Ja. Lincoln et al., EXOGENOUS MYELOPEROXIDASE ENHANCES BACTERIAL PHAGOCYTOSIS AND INTRACELLULAR KILLING BY MACROPHAGES, Infection and immunity, 63(8), 1995, pp. 3042-3047
It is well documented that myeloperoxidase (MyPo) contributes to the b
actericidal activities of neutrophils and monocytes. Since mature macr
ophages (M phi) are devoid of this enzyme, its participation in M phi-
mediated phagocytosis acid bacterial killing has not been completely d
efined. The present study demonstrates that exogenously added MyPo, at
physiological levels, enhances both phagocytosis and killing of Esche
richia coil. Murine peritoneal M phi were exposed to various concentra
tions of MyPo for different time intervals. Viable opsonized E. coli w
as added either prior to or after addition of MyPo. Thioglycolate-indu
ced but not resident M phi exhibited an increase in the number of phag
ocytizing cells. Both resident and thioglycolate-induced M phi demonst
rated increased bactericidal activity, Physiological levels of soluble
MyPo also induced a significant increase in chemiluminescence. Since
luminol dependent chemiluminescence measures reactive oxygen intermedi
ate production, studies were done to determine whether superoxide anio
n or H2O2 was involved in MyPo-iuduced M phi killing. Both superoxide
dismutase and catalase ablated MyPo-induced bactericidal activity. The
above data suggest that soluble MyPo, released from neutrophils at a
site of infection or inflammation, can enhance both phagocytosis and k
illing of microorganisms.