Microfibril-associated protein 2 (MFAP2)

Microfibril-associated protein 2 (MFAP2), also known as microfibril-associated glycoprotein 1 (MAGP-1), is a glycoprotein component of the extracellular matrix (ECM) that binds fibrillin and is essential in microfibril assembly, elastinogenesis, and regulation of tissue architecture[2][3][4]. MFAP2 plays key roles in controlling the bioavailability and signaling of growth factors, particularly the TGF-β family, by binding active forms and modulating ECM and cellular interactions[2][4][5]. It is implicated in cancer progression by regulating ECM remodeling, epithelial-mesenchymal transition, angiogenesis, and immune infiltration[1][5]. Genetic and expression studies show MFAP2 is essential for bone health, vascular stability, and metabolic function in animal models, with aberrant expression implicated in multiple human diseases[1][3][5]. There are currently no approved drugs that directly target MFAP2, but its functions make it a promising candidate for biomarker and potential therapeutic intervention in oncology and connective tissue disorders[1][5].

Other names

Microfibrillar-associated protein 2MAGP1MAGP-1MAGPMicrofibril-associated glycoprotein 1microfibril-associated glycoprotein-1

No approved drugs directly target MFAP2; as an ECM protein, its disease-modifying potential primarily involves modulation of growth factor signaling (especially TGF-β superfamily), cell-ECM interaction, and integrin signaling[2][4][5].