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. 2012 Jul 6;7(7):e40242. doi: 10.1371/journal.pone.0040242

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Hocher et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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A: Under conditions of oxidative stress the methionine residues at position 8 and 18 may be oxidized to methionine sulfoxide and methionine sulfone. Oxidation to methionine sulfoxide is reversible, whereas the second oxidation step to methionine sulfone is irreversible. Oxidized PTH changes its 3-dimesional structure. This blocks the interaction of PTH with its receptor. B: Schematic diagram of the full length PTH(1–84) molecule (“bioactive” intact PTH). Oxidation at position Met 8 and/or Met 18 (red) alters the receptor binding site of PTH. Oxidized PTH does not bind the PTH receptor anymore and is thus biologically inactive. (see: E. Blind, Clin. Lab. 2008;54∶439-446, reference 3).