Elsevier

Gene

Volume 179, Issue 2, 1996, Pages 279-286
Gene

Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta

https://doi.org/10.1016/S0378-1119(96)00387-3Get rights and content

Abstract

A 4040-bp cDNA was cloned from a human placenta library by screening with a polymerase chain reaction-amplified fragment. The fragment was generated from the library using primers corresponding to conserved sequences encompassing the topa quinone (TPQ) cofactor sites of the copper-containing proteins, bovine serum amine oxidase (BSAO) and human kidney diamine oxidase (DAO). The cloned cDNA contains a coding sequence from positions 161 to 2449. Between bases 2901 and 2974, in a very long 1591-bp 3′-untranslated region, there is a G/A-rich region in the minus strand, which contains a (AGG)5 tandem repeat. The human placenta cDNA sequence and its translated amino acid sequence are 84% and 81% identical to the corresponding BSAO sequences, while the identities for the placenta sequences and those for human kidney DAO are 60% and 41%, respectively. The TPQ consensus nucleotide and protein sequences are identical for the placenta enzyme and BSAO, but the corresponding sequences for human kidney DAO are nonidentical. Three His residues that have been identified as Cu(II) ligands in other amine oxidases are conserved in the human placenta amine oxidase protein sequence. It was concluded that the placenta cDNA open-reading frame codes for a copper-containing, TPQ-containing monoamine oxidase. A putative 19-amino acid signal peptide was identified for human placenta amine oxidase. The resulting mature protein would be composed of 744 amino acids, and would have a Mr of 82 525. Comparison of the human placenta amine oxidase with DNA sequences found in GenBank suggests that the gene for this enzyme is located in the q21 region of human chromosome 17, near the BRCA1 gene.

References (44)

  • A. Rossi et al.

    cDNA-derived amino-acid sequence of lentil seedlings' amine oxidase

    FEBS Lett.

    (1992)
  • K. Tanizawa et al.

    Cloning and sequencing of pheylethylamine oxidase from Arthrobacter globoformis and implication of Tyr-382 as the precursor to its covalently bound quinone cofactor

    Biochem. Biophys. Res. Commun.

    (1994)
  • A.J. Tipping et al.

    Cloning and molecular analysis of the pea seedling copper amine oxidase

    J. Biol. Chem.

    (1995)
  • P. Barbry et al.

    Human kidney amiloride-binding pretein: cDNA structure and functional expression

  • J.R.D. Blicharski et al.

    Semicarbazide-sensitive amine oxidase activity in rat aortic cultured smooth muscule cells

    J. Neural. Transm. (Suppl.)

    (1990)
  • F. Boomsma et al.

    Plasma semicarbazide-sensitive amine oxidase activity is elevated in diabetes mellitus and correlates with glycosylated haemoglobin

    Clin. Sci.

    (1995)
  • M.A. Brown et al.

    Physical mapping, cloning, and identification of genes within a 500-kb region containing BRCA1

  • V. Campazano et al.

    Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion

    Science

    (1996)
  • J.C. Carlson et al.

    Generation of free radicals and messanger function

    J. Appl. Physiol.

    (1995)
  • A. Fernandez de Arriba et al.

    Monoamine oxidase and semicarbazide-sensitive amine oxidase activities in bovine eye

    J. Neural. Transm. (Suppl).

    (1990)
  • L.S. Friedman et al.

    The search for BRCA1

    Cancer Res.

    (1990)
  • J.M. Hall et al.

    Linkage of early-onset familial breast cancer to chromosome 17q21

    Science

    (1990)
  • Cited by (71)

    • Influence of susceptibility to hydrolysis and hydrophobicity of arylsemicarbazones on their anti-nociceptive and anti-inflammatory activities

      2012, European Journal of Medicinal Chemistry
      Citation Excerpt :

      During inflammation, lymphocyte migration plays an important role and is mediated by endothelial cells activation by well-characterized biomolecules, such as SSAO [10]. SSAO cloning showed that it belongs to amino-oxidases family, identical to a copper-containing amino-oxidase associated to cell membrane [19,20]. This enzyme converts primary amines to aldehydes, releasing ammonia and hydrogen peroxide [21].

    • Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes

      2007, Biochimie
      Citation Excerpt :

      Affinity constants were also different between WAT and placenta, but with a lower level of significance: Km = 251 ± 18 vs. 436 ± 82 μM, respectively (P < 0.02). Thus adipose tissue is richer in SSAO activity than placenta, previously considered as a reference for SSAO studies [7]. Under similar conditions, Vmax for MAO-dependent tyramine oxidation was 1.30 ± 0.12 and 15.1 ± 2.7 nmol oxidized/mg protein/min in human WAT and liver, respectively (P < 0.001, n = 8 and 3), with Km being 81 ± 9 and 115 ± 2 μM.

    View all citing articles on Scopus
    View full text