Search

Objective To explore the pathogenic mechanism of myelin oligodendrocyte glycoprotein-IgG（MOG-IgG）associated disorders （MOGAD） and screen the treatment drugs by establishing the MOGAD in vitro demyelination model. Methods The patient-derived MOG-IgG was purified by using the affinity chromatography based on transfected cells. The MOGAD in vitro demyelination model was constructed by the interaction between MOG-IgG and complement based on rat organotypic cerebellar slice and neuron-oligodendrocyte co-culture model. The expression level of myelin basic protein （MBP） and its colocalization with neurofilament protein （NF） were used as indicators to evaluate the myelin formation and injury. The myelin repair effect of drugs that promote the remyelination for multiple sclerosis was evaluated in this demyelination model. Results Highly-specific MOG-IgG was purified by the affinity chromatography based on transfected cells. After the treatment of antibodies and complement, the expression level of MBP and the colocalization degree of MBP-NF were significantly decreased in the MOG-IgG group （P = 0.003, P < 0.001）. After drug treatment, the expression levels of MBP were significantly up-regulated in the clemastine and domperidone groups （P = 0.030, P = 0.001）, and the colocalization degree of MBP-NF was significantly increased in the clemastine and domperidone groups （both P < 0.001）. Conclusions Highly-specific patient-derived MOG-IgG obtained by this method directly mediates myelin damage with the participation of complement. Clemastine and domperidone can promote the remyelination in this MOGAD in vitro demyelination model.