstream of the transcription start sites of the long form has been analyzed. Two bulks of cis-activating sequences have been identified. One of them constitutes the proximal promoter. It contains a palindromic sequence previously described as E-PAL. This motif is essential for the full activity of the promoter and behaves like a composite element. This first molecular cloning of a human gene coding for a diamine oxidase will allow us to further understand its regulation during cell growth and/or embryonic development.
authors.affiliation: Institut de Pharmacologie Moléculaire et Cellulaire, Sophia Antipolis, Valbonne, France.
authors.forename: O
authors.initials: O
authors.lastname: Chassande
authors.forename: S
authors.initials: S
authors.lastname: Renard
authors.forename: P
authors.initials: P
authors.lastname: Barbry
authors.forename: M
authors.initials: M
authors.lastname: Lazdunski
mesh_terms: D006631:Amine Oxidase (Copper-Containing) / Q000096:biosynthesis / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000096:biosynthesis / Q000235:genetics*; D015500:Chloramphenicol O-Acetyltransferase / Q000096:biosynthesis / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000235:genetics; D017931:DNA Primers; D005091:Exons; D015698:Genomic Library; D006367:HeLa Cells; D015186:Hominidae / Q000235:genetics*; D006801:Humans; D007438:Introns; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D016133:Polymerase Chain Reaction; D011401:Promoter Regions, Genetic; D015183:Restriction Mapping; D014158:Transcription, Genetic; D014162:Transfection
chemical_list: D002352:Carrier Proteins; D017931:DNA Primers; D004247:DNA; D006631:Amine Oxidase (Copper-Containing); C065976:AOC1 protein, human; D015500:Chloramphenicol O-Acetyltransferase