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Regulation of cell function by methionine oxidation and reduction
Author(s) -
Hoshi Toshinori,
Heinemann Stefan H.
Publication year - 2001
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1111/j.1469-7793.2001.0001j.x
Subject(s) - methionine sulfoxide reductase , methionine , methionine sulfoxide , cysteine , biochemistry , chemistry , amino acid , msra , reactive oxygen species , enzyme
Reactive oxygen species (ROS) are generated during normal cellular activity and may exist in excess in some pathophysiological conditions, such as inflammation or reperfusion injury. These molecules oxidize a variety of cellular constituents, but sulfur‐containing amino acid residues are especially susceptible. While reversible cysteine oxidation and reduction is part of well‐established signalling systems, the oxidation and the enzymatically catalysed reduction of methionine is just emerging as a novel molecular mechanism for cellular regulation. Here we discuss how the oxidation of methionine to methionine sulfoxide in signalling proteins such as ion channels affects the function of these target proteins. Methionine sulfoxide reductase, which reduces methionine sulfoxide to methionine in a thioredoxin‐dependent manner, is therefore not only an enzyme important for the repair of age‐ or degenerative disease‐related protein modifications. It is also a potential missing link in the post‐translational modification cycle involved in the specific oxidation and reduction of methionine residues in cellular signalling proteins, which may give rise to activity‐dependent plastic changes in cellular excitability.