MFAP4 belongs to the fibrinogen-related domain (FReD) family, which includes proteins involved in tissue homeostasis and innate immunity . The protein has binding specificities for both collagen and carbohydrates, suggesting its involvement in cell adhesion and intercellular interactions . MFAP4 primarily assembles into trimeric and hexameric structures of homodimers .
MFAP4 specifically binds to tropoelastin, fibrillin-1, and fibrillin-2, as well as the elastin cross-linking amino acid desmosine . These interactions are crucial for the proper organization and assembly of elastic fibers. MFAP4 has been shown to co-localize with fibrillin-1-positive fibers in vivo, indicating its role in elastic fiber formation .
The protein is thought to contribute to the assembly and maintenance of elastic fibers, which are essential for the elasticity and resilience of various tissues, including skin, lungs, and blood vessels . MFAP4’s involvement in elastic fiber formation makes it a key player in maintaining the structural integrity of these tissues.
Human recombinant MFAP4 is produced using recombinant DNA technology, which involves inserting the MFAP4 gene into a suitable expression system, such as bacteria or mammalian cells. This allows for the large-scale production of the protein for research and therapeutic purposes.