Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis

Caspase-2 was reported to be involved in a number of apoptotic pathways triggered by various stimuli. However, the molecular mechanism of procaspase-2 activation in the course of apoptosis remains poorly defined. In this report, we demonstrate that procaspase-2 is recruited to the CD95 (Fas/APO-1) d...

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Bibliographic Details
Published in:Blood 2006-07, Vol.108 (2), p.559-565
Main Authors: Lavrik, Inna N., Golks, Alexander, Baumann, Simone, Krammer, Peter H.
Format: Article
Language:English
Subjects:
Apoptosis
B-Lymphocytes
Biological and medical sciences
Caspase 2
Caspases - metabolism
Caspases - physiology
Cell Line, Tumor
Death Domain Receptor Signaling Adaptor Proteins
Enzyme Activation
Enzyme Precursors - metabolism
fas Receptor - metabolism
fas Receptor - physiology
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Humans
Immunobiology
Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation
Signal Transduction
T-Lymphocytes
Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism
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Summary:Caspase-2 was reported to be involved in a number of apoptotic pathways triggered by various stimuli. However, the molecular mechanism of procaspase-2 activation in the course of apoptosis remains poorly defined. In this report, we demonstrate that procaspase-2 is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex (DISC) in human T- and B-cell lines. We show that procaspase-2 is activated at the DISC on CD95 stimulation. Despite its presence at the DISC, caspase-2 does not initiate apoptosis on CD95 stimulation in caspase-8–deficient cell lines. Taken together, our data reveal that caspase-2 is activated at the DISC but does not play an initiating role in the CD95-induced apoptosis.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood-2005-07-007096