Peroxidase-H2O2-halide system: Cytotoxic effect on mammalian tumor cells
RA Clark, SJ Klebanoff, AB Einstein and A Fefer
Myeloperoxidase, H2O2, and a halide constitute a potent antimicrobial
system. A cytotoxic effect of this system on a line of mouse ascitic
lymphoma cells (LSTRA) is demonstrated here using four different assay
systems: 51Cr release, trypan blue exclusion, inhibition of glucose C-1
oxidation, and loss of oncogenicity for mice. Deletion of each component of
the system, preheating the peroxidase, or addition of azide, cyanide, or
catalase abolished the cytotoxicity. Myeloperoxidase was effective with
either chloride or iodide as the halide, while lastoperoxidase was
effective with iodide but not chloride. The iodinated thyroid hormones,
triiodothyronine and thyroxine, could substitute for the halide, and H2O2
could be replaced by a peroxide- generating enzyme system such as glucose
and glucose oxidase or by H2O2 producing bacteria such as pneumococci or
streptococci. The possibility is raised that the peroxidases of
inflammatory cells and certain biologic fluids may affect tumor initiation
or growth in vivo.
Volume 45,
Issue 2,
pp. 161-170,
02/01/1975
Copyright © 1975 by The American Society of Hematology
