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Immuno cytochemical study of p 0 glyco protein p 1 and p 2 basic proteins and myelin associated glyco protein in lesions of idiopathic poly neuritis


, : Immuno cytochemical study of p 0 glyco protein p 1 and p 2 basic proteins and myelin associated glyco protein in lesions of idiopathic poly neuritis. Neuropathology & Applied Neurobiology 7(6): 421-434

To investigate the mechanism of myelin breakdown in idiopathic polyneuritis in humans, paraffin and Epon sections of lesions were immunostained with antisera to 4 proteins in myelin sheaths. Three of these (P0, P2 and BP) are constituents of compact myelin whereas myelin-associated glycoprotein (MAG) is restricted to membranes near Schwann cell cytoplasm in periaxonal and paranodal regions and in Schmidt-Lanterman clefts. In early lesions, there were focal abnormalities in P2, P0 and BP immunostaining of paranodal and internodal myelin. No single protein was affected selectively and lesions occurred in fibers of all sizes, not just in larger fibers selectively stained by P2 antiserum. Early changes in MAG immunostaining occurred only in regions where myelin immunostaining also was abnormal. More severe, later changes in the distribution of P0, P2, BP and MAG were consistent with the sequence of myelinated fiber alterations seen in segmental demyelination and Wallerian degeneration. In regenerating fibers, MAG antiserum stained by P0 and BP antisera, but only by P2 antiserum. Myelin sheath changes are identified more easily in immunostained sections than in conventional histological preparations. In idiopathic neuritis, myelin sheaths are the primary target. The breakdown of myelin and its proteins is not secondary to Schwann cell damage.

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