Caspases
Caspase Inhibitors
Apoptosis
Caspase 6
Caspase 3
Caspase 7
Amino Acid Chloromethyl Ketones
Cysteine Proteinase Inhibitors
Caspase 9
Caspases, Effector
Caspase 8
Caspase 2
Caspases, Initiator
Enzyme Activation
X-Linked Inhibitor of Apoptosis Protein
DNA Fragmentation
Cytochrome c Group
Proto-Oncogene Proteins c-bcl-2
Inhibitor of Apoptosis Proteins
Caspase 1
Antigens, CD95
Mitochondria
Cysteine Endopeptidases
Apoptotic Protease-Activating Factor 1
Poly(ADP-ribose) Polymerases
Cytochromes c
Jurkat Cells
Cell Death
Caspase 10
bcl-2-Associated X Protein
BH3 Interacting Domain Death Agonist Protein
Apoptosis Regulatory Proteins
Signal Transduction
bcl-X Protein
Apoptosomes
Apoptosis Inducing Factor
Staurosporine
In Situ Nick-End Labeling
Calpain
Fas-Associated Death Domain Protein
Enzyme Inhibitors
Fas Ligand Protein
Cell Survival
Tumor Cells, Cultured
Caspase 12
Serpins
HL-60 Cells
Annexin A5
TNF-Related Apoptosis-Inducing Ligand
Necrosis
Proteins
Carrier Proteins
Membrane Potential, Mitochondrial
HeLa Cells
Blotting, Western
Substrate Specificity
Cells, Cultured
Mitochondrial Proteins
Granzymes
Amino Acid Sequence
Cascara
Tumor Necrosis Factor-alpha
Etoposide
CRADD Signaling Adaptor Protein
bcl-2 Homologous Antagonist-Killer Protein
Molecular Sequence Data
Caspase 14
Reactive Oxygen Species
Transfection
Genes, bcl-2
Cytosol
Phosphatidylserines
Models, Biological
Receptor-Interacting Protein Serine-Threonine Kinases
Death Domain Receptor Signaling Adaptor Proteins
Mitochondrial Membranes
Lamins
Tumor Suppressor Protein p53
Dose-Response Relationship, Drug
Drosophila Proteins
Coumarins
U937 Cells
Intracellular Signaling Peptides and Proteins
Flow Cytometry
Proto-Oncogene Proteins
Protein Processing, Post-Translational
Protein Structure, Tertiary
Antineoplastic Agents, Phytogenic
JNK Mitogen-Activated Protein Kinases
Receptors, TNF-Related Apoptosis-Inducing Ligand
Receptors, Death Domain
Receptors, Tumor Necrosis Factor
NF-kappa B
Adaptor Proteins, Signal Transducing
Tosyllysine Chloromethyl Ketone
Neoplasm Proteins
Protein Synthesis Inhibitors
CASP8 and FADD-Like Apoptosis Regulating Protein
Bongkrekic Acid
Serine Endopeptidases
bcl-Associated Death Protein
Proteolysis
Membrane Potentials
Propidium
Intracellular Membranes
Cell Nucleus
Microscopy, Fluorescence
Neurons
Proteasome Endopeptidase Complex
Bcl-2 regulates amplification of caspase activation by cytochrome c. (1/9903)
Caspases, a family of specific proteases, have central roles in apoptosis [1]. Caspase activation in response to diverse apoptotic stimuli involves the relocalisation of cytochrome c from mitochondria to the cytoplasm where it stimulates the proteolytic processing of caspase precursors. Cytochrome c release is controlled by members of the Bcl-2 family of apoptosis regulators [2] [3]. The anti-apoptotic members Bcl-2 and Bcl-xL may also control caspase activation independently of cytochrome c relocalisation or may inhibit a positive feedback mechanism [4] [5] [6] [7]. Here, we investigate the role of Bcl-2 family proteins in the regulation of caspase activation using a model cell-free system. We found that Bcl-2 and Bcl-xL set a threshold in the amount of cytochrome c required to activate caspases, even in soluble extracts lacking mitochondria. Addition of dATP (which stimulates the procaspase-processing factor Apaf-1 [8] [9]) overcame inhibition of caspase activation by Bcl-2, but did not prevent the control of cytochrome c release from mitochondria by Bcl-2. Cytochrome c release was accelerated by active caspase-3 and this positive feedback was negatively regulated by Bcl-2. These results provide evidence for a mechanism to amplify caspase activation that is suppressed at several distinct steps by Bcl-2, even after cytochrome c is released from mitochondria. (+info)Caspase-mediated cleavage of p21Waf1/Cip1 converts cancer cells from growth arrest to undergoing apoptosis. (2/9903)
The cyclin-dependent kinase inhibitor p21waf1/Cip1 is a downstream effector of the p53-dependent cell growth arrest. We report herein that p21 was cleaved by caspase-3/CPP32 at the site of DHVD112L during the DNA damage-induced apoptosis of cancer cells. The cleaved p21 fragment could no more arrest the cells in G1 phase nor suppress the cells undergoing apoptosis because it failed to bind to the proliferating cell nuclear antigen (PCNA) and lost its capability to localize in the nucleus. Thus, caspase-3-mediated cleavage and inactivation of p21 protein may convert cancer cells from growth arrest to undergoing apoptosis, leading to the acceleration of chemotherapy-induced apoptotic process in cancer cells. (+info)Caspase 3 inactivation to suppress Fas-mediated apoptosis: identification of binding domain with p21 and ILP and inactivation machinery by p21. (3/9903)
