European Journal of Biomedical and Pharmaceutical Sciences

HISTOCHEMICAL LOCALIZATION OF MONOAMINE OXIDASE AND GLUCOSE 6 PHOSPHATE DEHYDROGENASE AND THEIR PROBABLE ROLE IN GUINEA PIGS WITH EXPERIMENTAL ALLERGIC ENCEPHALOMYELITIS

Dr. Mohamed Noorulla*

ABSTRACT

The pathogenesis and etiology of the demyelinating diseases, in particular Multiple Sclerosis, has been a subject for discussion and speculation since a long time. Several experimental models have been worked out to evolve the pathogenesis and etiology of demyelination. Experimental Allergic Encephalomyelitis is one such model, extensively studied for probing the basis of autoimmune reactivity and defining its role in neurologic disorders characterized by inflammation, demyelination including neurodegeneration as in multiple sclerosis in man. The two oxidoreductases, Monoamine oxidase and Glucose 6 phosphate dehydrogenase play a significant role in the pathogenesis of Experimental Allergic Encephalomyelitis involving hypertrophied astrocytes and mitochondria. Experimental Allergic Encephalomyelitis was induced in the adult healthy guinea pigs by weekly intradermal injection of homologous whole brain and spinal cord antigen together with complete Freund’s adjuvant into the foot pad of the animal. The animals were observed for clinical features of the disease after injection. Histochemical localization of Monoamine oxidase was examined by Tryptamine – tetrazolium method of Glenner and Glucose 6 phosphate dehydrogenase activity by the method of Cohan. The increased activity of Glucose 6 phosphate dehydrogenase and Monoamine oxidase at the margins and in the immediate vicinity of the plaques might be due to hypertrophied astrocytes leading to an increased activity of oxidoreductases in experimental allergic encephalomyelitis. The Purkinje neurones show hyper activity of both the enzymes.

Keywords: Experimental allergic encephalomyelitis, Multiple sclerosis, Inflammation, Demyelination, Monoamine oxidase, Glucose 6 phosphate dehydrogenase.