Macrophage migration inhibitory factor

Macrophage migration inhibitory factor (MIF), also known as glycosylation-inhibiting factor (GIF), L-dopachrome isomerase, or phenylpyruvate tautomerase is a

Macrophage migration inhibitory factor assembles into a trimer composed of three identical subunits. Each of these monomers contain two antiparallel alpha helices and a four-stranded beta sheet. The monomers surround a central channel with 3-fold rotational symmetry.^[12][13]

Response to injury

Cytokines play an important role in promoting wound healing and tissue repair. Cell injury results in MIF release which then interacts with CD74. MIF-CD74 signaling activates pro-survival and proliferative pathways that protects the host during injury.^[14]

Enzymatic activity

MIF contains two motifs with catalytic activity. The first is a 27 amino acid motif located at the

This gene encodes a lymphokine involved in cell-mediated immunity, immunoregulation, and inflammation.^[18][19][20] MIF plays a role in the regulation of macrophage function in host defense through the suppression of anti-inflammatory effects of glucocorticoids.^[20][21][22] This lymphokine and the JAB1 protein form a complex in the cytosol near the peripheral plasma membrane, which may indicate a role in integrin signaling pathways.^[23]

Mechanism of action

MIF binds to

• BNIPL,^[27]
• CD74,^{[28][29][30][31][32][33]}
• COPS5,^[34][35]
• CXCR4,^[36][37][38] and
• RPS19.^[39]

Multiple protozoan parasites produce homologs MIF that have similar inflammatory functions to human MIF, and play a role in their pathogenesis, invasion and immune evasion.^[42][43] A preclinical study showed that blocking parasite MIF improves outcome in severe protozoan infections.^[44] Examples of protozoans with MIF homologs that have been reported:

• Entamoeba histolytica,^[45]
• Plasmodium falciparum,^[46]
• Toxoplasma gondii,^[47]
• Leishmania,^[48]
• Trichomonas vaginalis.^[49]

References