The death mediator caspase acts as the dominant regulator during cell death induction. The CPP32 subfamily, including caspase 3 (CPP32/Yama/Apopain), is essential for the cell death signaling. We recently reported that activation of caspase 3 is regulated by complex formation with p21 or ILP. In the present study, we investigated the binding domain with p21 and ILP to further characterize the caspase 3 inactivation machinery. Our results show that caspase 3 contains p21 binding domain in the N-terminus and ILP binding domain in the active site. Further, the caspase 3 binding domain in p21 was independent of the Cdk- or PCNA-binding domain. We also found caspase 3 protection by p21 from the p3-site cleavage serineproteinase contributes to the suppression machinery. Here, we propose the caspase 3 inactivation system by p21 and ILP as new essential system in the regulation of cell death. (+info)Activation of c-Abl tyrosine kinase requires caspase activation and is not involved in JNK/SAPK activation during apoptosis of human monocytic leukemia U937 cells. (4/9903)
Genotoxic stress triggers the activation of several sensor molecules, such as p53, JNK1/SAPK and c-Abl, and occasionally promotes the cells to apoptosis. We previously reported that JNK1/SAPK regulates genotoxic stress-induced apoptosis in p53-negative U937 cells by activating caspases. c-Abl is expected to act upstream of JNK1/SAPK activation upon treatment with genotoxic stressors, but its involvement in apoptosis development is still unclear. We herein investigated the kinase activities of c-Abl and JNK1/SAPK during apoptosis elicited by genotoxic anticancer drugs and tumor necrosis factor (TNF) in U937 cells and their apoptosis-resistant variant UK711 cells. We found that the activation of JNK1/SAPK and c-Abl correlated well with apoptosis development in these cell lines. Unexpectedly, however, the JNK1/SAPK activation preceded the c-Abl activation. Moreover, the caspase inhibitor Z-Asp suppressed c-Abl activation and the onset of apoptosis but not the JNK1/SAPK activation. Interestingly, c-Abl tyrosine kinase inhibition by CGP 57148 reduced apoptosis without interfering with JNK1/SAPK activation. These results indicate that c-Abl acts not upstream of JNK1/ SAPK but downstream of caspases during the development of p53-independent apoptosis and is possibly involved in accelerating execution of the cell death pathway. (+info)Fas/Apo [apoptosis]-1 and associated proteins in the differentiating cerebral cortex: induction of caspase-dependent cell death and activation of NF-kappaB. (5/9903)
The developing cerebral cortex undergoes a period of substantial cell death. The present studies examine the role of the suicide receptor Fas/Apo[apoptosis]-1 in cerebral cortical development. Fas mRNA and protein are transiently expressed in subsets of cells within the developing rat cerebral cortex during the peak period of apoptosis. Fas-immunoreactive cells were localized in close proximity to Fas ligand (FasL)-expressing cells. The Fas-associated signaling protein receptor interacting protein (RIP) was expressed by some Fas-expressing cells, whereas Fas-associated death domain (FADD) was undetectable in the early postnatal cerebral cortex. FLICE-inhibitory protein (FLIP), an inhibitor of Fas activation, was also expressed in the postnatal cerebral cortex. Fas expression was more ubiquitous in embryonic cortical neuroblasts in dissociated culture compared to in situ within the developing brain, suggesting that the environmental milieu partly suppresses Fas expression at this developmental stage. Furthermore, FADD, RIP, and FLIP were also expressed by subsets of dissociated cortical neuroblasts in culture. Fas activation by ligand (FasL) or anti-Fas antibody induced caspase-dependent cell death in primary embryonic cortical neuroblast cultures. The activation of Fas was also accompanied by a rapid downregulation of Fas receptor expression, non-cell cycle-related incorporation of nucleic acids and nuclear translocation of the RelA/p65 subunit of the transcription factor NF-kappaB. Together, these data suggest that adult cortical cell number may be established, in part, by an active process of receptor-mediated cell suicide, initiated in situ by killer (FasL-expressing) cells and that Fas may have functions in addition to suicide in the developing brain. (+info)Activation of stress-activated protein kinase/c-Jun NH2-terminal kinase and p38 kinase in calphostin C-induced apoptosis requires caspase-3-like proteases but is dispensable for cell death. (6/9903)
