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Blood, 1 September 2001, Vol. 98, No. 5, pp. 1542-1548
NEOPLASIA
Rapid extracellular release of cytochrome c is specific for
apoptosis and marks cell death in vivo
Andrea Renz,
Wolfgang E. Berdel,
Michael Kreuter,
Claus Belka,
Klaus Schulze-Osthoff, and
Marek Los
From the Department of Immunology and Cell Biology,
Department of Hematology/Oncology, University of Münster, D-48149
Münster, Germany, and Department of Radiation Oncology,
University of Tübingen, D-72076, Tübingen, Germany.
Diverse death stimuli including anticancer drugs trigger apoptosis
by inducing the translocation of cytochrome c from the outer
mitochondrial compartment into the cytosol. Once released, cytochrome c
cooperates with apoptotic protease-activating factor-1 and
deoxyadenosine triphosphate in caspase-9 activation and initiation of
the apoptotic protease cascade. The results of this study show that on
death induction by chemotherapeutic drugs, staurosporine and triggering
of the death receptor CD95, cytochrome c not only translocates into the
cytosol, but furthermore can be abundantly detected in the
extracellular medium. The cytochrome c release from the cell is a rapid
and apoptosis-specific process that occurred within 1 hour after
induction of apoptosis, but not during necrosis. Interestingly,
elevated cytochrome c levels were observed in sera from patients with
hematologic malignancies. In the course of cancer chemotherapy, the
serum levels of cytochrome c in the majority of the patients grew
rapidly as a result of increased cell death. These data suggest that
monitoring of cytochrome c in the serum of patients with tumors might
serve as a useful clinical marker for the detection of the onset of
apoptosis and cell turnover in vivo.
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