CASP7

(redirected from caspase-7)

CASP7

A gene on chromosome 10q25 that encodes a protein belonging to the cysteine-aspartic acid protease (caspase) family which, once activated by proteolytic processing, plays a central role in the execution phase of apoptosis. Effector (also called executioner) caspases CASP3, -6 and -7 are responsible for cleaving downstream substrates—CASP7 cleaves and activates sterol regulatory element binding proteins (SREBPs). It is highly expressed in the lung, skeletal muscle, liver, kidney, spleen and heart.
Segen's Medical Dictionary. © 2012 Farlex, Inc. All rights reserved.
References in periodicals archive ?
It involves the activation of caspase-9 which then triggers a cascade of events involving caspase-3 and caspase-7 activation8.
XIAP, a member of IAP family with baculovirus IAP repeat (BIR) domain, has been shown to bind to and inhibit caspase-3 and caspase-7 via the BIR2 linker region, leading to alternation of cellular localization and blockage of the caspases docking to their substrates [29].
Bressenot, A., et al., Assessment of apoptosis by immunohistochemistry to active caspase-3, active caspase-7, or cleaved PARP in monolayer cells and spheroid and subcutaneous xenografts of human carcinoma.
Different sub-cellular distribution of Caspase-3 and Caspase-7 following Fas-induced apoptosis in mouse liver.
To rule out the possibility that caspase-7, which shares similar substrate specificity with caspase-3, is compensatory activated in [Casp3.sup.-/-][ApoE.sup.-/-] BMDM and [Casp3.sup.-/-][ApoE.sup.-/-] VSMCs, a fluorometric DEVD substrate-based caspase activity assay was performed.
Executioner caspase-3 and caspase-7 are functionally distinct proteases.
The protective effects shown by caspase inhibitors are further supported by experiments using selective caspase-7 deficient mice that were found to be resistant to lipopolysaccharide-induced lymphocyte apoptosis as well as lipopolysaccharide-induced lethality, independent of the excessive production of serum cytokines (44).
As a consequence, cleaved caspase-9 and cleaved caspase-7 levels were significantly downregulated, indicating negative regulation of apoptosis by COC extract.
They observed no significant differences in the activation of downstream executioner caspase-3 and caspase-7 in HeLa cells infected with wild-type EPEC or a [DELTA]nleF EPEC derivative [25].
Executioner caspases (caspase-3, caspase-6, and caspase-7) and upstream effector caspases (caspase-2, caspase-8, caspase-9, and caspase-10) are well known as mediators in AD brains [23].
This leads to the activation of caspase-9, which then triggers a cascade of caspases activation (caspase-3 and caspase-7) resulting in the morphological and biochemical changes associated with apoptosis.
Full browser ?