MIF is a cytokine that is involved in various immune responses. It is known to enhance macrophage functions such as adherence, spreading, phagocytosis, and tumoricidal activity . Structurally, MIF assembles into a trimer composed of three identical subunits, each containing two antiparallel alpha helices and a four-stranded beta sheet . This trimeric structure is crucial for its biological activity.
MIF is classified as an inflammatory cytokine due to its ability to induce the production of a large number of proinflammatory molecules . It plays a pivotal role in the pathogenesis of various inflammatory diseases, including rheumatoid arthritis (RA), by promoting inflammation and angiogenesis . MIF also counteracts the inhibitory effects of glucocorticoids on the immune system, thereby acting as a negative regulator of glucocorticoid-induced immunosuppression .
The production of recombinant MIF proteins has enabled more detailed investigations into its functions. In 1989, MIF was heterologously expressed as a recombinant protein, allowing researchers to study its role in various disease models . Recombinant MIF has been instrumental in resolving its crystal structure and understanding its diverse biological activities.
Given its involvement in numerous inflammatory and immune processes, MIF is considered a potential therapeutic target. However, targeting MIF therapeutically requires careful consideration due to its pleiotropic nature and the timing and severity of tissue injury . Therapeutics that target or mimic MIF family proteins are being explored for their potential in treating inflammatory diseases and promoting tissue repair.