Reversible inhibition monoamine oxidase - A improves vascular dysfunction in canine carotid arteries exposed to angiotensin II

Adrian Sturza, Lavinia Noveanu, Oana Duicu, Maria Danila, Norbert Jost, Danina Muntean, Mircea Munteanu

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7 Citations (Scopus)

Abstract

Monoamine oxidase (MAO) is a flavinic enzyme, with two isoforms (A and B), located at the outer mitochondrial membrane that constantly generate hydrogen oeroxide (H2O2) as by-product of their catalytic cycle. We investigated the role of monoamine oxidase (MAO) in development of endothelial dysfunction in isolated dog carotid arteries after in vitro exposure to angiotensin 2 (Ang II). Canine carotid artery segments were incubated with Ang II in the presence or absence of moclobemide (a reversible MAO-A inhibitor) or catalase. Subsequently, the fragments were used for organ bath studies of vascular reactivity and for the hydrogen peroxide measurements. Pretreatment of vascular rings revealed that incubation with Ang elicited endothelial dysfunction via H2O2 production whereas co-treatment with moclobemide reduced the H2O2 levels and improved the vascular function in Ang II-treated vessels; in presence of L-NAME the effect of moclobemide was absent. In conclusion, MAO is an important source of ROS production, activated in response to Ang II and treatment with MAO inhibitors represents a possibility to reverse this negative effect.

Original languageEnglish
Pages (from-to)851-854
Number of pages4
JournalRevista de Chimie
Volume66
Issue number6
Publication statusPublished - Jun 1 2015

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Keywords

  • Angiotensin 2
  • Endothelial dysfunction
  • Moclobemide
  • Monoamine oxidase
  • Oxidative stress

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science (miscellaneous)
  • Engineering(all)
  • Surfaces, Coatings and Films
  • Materials Chemistry

Cite this

Sturza, A., Noveanu, L., Duicu, O., Danila, M., Jost, N., Muntean, D., & Munteanu, M. (2015). Reversible inhibition monoamine oxidase - A improves vascular dysfunction in canine carotid arteries exposed to angiotensin II. Revista de Chimie, 66(6), 851-854.