Myelinbasprotein

Myelinbasprotein, commonly referred to as myelin basic protein (MBP), is a major structural protein of the myelin sheath that insulates axons in the central nervous system. It is produced by oligodendrocytes and contributes to the dense compaction of the multilamellar myelin membrane by interacting with lipid bilayers and other myelin proteins. MBP is highly basic and intrinsically disordered in solution, allowing it to adopt membrane-associated conformations that stabilize the close apposition of cytoplasmic leaflets.

Multiple isoforms of MBP arise from alternative splicing and post-translational modifications, including phosphorylation and citrullination, which affect its charge, membrane binding, and susceptibility to proteolysis. These biochemical properties are important for normal myelin assembly, plasticity, and maintenance.

Clinically, MBP is notable as a key autoantigen implicated in demyelinating disorders. Immune responses against MBP have been associated with multiple sclerosis and experimental models of autoimmune encephalomyelitis, and fragments of MBP can be detected in cerebrospinal fluid following acute myelin injury. MBP is also used as a research marker of myelination and demyelination in neuropathological studies. Ongoing research explores how MBP structure, modifications, and interactions contribute to both normal myelin function and disease processes.