A Histochemical Study of Phagocytic and Enzymatic Functions of Rabbit Mononuclear and Polymorphonuclear Exudate Cells and Alveolar Macrophages

The cytochrome oxidase (CO), aminopeptidase (AMP), succinic dehydrogenase (SD), acid phosphatase, esterase, and alkaline phosphatase of rabbit mononuclear (MN) and polymorphonuclear (PMN) peritoneal exudate cells and pulmonary alveolar macrophages (AM) - air dried on Mylar strips - were characterized by histochemical techniques with respect to stability, activators, inhibitors, and pH optima. A granule count method was established for the quantitation of these enzymes. For the acid phosphatase of MN, in which the most precise results were obtained, time, pH, substrate, and inhibitor curves resembled those commonly obtained biochemically. Five of these enzymes were usually more active in AM than MN, whereas the sixth, alkaline phosphatase, was not present in either cell type. AM also tended to consume more oxygen than MN and to divide more frequently. Since the most active cells in the population would be first involved in the host's defense against microbial agents, a comparison was made of the 10 per cent of the AM and MN with the highest enzymatic activities. No differences were found in the granule counts that were not reflected by the means. However, within a given AM population, cells containing ingested dust particles seemed to have higher enzymatic activities than those without particles. MN had greater acid phosphatase and SD activities than PMN and consumed more oxygen, but the CO, AMP, and esterase activites of both types of cells were of similar magnitude. PMN showed high alkaline phosphatase activity; MN showed none. A survey of the histochemical literature indicates that a positive correlation between the enzymatic and phagocytic activities of both MN and PMN exists in vivo.