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Human Caspase 4 Protein expressed in Escherichia coli (E. coli) - ABIN2487273
Chen, Xia, Fang, Hawke, Lu: Caspase-10-mediated heat shock protein 90 beta cleavage promotes UVB irradiation-induced cell apoptosis. in Molecular and cellular biology 2009
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Results indicate functional differences between human caspase-4 and murine caspase-11.
The last four amino acids of the NleF carboxy terminus are essential in inhibiting caspase-4-dependent inflammatory cell death.
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 Proteins) 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 Proteins) mediate IL-1alpha and IL-1beta (show IL1B Proteins) release from human monocytes after lipopolysaccharides stimulation.
both caspase-4 and caspase-5 (show CASP5 Proteins) 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 Proteins) inflammasome activation to drive IL-1beta (show IL1B Proteins) maturation.
Together, these data suggest that caspase-11/IL-1alpha pathway plays an important role in defending against Klebsiella pneumoniae by recruiting neutrophils in the early stage of infection.
Results indicate functional differences between human caspase-4 and murine caspase-11 (caspase 4).
The results demonstrate the activation of the caspase 1 (show CASP1 Proteins) precursor by caspase 11 and suggest a new mechanism of protection of Theiler murine encephalomyelitis virus-infected astrocytes from apoptosis.
Data suggest that Brucella melitensis effector protein TcpB suppresses caspase-4/11--mediated inflammation, subverting inflammasome activation in mouse macrophages; TcpB induces ubiquitination/degradation of caspase-4/11; TcpB suppresses caspase-4/11--mediated pyroptosis and proinflammatory responses induced by lipopolysaccharide.
systemic exposure to the bacterial endotoxin lipopolysaccharide (LPS (show TLR4 Proteins)) causes severe endothelial pyroptosis that is mediated by the inflammatory caspases, human caspases 4/5 in human ECs, or the murine homolog caspase-11 in mice in vivo.
Caspase (show CASP3 Proteins)-l, Caspase-11 and Dectin-1 (show CLEC7A Proteins)/syk (show SYK Proteins) pathway are involved in the IL-1beta (show IL1B Proteins) generation in fungal keratosis.
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 Proteins) via the RhoA GTPase, whereas caspase-1 (show CASP1 Proteins) 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 Proteins)-activated IL-18 (show IL18 Proteins) induces IFN-gamma (show IFNG Proteins) to prime caspase-11 and rapidly clear Burkholderia thailandensis infection.
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
, caspase 4
, caspase 13
, evolutionary related interleukin-1-beta-converting enzyme
, IL-1 beta-converting enzyme
, caspase-1/caspase-4 hybrid
, interleukin-1 beta convertase
, interleukin-1 beta-converting enzyme
, caspase 11, apoptosis-related cysteine peptidase
, caspase 11, apoptosis-related cysteine protease
, caspase-11 short form splicing
, protease ICH-3
, caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase)
, caspase 4, apoptosis-related cysteine peptidase