Inhibition of neutrophil myeloperoxidase activity by selected tissues.
Myeloperoxidase, a polymorphonuclear leukocyte-specific enzyme, has been used previously to quantify the number of polymorphonuclear leukocytes in tissue. When this method was employed in an attempt to measure polymorphonuclear leukocyte numbers in infected kidneys, it was found that myeloperoxidase could not be demonstrated, although significant numbers of neutrophils were present in the pyelonephritic lesions. Further studies were carried out to determine the effect of other tissues on free and cell-bound exogenous myeloperoxidase. We have shown that while skin had little effect on enzyme levels, liver and spleen totally destroyed myeloperoxidase activity within 30 sec. Cardiac and striated muscle had an intermediate effect. When intact neutrophils were added to fresh cardiac tissue 72.5% myeloperoxidase activity was destroyed during the enzyme solubilization procedure. These findings indicate that the technique can only be used for the quantification of polymorphonuclear leukocytes in selected tissues and that appropriate controls are essential. Previous studies in which myeloperoxidase levels have been used to estimate polymorphonuclear leukocyte numbers in cardiac tissue will need reevaluation.
D000818:Animals; D006321:Heart / Q000502:physiology; D066298:In Vitro Techniques; D009504:Neutrophils / Q000201:enzymology*; D009195:Peroxidase / Q000032:analysis / Q000037:antagonists & inhibitors*; D051381:Rats
D009195:Peroxidase