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Blood, Vol. 93 No. 9 (May 1), 1999:
pp. 3106-3115
Bcl-Xl- and Bax- -Mediated Regulation of Apoptosis of
Human Neutrophils Via Caspase-3
Pamela Weinmann,
Peter Gaehtgens, and
Barbara Walzog
From the Department of Physiology, Freie Universität, Berlin,
Germany.
In this study, a mechanism is reported which determines the lifetime
of polymorphonuclear neutrophils (PMN). In human PMN freshly isolated
from the circulation, expression of bcl-Xl, bax- , and
bak, members of the bcl-2 family of apoptosis-associated genes, was
found using the reverse transcription-polymerase chain reaction technique. In contrast, no expression of bcl-2 was seen in PMN, whereas
the myeloid cell line HL-60 was positive for bcl-2 mRNA. Two gene
products, Bcl-Xl and Bax-, which are known to function as the regulatory machinery of programmed cell death (apoptosis), were
detected at the protein level in PMN. Moreover, differential expression
of these proteins was found upon induction or prevention of apoptosis
by cytokines: Whereas induction of apoptosis by tumor necrosis
factor- was associated with a reduction of expression of the
anti-apoptotic Bcl-Xl protein, prevention of apoptosis by
granulocyte-macrophage colony-stimulating factor led to a
downregulation of expression of the death-promoting Bax- protein.
This shift of balance of anti- and pro-apoptotic proteins was found to
control caspase-3 activity which, in turn, downregulated
Bcl-Xl expression in PMN undergoing apoptosis. Thus,
cytokines can affect the ratio of Bax-/Bcl-Xl expression
in human PMN and modulate the subsequent activity of caspase-3, which
functions as executer of the programmed cell death and may
promote apoptosis by a positive feed-forward mechanism that
downregulates Bcl-Xl.
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