Electron-immunocytochemical localization of neuron-specific enolase in cytoplasm and on membranes of primary and metastatic cerebral tumours and on glial filaments of glioma cells.

A series of primary and metastatic human brain tumours was evaluated immunocytochemically for the electron microscopic localization of neuron-specific enolase (NSE). All contained cells which, regardless of the cell type, demonstrated an irregular distribution of NSE in their cytoplasm and on membranes. This was in contrast to the staining pattern in normal central nervous system (CNS) cells which, as previously reported (Vinores et al. 1984b), show only diffuse cytoplasmic staining usually not associated with membranes. In the tumours, the interior of nuclei and the cristae and matrices of mitochondria were consistently negative, as in normal CNS cells. Except in one low-grade fibrillary astrocytoma, the cytoplasmic filaments in neoplastic astrocytes were often, but not invariably, stained for NSE. The fine structural localization of NSE in neoplastic cells suggests that the conversion of 2-D-glycerophosphate to phosphoenolpyruvate by enolase may occur on the membrane and, in the case of astrocytic tumours, on the cytoplasmic filaments as well as in the cytoplasm. When cells which contain only the non-neuronal form of enolase (NNE) transform to neoplastic cells, they may acquire the ability to produce NSE. This presumably enables them to accommodate the increased metabolic demands of neoplasia by allowing them to elude the regulatory controls that are specific for NNE.