IMMUNOCYTOCHEMICAL STUDY OF P0 GLYCOPROTEIN, P1 AND P2 BASIC PROTEINS, AND MYELIN‐ASSOCIATED GLYCOPROTEIN (MAG) IN LESIONS OF IDIOPATHIC POLYNEURITIS

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Abstract
Schober R., Itoyama Y., Sternberger N.H., Trapp B.D., Richardson E.P., Asbury A.K., Quarles R.H. & Webster H. deF. (1981) Neuropathology and Applied Neurobiology 7, 421–434 Immunocytochemical study of P0 glycoprotein, P1 and P2 basic proteins, and myelin-associated glycoprotein (MAG) in lesions of idiopathic polyneuritis To investigate the mechanism of myelin breakdown in idiopathic polyneuritis, paraffin and Epon sections of lesions were immunostained with antisera to four 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 intemodal myelin. No single protein was affected selectively and lesions occurred in fibres of all sizes, not just in larger fibres 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 fibre alterations seen in segmental demyelination and Wallerian degeneration. In regenerating fibres, MAG antiserum stained periaxonal regions intensely; thin regenerating myelin sheaths were stained by P0 and BP antisera, but not by P2 antiserum. The results show that myelin sheath changes are identified more easily in immunostained sections than in conventional histological preparations. Our data also suggest that in idiopathic neuritis, myelin sheaths are the primary target and that the breakdown of myelin and its proteins is not secondary to Schwann cell damage.