Sodium bicarbonate enhances membrane-bound and soluble human semicarbazide-sensitive amine oxidase activity in vitro

Mar Hernandez-Guillamon, Irene Bolea, Montse Solé, Mercè Boada, K. F. Tipton, Mercedes Unzeta

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

Abstract

Semicarbazide-sensitive amine oxidase (SSAO) is a multifunctional enzyme with different biological roles that depend on the tissue where it is expressed. Because SSAO activity is altered in several pathological conditions, we were interested in studying the possible regulation of the human enzyme activity. It has been previously reported that SSAO activity is increased in the presence of Dulbecco's modified Eagle medium (DMEM) in vitro. The aim of the present work was to investigate the effects of the different constituents of DMEM on human SSAO activity. We found that sodium bicarbonate was the only component able to mimic the enhancement of both human aorta and plasma SSAO activity in vitro, suggesting a possible physiological role of bicarbonate as an intrinsic modulator of the human enzyme. Failure to take this activating effect into account could also result in inaccuracies in the reported tissue activities of this enzyme. © 2007 The Japanese Biochemical Society.
Original languageEnglish
Pages (from-to)571-576
JournalJournal of Biochemistry
Volume142
DOIs
Publication statusPublished - 1 Nov 2007

Keywords

  • Activity enhancement
  • Dulbecco's modified eagle medium
  • Semicarbazide- sensitive amine oxidase
  • Sodium bicarbonate
  • Vascular adhesion protein-1

Fingerprint Dive into the research topics of 'Sodium bicarbonate enhances membrane-bound and soluble human semicarbazide-sensitive amine oxidase activity in vitro'. Together they form a unique fingerprint.

Cite this