Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase. Andrés, N, Lizcano, J M, Rodríguez, M J, Romera, M, Unzeta, M, & Mahy, N J Histochem Cytochem, 49(2):209–17, 2, 2001.
Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase. [link]Paper  doi  abstract   bibtex   
Semicarbazide-sensitive amine oxidase (SSAO), widely distributed in highly vascularized mammalian tissues, metabolizes endogenous and xenobiotic aromatic and aliphatic monoamines. To assess whether its physiological role in humans is restricted to oxidation, we used an immunohistochemical approach to examine the cellular localization of SSAO in human peripheral tissues (adrenal gland, duodenum, heart, kidney, lung, liver, pancreas, spleen, thyroid gland, and blood vessels) and also analyzed its subcellular localization. The results are in agreement with the specific activities also determined in the same samples and are discussed with reference to the tissue distribution of monoamine oxidase A and B. Together with the oxidative deamination of monoamines, SSAO cellular localization indicates that, in most human peripheral tissues, it might participate in the regulation of physiological processes via H(2)O(2) generation. (J Histochem Cytochem 49:209-217, 2001)
@article{Andres-2001-ID175,
  title     = {Tissue activity and cellular localization of human semicarbazide-sensitive
               amine oxidase.},
  abstract  = {Semicarbazide-sensitive amine oxidase ({SSAO}), widely distributed in
               highly vascularized mammalian tissues, metabolizes endogenous and
               xenobiotic aromatic and aliphatic monoamines. To assess whether its
               physiological role in humans is restricted to oxidation, we used an
               immunohistochemical approach to examine the cellular localization of {SSAO}
               in human peripheral tissues (adrenal gland, duodenum, heart, kidney, lung,
               liver, pancreas, spleen, thyroid gland, and blood vessels) and also
               analyzed its subcellular localization. The results are in agreement with
               the specific activities also determined in the same samples and are
               discussed with reference to the tissue distribution of monoamine oxidase A
               and B. Together with the oxidative deamination of monoamines, {SSAO}
               cellular localization indicates that, in most human peripheral tissues, it
               might participate in the regulation of physiological processes via H(2)O(2)
               generation. (J Histochem Cytochem 49:209-217, 2001)},
  author    = {Andrés, N and Lizcano, J M and Rodríguez, M J and Romera, M and Unzeta, M
               and Mahy, N},
  journal   = {J Histochem Cytochem},
  volume    = {49},
  number    = {2},
  pages     = {209--17},
  year      = {2001},
  month     = {2},
  url       = {https://www.ncbi.nlm.nih.gov/pubmed/11156689},
  pmid      = {11156689},
  doi       = {10.1177/002215540104900208},
  keywords  = {Humans, Cell Line, Amine Oxidase (Copper-Containing), Enzyme Inhibitors,
               Immunoblotting, Immunohistochemistry, Organ Specificity, Semicarbazides},
  file      = {FULLTEXT:pdfs/000/000/000000175.pdf:PDF}
}

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