The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter

J Biol Chem. 1994 May 20;269(20):14484-9.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amine Oxidase (Copper-Containing) / biosynthesis
  • Amine Oxidase (Copper-Containing) / genetics*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carrier Proteins / biosynthesis
  • Carrier Proteins / genetics*
  • Chloramphenicol O-Acetyltransferase / biosynthesis
  • Chloramphenicol O-Acetyltransferase / metabolism
  • DNA / chemistry
  • DNA / genetics
  • DNA Primers
  • Exons
  • Genomic Library
  • HeLa Cells
  • Hominidae / genetics*
  • Humans
  • Introns
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Polymerase Chain Reaction
  • Promoter Regions, Genetic*
  • Restriction Mapping
  • Transcription, Genetic
  • Transfection


  • Carrier Proteins
  • DNA Primers
  • DNA
  • Amine Oxidase (Copper-Containing)
  • AOC1 protein, human
  • Chloramphenicol O-Acetyltransferase

Associated data

  • GENBANK/X78212