Apoptosis was induced in human glioma cell lines by exposure to 100 nM calphostin C, a specific inhibitor of protein kinase C. Calphostin C-induced apoptosis was associated with synchronous down-regulation of Bcl-2 and Bcl-xL as well as activation of caspase-3 but not caspase-1. The exposure to calphostin C led to activation of stress-activated protein kinase/c-Jun NH2-terminal kinase (SAPK/JNK) and p38 kinase and concurrent inhibition of extracellular signal-regulated kinase (ERK). Upstream of ERK, Shc was shown to be activated, but its downstream Raf1 and ERK were inhibited. The pretreatment with acetyl-Tyr-Val-Ala-Asp-aldehyde, a relatively selective inhibitor of caspase-3, or benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (z-VAD.fmk), a broad spectrum caspase inhibitor, similarly inhibited calphostin C-induced activation of SAPK/JNK and p38 kinase as well as apoptotic nuclear damages (chromatin condensation and DNA fragmentation) and cell shrinkage, suggesting that caspase-3 functions upstream of SAPK/JNK and p38 kinase, but did not block calphostin C-induced surface blebbing and cell death. On the other hand, the inhibition of SAPK/JNK by transfection of dominant negative SAPK/JNK and that of p38 kinase by SB203580 induced similar effects on the calphostin C-induced apoptotic phenotypes and cell death as did z-VAD.fmk and acetyl-Tyr-Val-Ala-Asp-aldehyde, but the calphostin C-induced PARP cleavage was not changed, suggesting that SAPK/JNK and p38 kinase are involved in the DNA fragmentation pathway downstream of caspase-3. The present findings suggest, therefore, that the activation of SAPK/JNK and p38 kinase is dispensable for calphostin C-mediated and z-VAD.fmk-resistant cell death. (+info)Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases. (7/9903)
Alzheimer's disease is characterized by neurodegeneration and deposition of betaA4, a peptide that is proteolytically released from the amyloid precursor protein (APP). Missense mutations in the genes coding for APP and for the polytopic membrane proteins presenilin (PS) 1 and PS2 have been linked to familial forms of early-onset Alzheimer's disease. Overexpression of presenilins, especially that of PS2, induces increased susceptibility for apoptosis that is even more pronounced in cells expressing presenilin mutants. Additionally, presenilins themselves are targets for activated caspases in apoptotic cells. When we analyzed APP in COS-7 cells overexpressing PS2, we observed proteolytic processing close to the APP carboxyl terminus. Proteolytic conversion was increased in the presence of PS2-I, which encodes one of the known PS2 pathogenic mutations. The same proteolytic processing occurred in cells treated with chemical inducers of apoptosis, suggesting a participation of activated caspases in the carboxyl-terminal truncation of APP. This was confirmed by showing that specific caspase inhibitors blocked the apoptotic conversion of APP. Sequence analysis of the APP cytosolic domain revealed a consensus motif for group III caspases ((IVL)ExD). Mutation of the corresponding Asp664 residue abolished cleavage, thereby identifying APP as a target molecule for caspase-like proteases in the pathways of programmed cellular death. (+info)Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury. (8/9903)
We investigated mechanisms of cell death during hypoxia/reoxygenation of cultured kidney cells. During glucose-free hypoxia, cell ATP levels declined steeply resulting in the translocation of Bax from cytosol to mitochondria. Concurrently, there was cytochrome c release and caspase activation. Cells that leaked cytochrome c underwent apoptosis after reoxygenation. ATP depletion induced by a mitochondrial uncoupler resulted in similar alterations even in the presence of oxygen. Moreover, inclusion of glucose during hypoxia prevented protein translocations and reoxygenation injury by maintaining intracellular ATP. Thus, ATP depletion, rather than hypoxia per se, was the cause of protein translocations. Overexpression of Bcl-2 prevented cytochrome c release and reoxygenation injury without ameliorating ATP depletion or Bax translocation. On the other hand, caspase inhibitors did not prevent protein translocations, but inhibited apoptosis during reoxygenation. Nevertheless, they could not confer long-term viability, since mitochondria had been damaged. Omission of glucose during reoxygenation resulted in continued failure of ATP production, and cell death with necrotic morphology. In contrast, cells expressing Bcl-2 had functional mitochondria and remained viable during reoxygenation even without glucose. Therefore, Bax translocation during hypoxia is a molecular trigger for cell death during reoxygenation. If ATP is available during reoxygenation, apoptosis develops; otherwise, death occurs by necrosis. By preserving mitochondrial integrity, BCL-2 prevents both forms of cell death and ensures cell viability. (+info)Necrosis is a type of cell death that occurs when cells are exposed to excessive stress, injury, or inflammation, leading to damage to the cell membrane and the release of cellular contents into the surrounding tissue. This can lead to the formation of gangrene, which is the death of body tissue due to lack of blood supply.
