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CASP7 — GZMB
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind Interaction:
GZMB
—
CASP7
Scott et al., EMBO J 2005*
-
IRef Bind_translation Interaction:
GZMB
—
CASP7
(experimental interaction detection)
Scott et al., EMBO J 2005*
-
IRef Hprd Interaction:
CASP7
—
GZMB
(in vitro)
Gu et al., J Biol Chem 1996*
-
IRef Innatedb Interaction:
GZMB
—
CASP7
(unknown, -)
Adrain et al., J Biol Chem 2005*
-
IRef Innatedb Interaction:
GZMB
—
CASP7
(unknown, -)
Cullen et al., J Cell Biol 2007*
-
IRef Innatedb Interaction:
GZMB
—
CASP7
(unknown, -)
Cullen et al., J Biol Chem 2009*
-
IRef Innatedb Interaction:
GZMB
—
CASP7
(unknown, -)
Scott et al., EMBO J 2005*
Text-mined interactions from Literome
Tepper et al., Blood 1999
(Burkitt Lymphoma) :
The apoptotic pathway distal to the DISC is intact because ceramide analogs, staurosporine, and
granzyme B activate
caspase-3 and induce apoptosis
Pathan et al., J Biol Chem 2001
(Neoplasms) :
TUCAN interferes with binding of Apaf1 to procaspase-9 and suppresses
caspase activation
induced by the Apaf1 activator, cytochrome c. Overexpression of TUCAN in cells by stable or transient transfection inhibits apoptosis and caspase activation induced by Apaf1/caspase-9 dependent stimuli, including Bax, VP16, and staurosporine, but not by Apaf1/caspase-9 independent stimuli, Fas and
granzyme B
Jerome et al., J Immunol 2001
:
In contrast,
caspase 3
activation in mitochondria-free cell lysates by
granzyme ( gr ) B was inhibited equivalently by Us5 deletion and rescue viruses, suggesting that gJ is not required for HSV to inhibition this process
Goping et al., Immunity 2003
:
Thus
granzyme B mediates direct cleavage of
caspase 3 and also activates mitochondrial disruption, resulting in the release of proapoptotic proteins that suppress caspase inhibition
Fellows et al., Blood 2007
:
Although GzmH is most closely related to the
caspase activating
granzyme B (GzmB) , neither a natural substrate nor a role in immune defense reactions has been demonstrated for this orphan granzyme
Gu et al., J Biol Chem 1996
:
The cleavage and
activation of
CMH-1 by
granzyme B in vitro sugge st that, in addition to CPP32, CMH-1 may also play a role in CTL mediated cell killing
Chinnaiyan et al., Curr Biol 1996
:
Here we report that
granzyme B also
activates ICE-LAP3/Mch3/CMH-1 ( referred to here as ICE-LAP3 ), which, along with Yama and Mch2, forms a subset of the ICE/CED-3 family of cysteine proteases most closely related to the Caenorhabditis elegans cell death gene, CED-3
Zapata et al., J Biol Chem 1998
:
Since the
granzyme B is a direct
activator of
caspase-3 and its expression is induced following T-cell activation, we tested the effects of anti-GraB, an engineered serpin that specifically inhibits GraB