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Description

Myelin basic protein (UniProt: P02686, also known as MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein) is encoded by the MBP gene (Gene ID: 4155) in human. MBP is a homodimeric protein that is found in both the central and the peripheral nervous system. It is one of the most abundant protein component of the myelin membrane in the CNS and plays a role in both the formation and stabilization of this myelin membrane. It is responsible for adhesion of the cytosolic surfaces of multilayered compact myelin. MBP can interact with many polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and with negatively charged lipids. MBP isoforms are found in both the central and the peripheral nervous system, whereas Golli-MBP isoforms are expressed in fetal thymus, spleen and spinal cord, as well as in cell lines derived from the immune system. MBP expression begins abruptly in 14-16-week-old fetuses. Even smaller isoforms seem to be produced during embryogenesis, some of these persisting in the adult. MBP citrullination by peptidylarginine deiminase (PAD) leads to incomplete protein-lipid bilayer interactions and increases its vulnerability to proteolytic enzymes, resulting in disorganization of the myelin sheath in the central nervous system. Citrullinated MBP (citMBP) has been suggested to be a hallmark of demyelination. MBP citrullination has frequently been demonstrated in various CNS disorders. citMBP at R25, R122, and R130 is reported in the brains of subjects with Creutzfeldt-Jakob disease (CJD). Clone 1B8 specifically recognizes citMBP at R25. (Ref.: Jang, B., et al. (2017). Mol. Neurobiol. 55(4), 3172-3184, Boggs, JM (2006). Cell. Mol. Life Sci. 63(17), 1945-1961).