Methylamine metabolism to formaldehyde by vascular semicarbazide-sensitive amine oxidase

Paul J. Boor, Margaret B. Trent, Geoffrey A. Lyles, Ming Tao, G. A.S. Ansari

Research output: Contribution to journalArticlepeer-review

61 Scopus citations


The capacity of the vascular enzyme, semicarbazide-sensitive amine oxidase (SSAO), to metabolize methylamine to the potentially toxic product, formaldehyde, was tested using rat aortic homogenates and purified porcine aortic SSAO. Formaldehyde production in incubations of enzyme source with methylamine (1 mM) was detected by high performance liquid chromatography and product was confirmed by desorption chemical ionization mass spectrometry (DCI-MS). Inhibitor studies using the specific SSAO inhibitor semicarbazide and the monoamine oxidase inhibitor pargyline indicate that SSAO is responsible for metabolism of methylamine to formaldehyde. These results suggest the possibility that elevated methylamine found in several pathologic states (such as uremia and diabetes mellitus), or generated from exogenous sources, could result in overproduction of formaldehyde in tissues with high SSAO activity, especially blood vessels.

Original languageEnglish (US)
Pages (from-to)251-258
Number of pages8
Issue number3
StatePublished - 1992
Externally publishedYes


  • Aorta
  • Formaldehyde
  • Methylamine
  • Pargyline
  • Semicarbazide
  • Semicarbazide-sensitive amine oxidase

ASJC Scopus subject areas

  • Toxicology


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