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Blood, Vol. 95 No. 1 (January 1), 2000:
pp. 256-262
Nuclear factor- B activation by the photochemotherapeutic agent
verteporfin
D. J. Granville,
C. M. Carthy,
H. Jiang,
J. G. Levy,
B. M. McManus,
J.-Y. Matroule,
J. Piette, and
D. W. C. Hunt
From QLT PhotoTherapeutics Inc and the Department of Pathology and
Laboratory Medicine, St. Paul's Hospital-University of British
Columbia, Vancouver, Canada; and the Laboratory of Virology, Institute
of Pathology, University of Liege, Liege, Belgium.
The nuclear factor-kappa B (NF- B) gene transactivator serves in
the formation of immune, inflammatory, and stress responses. In
quiescent cells, NF-B principally resides within the cytoplasm in
association with inhibitory (IB) proteins. The status of IB
and NF-B proteins was evaluated for promyelocytic leukemia HL-60
cells treated at different intensities of photodynamic therapy (PDT).
The action of the potent photosensitizer, benzoporphyrin derivative
monoacid ring A (verteporfin), and visible light irradiation were
assessed. At a verteporfin concentration that produced the death of a
high proportion of cells after light irradiation, evidence of caspase-3
and caspase-9 processing and of poly(ADP-ribose) polymerase cleavage
was present within whole cell lysates. The general caspase inhibitor
Z-Val-Ala-Asp-fluoromethylketone (ZVAD.fmk) effectively blocked these
apoptosis-related changes. Recent studies indicate that IB proteins
may be caspase substrates during apoptosis. However, the level of
IB was unchanged for HL-60 cells undergoing PDT-induced
apoptosis. IB levels decreased during PDT-induced apoptosis,
though ZVAD.fmk did not affect this change. At a less intensive level
of photosensitization, cellular IB levels were transiently
depressed after PDT. At these times, p50 and RelA NF-B species were
increased within nuclear extracts, as revealed by electrophoretic
mobility supershift assays. HL-60 cells transiently transfected with a
B-luciferase reporter construct exhibited elevated luciferase
activity after PDT or treatment with tumor necrosis factor-, a
well-characterized NF-B activator. Productive NF-B activation and
associated gene transcription may influence the phenotype and behavior
of cells exposed to less intensive PDT regimens. However, IB is
not subject to caspase-mediated degradation as a component of
PDT-induced apoptosis. (Blood. 2000;95:256-262)
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