Peroxidasin-like protein: A novel peroxidase homologue in the human heart

Zalán Péterfi, Zsuzsanna E. Tóth, Hajnal A. Kovács, Enik Lázár, Adrienn Sum, Ágnes Donkó, Gábor Sirokmány, Ajay M. Shah, Miklós Geiszt

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9 Citations (Scopus)

Abstract

AimsPeroxidases serve diverse biological functions including well-characterized activities in host defence and hormone biosynthesis. More recently, peroxidasin (PXDN) was found to be involved in collagen IV cross-linking in the extracellular matrix (ECM). The aim of this study was to characterize the expression and function of peroxidasin-like protein (PXDNL), a previously unknown peroxidase homologue.Methods and resultsWe cloned the PXDNL cDNA from the human heart and identified its expression pattern by northern blot, in situ hybridization, and immunohistochemistry. PXDNL is expressed exclusively in the heart and it has evolved to lose its peroxidase activity. The protein is produced by cardiomyocytes and localizes to cell-cell junctions. We also demonstrate that PXDNL can form a complex with PXDN and antagonizes its peroxidase activity. Furthermore, we show an increased expression of PXDNL in the failing myocardium.ConclusionPXDNL is a unique component of the heart with a recently evolved inactivation of peroxidase function. The elevation of PXDNL levels in the failing heart may contribute to ECM dysregulation due to its antagonism of PXDN function.

Original languageEnglish
Pages (from-to)393-399
Number of pages7
JournalCardiovascular research
Volume101
Issue number3
DOIs
Publication statusPublished - Mar 1 2014

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Keywords

  • Extracellular matrix
  • Peroxidase
  • Peroxidasin
  • Peroxidasin-like protein
  • Reactive oxygen species

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine
  • Physiology (medical)

Cite this

Péterfi, Z., Tóth, Z. E., Kovács, H. A., Lázár, E., Sum, A., Donkó, Á., Sirokmány, G., Shah, A. M., & Geiszt, M. (2014). Peroxidasin-like protein: A novel peroxidase homologue in the human heart. Cardiovascular research, 101(3), 393-399. https://doi.org/10.1093/cvr/cvt256