HISTOCHEMICAL MARKER OF HUMAN CATECHOLAMINE NEURONS IN GANGLION-CELLS AND PROCESSES OF A TEMPORAL-LOBE GANGLIOGLIOMA

A temporal lobe ganglioglioma was surgically removed from an 8-year-old boy who had developed temporal lobe paroxysmal convulsions. The present study describes staining reactions of the ganglioglioma tissue with histochemical methods designed to demonstrate the protein bodies, which are markers of catecholamine neurons in humans. Brookes’ procedure for basic proteins and rhodamine B for lipids showed identical staining of the following: (1) spherical inclusion bodies in the neoplastic neurons, (2) large eosinophilic globules in the dilated neuronal processes, and (3) the protein bodies in the neurons of human locus ceruleus and sympathetic ganglion. We conclude that the catecholamine neurons of the ganglioglioma possess the same marker of aminergic identity as normal catecholamine neurons in humans. Thus, this marker could be used as an additional diagnostic tool for the identification of this type of tumor

The fine structure of large dense-core organelles in human locus coeruleus neurons

Protein bodies, the characteristic spherical organelles present in human monoamine neurons, have been shown in previous electron microscope studies to originate as dense bodies in mitochondria. This study was designed to investigate the presence of catecholamine reaction products in the dense bodies of locus coeruleus neurons, in frozen fresh post-mortem brain tissue with the use of potassium permanganate (KMnO4) fixation. This fixation procedure forms a dense KMnO4/catecholamine reaction product, visible in the electron microscope, in the large dense-core vesicles of experimental animals. Our results demonstrate the localization of KMnO4 dense product in the cores of double membrane-bound spherical organelles, as well as in spherical structures in the matrix of typical mitochondria. No typical large dense-core vesicles were observed in these catecholamine neurons of the tissues studied. Our findings are consistent with the notion that altered mitochondria may contribute to the formation of a new type of large dense-core vesicle in the locus coeruleus neurons of man, which is probably an evolutionary adaptation of amine-storing organelles

LEWY BODIES IN PARKINSONISM SHARE COMPONENTS WITH INTRANEURONAL PROTEIN BODIES OF NORMAL BRAINS

Histochemical characteristics of the Lewy bodies, in catecholamine neurons of 10 Parkinsonian patients, were compared to those of the spherical protein bodies, the basic protein-rich markers of catecholamine neurons in man. Special methods for proteins and lipids showed that the core of the Lewy bodies, in the neurons of the locus coeruleus and the substantia nigra, contains basic proteins and lipids normally found in the protein bodies. Acid fuchsin and the lipid-soluble fluorescent dye rhodamine B stained the entire core of the Lewy body in the parkinsonian brains and the entire sphere of the protein body in the control brains. Bromsulfophthalein, another acidic dye, which selectively binds to the enzyme gluthathione-S-transferase, had affinity only for a ring-like lamina at the outer layer of the core of the Lewy body and for the outer rim of the protein body. These results demonstrate that Lewy bodies and protein bodies contain similar macromolecular components, that is lipids and two different types of proteins, which also show similar stratification in the two structures. On the other hand, the presence in several neurons of Parkinsonian patients, of aggregates representing transitional forms between protein bodies and Lewy bodies, indicates that abnormalities of protein bodies precede, and are somehow linked to Lewy body production