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Cell surface monoamine oxidases: enzymes in search of a function
Author(s) -
Jalkanen S.,
Salmi M.
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.15.3893
Subject(s) - monoamine oxidase , biology , semicarbazide , biochemistry , enzyme , monoamine neurotransmitter , cell , metabolism , hydrogen peroxide , substrate (aquarium) , cell growth , cell adhesion , microbiology and biotechnology , chemistry , serotonin , receptor , ecology , organic chemistry
Ectoenzymes with a catalytically active domain outside the cell surface have the potential to regulate multiple biological processes. A distinct class of copper‐containing semicarbazide‐sensitive monoamine oxidases, expressed on the cell surface and in soluble forms, oxidatively deaminate primary amines. Via transient covalent enzyme–substrate intermediates, this reaction results in production of aldehydes, hydrogen peroxide and ammonium, which are all biologically active substances. The physiological functions of these enzymes have remained unknown, although they have been suggested to be involved in the metabolism of biogenic amines. Recently, new roles have been proposed for these enzymes in regulation of glucose uptake and, even more surprisingly, in leukocyte–endothelial cell interactions. The emerging functions of ectoenzymes in signalling and cell–cell adhesion suggest a novel mode of molecular control of these complex processes.