There are several types of necrosis, including:
1. Coagulative necrosis: This type of necrosis occurs when there is a lack of blood supply to the tissues, leading to the formation of a firm, white plaque on the surface of the affected area.
2. Liquefactive necrosis: This type of necrosis occurs when there is an infection or inflammation that causes the death of cells and the formation of pus.
3. Caseous necrosis: This type of necrosis occurs when there is a chronic infection, such as tuberculosis, and the affected tissue becomes soft and cheese-like.
4. Fat necrosis: This type of necrosis occurs when there is trauma to fatty tissue, leading to the formation of firm, yellowish nodules.
5. Necrotizing fasciitis: This is a severe and life-threatening form of necrosis that affects the skin and underlying tissues, often as a result of bacterial infection.
The diagnosis of necrosis is typically made through a combination of physical examination, imaging studies such as X-rays or CT scans, and laboratory tests such as biopsy. Treatment depends on the underlying cause of the necrosis and may include antibiotics, surgical debridement, or amputation in severe cases.
Caspase
Caspase 10
Caspase 4
Caspase-2
Caspase 7
Caspase 6
Caspase-10
Caspase 2
Caspase 11
Caspase 14
Caspase 1
Caspase 13
Caspase 5
Caspase 12
Caspase 3
Caspase 8
Caspase-9
Caspase-activated DNase
Caspase 16, pseudogene
Caspase-8 deficiency
Sf caspase-1
Death regulator Nedd2-like caspase
Caspase recruitment domain-containing protein 8
Caspase activity and apoptosis inhibitor 1
Apoptosis
Bcl-2 family
GSDMD
Calpain-2 catalytic subunit
GZMB
Belnacasan
Human Caspase-8 Antibody MAB704: R&D Systems
Kallenberger2014 - CD95L induced apoptosis initiated by caspase-8, wild-type HeLa cells (cis/trans-cis/trans variant) |...
Induction of Inflammation by West Nile virus Capsid through the Caspase-9 Apoptotic Pathway - Volume 8, Number 12-December 2002...
Caspase-7 Blocking Peptide | BioVision, Inc.
FAM-FLICA® Caspase-8 Assay Kit
Caspase-3, human recombinant proteinase | E1003 | APExBIO
The gRAMP CRISPR-Cas effector is an RNA endonuclease complexed with a caspase-like peptidase | TU Delft Repositories
Developing a circularly permuted variant of Renilla luciferase as a bioluminescent sensor for measuring Caspase-9 activity in...
caspase 3
Commentary
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IMSEAR at SEARO: Role of caspases in apoptosis and disease.
Lack of correlation between caspase activation and caspase activity assays in paclitaxel-treated MCF-7 breast cancer cells -...
Caspase-1, Human, Recombinant, E. coli | 218783
Caspase-3 inhibitor Z-DEVD-FMK - LubioScience
Acute Circadian Disruption Due to Constant Light Promotes Caspase 1 Activation in the Mouse Hippocampus. | Cells;12(14)2023 07...
