The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues

Claude Jourdan Le Saux, Heike Tronecker, Ljubica Bogie, Gillian D. Bryant-Greenwood, Charles D. Boyd, Katalin Csiszar

Research output: Contribution to journalArticlepeer-review

79 Scopus citations

Abstract

We have reported in this paper the complete cDNA sequence, gene structure, and tissue-specific expression of LOXL2, a new amine oxidase and a member of an emerging family of human lysyl oxidases. The predicted amino acid sequence, from several overlapping cDNA clones isolated from placenta and spleen cDNA libraries, shared extensive sequence homology with the conserved copper-binding and catalytic domains of both lysyl oxidase (LOX) and the lysyl oxidase-like (LOXL) protein. These conserved domains are encoded by five consecutive exons within the LOX, LOXL, and LOXL2 genes that also maintained exon-intron structure conservation. In contrast, six exons encoding the aminoterminal domains diverged both in sequence and structure. Exon 1 of the LOXL2 gene does not encode a signal sequence that is present in LOX and LOXL, suggesting a different processing and intracellular localization for this new protein. Expression of the LOXL2 gene was detected in almost all tissues with the highest steady state mRNA levels in the reproductive tissues, placenta, uterus and prostate. In situ hybridization identified placental syncytial and cytotrophoblasts responsible for the synthesis of LOXL2 mRNA and demonstrated a spatial and temporal expression pattern unique to the LOXL2 gene.

Original languageEnglish (US)
Pages (from-to)12939-12944
Number of pages6
JournalJournal of Biological Chemistry
Volume274
Issue number18
DOIs
StatePublished - Apr 30 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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