Journal
REDOX BIOLOGY
Volume 15, Issue -, Pages 135-142Publisher
ELSEVIER
DOI: 10.1016/j.redox.2017.11.028
Keywords
OxMIF; Carbamylation; N-terminal proline; Inflammation; Cytokine; Myeloperoxidase; Tautomerase; Redox regulation; Post-translational modification
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Funding
- Deutsche Forschungsgemeinschaft (DFG) [SFB1123/A3, SyNergy EXC1010]
- Else-Kroner-Fresenius-Stiftung (EKFS) [2014_A216]
- Marsden Fund Council from Government funding [UOO1102]
- Health Research Council of New Zealand
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Macrophage migration inhibitory factor (MIF) is a chemokine-like protein and an important mediator in the inflammatory response. Unlike most other pro-inflammatory cytokines, a number of cell types constitutively express MIF and secretion occurs from preformed stores. MIF is an evolutionarily conserved protein that shows a remarkable functional diversity, including specific binding to surface CD74 and chemokine receptors and the presence of two intrinsic tautomerase and oxidoreductase activities. Several studies have shown that MIF is subject to post-translational modification, particularly redox-dependent modification of the catalytic proline and cysteine residues. In this review, we summarize and discuss MIF post-translational modifications and their effects on the biological properties of this protein. We propose that the redox-sensitive residues in MIF will be modified at sites of inflammation and that this will add further depth to the functional diversity of this intriguing cytokine.
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