Macrophage migration inhibitory factor (MIF) modulates trophic signaling through interaction with serine protease HTRA1.

ABSTRACT: Macrophage migration inhibitory factor (MIF), a small conserved protein, is abundant in the immune- and central nervous system (CNS). MIF has several receptors and binding partners that can modulate its action on a cellular level. It is upregulated in neurodegenerative diseases and cancer although its function is far from clear. Here, we report the finding of a new binding partner to MIF, the serine protease HTRA1. This enzyme cleaves several growth factors, extracellular matrix molecules and is implicated in some of the same diseases as MIF. We show that the function of the binding between MIF and HTRA1 is to inhibit the proteolytic activity of HTRA1, modulating the availability of molecules that can change cell growth and differentiation. MIF is therefore the first endogenous inhibitor e

SUBMITTER: Fex Svenningsen A 

PROVIDER: S-EPMC5663815 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature