Human osteogenic sarcoma: fine structural localization of adenosine triphosphatase.

The localization of ATPases in 7 osteogenic sarcomas of osteoblastic, chondroblastic and fibroblastic type was investigated at the fine structural level using two types of substrates: one with lead as capturing ion and one with strontium (the latter presumed to reveal sites of Na+-K+-dependent transport ATPase). Reaction product with the lead-ATP medium was located on the plasma membrane and the membranes bordering subjacent vesicles and vacuoles in all the various types of osteoblastlike and fibroblastlike cells and also in types 1 and 3 chondroblastlike cells, and multinucleated giant cells believed to be neoplastic. Furthermore, deposits of reaction product were demonstrated in lysosomelike organelles in all the aforementioned cells. Except in the case of chondroblastlike cells, precipitates marking the localization of enzyme were confined to areas of the plasma membrane where adjacent cells were closely applied (the free surface lacked precipitates). In chondroblastlike cells the reaction product was usually deposited along the whole plasma membrane. Presence of L-Homoarginine or L-Tetramisole in the incubation medium in concentrations that have been shown to completely abolish alkaline phosphatase activity did not affect the occurrence of the reaction product with ATP as substrate indicating that the enzyme hydrolysing ATP was substrate-specific. Reaction product marking sites of Na+-K+-dependent ATPase was confined to plasma membranes and lysosomes of cells in vessel walls. The observations strengthen the notion obtained in studies on the localization of alkaline phosphatase, namely that osteoblastlike, chondroblastlike, and fibroblastlike cells in osteogenic sarcomas are histogenetically related to one another and to those multinucleated giant cells that presumably are of a neoplastic nature.