Milk fat globule-EGF factor 8 protein (MFG-E8)

Milk fat globule-EGF factor 8 protein (MFG-E8) is a secreted glycoprotein originally identified in milk and mammary epithelial cells, characterized by EGF-like and discoidin domains homologous to blood coagulation factor V/VIII[1][5]. Its primary function is to mediate the clearance of apoptotic cells by binding exposed phosphatidylserine on dying cells and interacting with specific integrins (αvβ3, αvβ5) on phagocytes, serving as a molecular bridge that facilitates engulfment and removal of cellular debris[2][5]. MFG-E8 is ubiquitously expressed across multiple tissues—including the intestine, mammary gland, skin, and immune cells—and plays crucial roles in maintaining tissue homeostasis, promoting mucosal healing, modulating angiogenesis, and inhibiting excessive inflammation or autoimmunity by supporting apoptotic cell removal[3][4][5]. Amyloid fragments derived from MFG-E8, such as medin, are implicated in age-related vascular amyloidosis[1]. Variations in MFG-E8 levels or activity are associated with a range of diseases, including chronic inflammation, autoimmune diseases, cancer, and vascular disorders[5]. Experimental therapies focus on both replacement (e.g., recombinant MFG-E8 for tissue repair) and inhibition (in cancer or neovascularization) of MFG-E8 function[3][5]. Direct interacting drugs are not currently approved, but recombinant MFG-E8 is under investigation as a clinical tool for tissue and immune modulation[3][5].

Other names

lactadherinmedinSED1EDIL1BA46OAcGD3SHsT19888hP47breast epithelial antigen BA46HMFGMFGMmilk fat globule-EGF factor 8SED-1sperm surface protein hP47O-acetyl disialoganglioside synthasesperm associated antigen 10SPAG10secreted epidermal growth factor repeat and discoidin domain-containing protein 1

Opsonization of apoptotic cells via binding to phosphatidylserine and integrin receptors (αvβ3, αvβ5) on phagocytes, facilitating apoptotic cell clearance[2][5]. Modulation of angiogenesis and cell migration, potentially through integrin signaling and cytoskeleton rearrangement[3]. Inhibition or antagonism as a means of blocking MFG-E8-induced angiogenesis in cancer models[1].