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Department of Bacterial and Blood Products, National Institute of Infectious Diseases, Tokyo, Japan
Although apoptotic cells are recognized and engulfed by macrophages
via a number of membrane receptors, little is known about the fate of
apoptotic cells after the engulfment. We observed in this study that
nucleosomal DNA fragments of apoptotic cells disappeared when they were
engulfed by the macrophage cell line J774.1 at 37oC.
Pretreatment of J774.1 cells with chloroquine inhibited intensive DNA
degradation, indicating that the cleavage of nucleosomal DNA fragments
of apoptotic cells may take place in the lysosomes of J774.1. When
apoptotic cells were exposed to a lysosome-rich fraction derived from
J774.1 cells under an acidic condition, nucleosomal DNA fragments of
apoptotic cells were no longer detectable by agarose gel
electrophoresis. Additionally, we found that the lysosome-rich fraction
of J774.1 cells contained an acid DNase that is similar to DNase II
with respect to its m.w., optimal pH, and sensitivity to the inhibitors
of DNase II. By exposure of apoptotic cells to the lysosomal-rich
fraction, nucleosomal core histones of apoptotic cells were hydrolyzed
along with degradation of nucleosomal DNA fragments. Addition of
pepstatin A to the reaction buffer resulted in accumulation of
180-bp DNA fragments and inhibition of hydrolysis of nucleosomal
core histones. Leupeptin or CA-074 partially inhibited the degradation
of nucleosomal DNA fragments and core histones. These findings suggest
that lysosomal enzymes of macrophages, e.g., DNase II-like acid DNase
and cathepsins, are responsible for the degradation of nucleosomes of
apoptotic cells.
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