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Zhang, Li, Jiang, Yu, An: Enhanced endoplasmic reticulum SERCA activity by overexpression of hepatic stimulator substance gene prevents hepatic cells from ER stress-induced apoptosis. in American journal of physiology. Cell physiology 2014
Akamatsu, Shibata, Ito, Sohma, Azuma, Otsuki: Riluzole induces apoptotic cell death in human prostate cancer cells via endoplasmic reticulum stress. in Anticancer research 2009
Pathophysiological studies showed that the overexpression of the CASP4 gene was involved in the loss of proximal tubules and renal injury in nephropathic cystinosis patients. Considering kidney's key roles in sodium filtration and reabsorption CASP4 genes are involved in Blood Pressure regulation.
We propose that microglial caspase-4 expression contributes to the cognitive impairments in Alzheimer's disease (AD), and that further study of caspase-4 will enhance our understanding of AD pathogenesis and may lead to novel therapeutic targets in AD.
this study shows that activation of caspase-4 is mediated by interactions with endotoxin-rich membrane interfaces rather than by endotoxin monomers
Specific activation of caspase-3 (show CASP3 ELISA Kits) and caspase-4 was found in proplatelets. Consistent with previous observations of caspase-4 autoactivation in response to endoplasmic reticulum (ER) stress, several ER stress marker proteins were expressed during proplatelet formation.
apoptosis is induced by rhein traditional Chinese medicine via induction of endoplasmic reticulum stress, caspase-4 and intracellular calcium in primary human hepatic HL-7702 cells
Caspase-4 and caspase-5 (show CASP5 ELISA Kits) mediate IL-1alpha and IL-1beta (show IL1B ELISA Kits) release from human monocytes after lipopolysaccharides stimulation.
both caspase-4 and caspase-5 (show CASP5 ELISA Kits) are functionally important for appropriate responses to intracellular Gram-negative bacteria.
caspase-4 activation alone is sufficient to induce pyroptosis, this process depends on the NLRP3 (show NLRP3 ELISA Kits) inflammasome activation to drive IL-1beta (show IL1B ELISA Kits) maturation.
This study reveled that CASP4 having a central role in the bipolar disease and schizophrenia manifestation.
NF-kappaB (show NFKB1 ELISA Kits) can mediate Fas (show FAS ELISA Kits)-induced apoptosis through caspase-4 protease
These data indicate that the caspase-11-mediated innate immune response plays a crucial role in defending against Acinetobacter baumannii.
Caspase-11 targets cofilin (show CFL1 ELISA Kits) via the RhoA GTPase, whereas caspase-1 (show CASP1 ELISA Kits) engages the Slingshot phosphatase
Hyperactive dendritic cells induce potent adaptive immune responses and are elicited by caspase-11, an enzyme that binds oxidized phospholipids and bacterial lipopolysaccharide.
Caspase-1 (show CASP1 ELISA Kits)-activated IL-18 (show IL18 ELISA Kits) induces IFN-gamma (show IFNG ELISA Kits) to prime caspase-11 and rapidly clear Burkholderia thailandensis infection.
These results argue that caspase-1 (show CASP1 ELISA Kits), -4 or -5 can be recruited to inflammasomes under specific circumstances, often leading to distinctly organized and localized complexes that may impact the functions of these proteases
gasdermin D is essential for caspase-11-dependent pyroptosis and interleukin-1beta maturation
But not in Casp11(-/-), Panx1 (show PANX1 ELISA Kits)(-/-), or P2x7 (show P2RX7 ELISA Kits)(-/-) mice.
active caspase-11 leads to a drop of intracellular potassium levels, which is necessary to activate NLRP3 (show NLRP3 ELISA Kits).
Data show that caspase-1 (show CASP1 ELISA Kits) but not caspase-11 was essential for the functional activities of the NLRC4 (show NLRC4 ELISA Kits) inflammasome.
Data indicate that genetic ablation of caspase-1 (show CASP1 ELISA Kits) and -11 from cpdm (show SHARPIN ELISA Kits) mice significantly reduced skin inflammation in sharpin (show SHARPIN ELISA Kits)-deficient mice.
This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain and a large and small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This caspase is able to cleave and activate its own precursor protein, as well as caspase 1 precursor. When overexpressed, this gene induces cell apoptosis. Alternative splicing results in transcript variants encoding distinct isoforms.
, apoptotic cysteine protease Mih1/TX
, caspase 4, apoptosis-related cysteine protease
, protease ICH-2
, protease TX
, caspase 11, apoptosis-related cysteine peptidase
, caspase 11, apoptosis-related cysteine protease
, caspase-11 short form splicing
, protease ICH-3
, caspase 11
, IL-1 beta-converting enzyme
, caspase-1/caspase-4 hybrid
, interleukin-1 beta convertase
, interleukin-1 beta-converting enzyme
, caspase 13
, evolutionary related interleukin-1-beta-converting enzyme