5 +/- 1.8 to 8.3 +/- 5.7% in c | Caspase Pathway
single polypeptide FPX caspase 1 sensor - Caspase1 Fluorescent Biosensor Details
Piperine induces apoptosis of lung cancer A549 cells via p53-dependent mitochondrial signaling pathway
Caspase-3 DEVD-R110 Fluorometric HTS Assay Kit | Technique alternative | 01018551680 - caspase-3.com
Huawei Announces Quad-Core Ascend G615 Smartphone | Tom's Hardware
Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation - CSHL Scientific Digital Repository
Pan-Caspase Inhibitor zVAD Induces Necroptotic and Autophagic Cell Death in TLR3/4-Stimulated Macrophages
La Caspase-3 est-elle impliquée dans la différenciation des cellules souches adultes ? - Normandie Université
Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-κB - Tohoku University
Induction of caspase-3-like protease may mediate delayed neuronal death in the hippocampus after transient cerebral ischemia ...
Identification of a caspase-derived N-terminal tau fragment in cellular and animal Alzheimer's disease models
Inhibitor5
- This in vitro assay employs the fluorescent inhibitor probe FAM-LETD-FMK to label active caspase-8 enzyme in living cells. (immunochemistry.com)
- Furthermore, piperine-induced apoptosis could be blocked by the broad caspase inhibitor z-VAD-fmk in majority. (nih.gov)
- In macrophages, necroptosis can be induced by co-treatment with Toll-like receptor (TLR) ligands (lipopolysaccharide [LPS] for TLR4 and polyinosinic-polycytidylic acid [poly I:C] for TLR3) and a cell-permeable pan-caspase inhibitor zVAD. (molcells.org)
- Furthermore, ventricular infusion of Z-DEVD-FMK, a caspase-3 inhibitor, decreased caspase-3 activity in the hippocampus and significantly reduced cell death and DNA fragmentation in the CA1 sector up to 7 d after ischemia. (unthsc.edu)
- The possibility that Bcl-x(L) inhibits cell death at a late (postmitochondrial) step in the death pathway is supported by this report of a novel apoptosis inhibitor, Aven, which binds to both Bcl-x(L) and the caspase regulator, Apaf-1. (johnshopkins.edu)
Inhibitors4
- A mutation in the allosteric site of the caspase 3 dimer interface of Val266 to histidine abolishes activity of the enzyme, and models predict that the mutation mimics the action of small molecule allosteric inhibitors by preventing formation of the active site. (ncsu.edu)
- This review discusses caspases, their inhibitors and regulators. (who.int)
- Since cytotoxic drugs used in chemotherapy of leukemia's and solid tumors cause apoptosis in target cells, elucidating the consequences of proteolytic activity occupies a central role for understanding of the molecular mechanism of apoptosis which can help us to use the caspase inhibitors as targets of therapy. (who.int)
- This issue should therefore be considered in developing caspase inhibitors for therapeutic applications. (cshl.edu)
Cleavage8
- Apoptosis in response to the ligand CD95L (also known as Fas ligand) is initiated by caspase-8, which is activated by dimerization and self-cleavage at death-inducing signaling complexes (DISCs). (ebi.ac.uk)
- Previous work indicated that the degree of substrate cleavage by caspase-8 determines whether a cell dies or survives in response to a death stimulus. (ebi.ac.uk)
- We derived and experimentally validated a minimal model in which cleavage of caspase-8 in the enzymatic domain occurs in an interdimeric manner through interaction between DISCs, whereas prodomain cleavage sites are cleaved in an intradimeric manner within DISCs. (ebi.ac.uk)
- The activation of caspase-8 by combined intra- and interdimeric cleavage ensures weak signaling at low concentrations of CD95L and strongly accelerated activation at higher ligand concentrations, thereby contributing to precise control of apoptosis. (ebi.ac.uk)
- For a caspase-9-specific test, 5 μg of pcWNV-Cp-DJY or pcWNV-CpWT was cotransfected with a dominant negative caspase-9 (DN caspase-9) construct, and cleavage of procaspase-9 protein was determined by Western blot analysis with antihuman caspase-9 antibody (MBL, Nagoya, Japan). (cdc.gov)
- Caspases are synthesized as precursor molecules that require processing at specific aspartate residues to produce the active enzyme which in turn leads to the cleavage of various death substrates that lead to morphological changes typical of apoptosis. (who.int)
- Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. (bvsalud.org)
- Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur. (bvsalud.org)
Apoptotic4
- It is known as the initiating caspase for the apoptotic cascade. (rndsystems.com)
- Recent studies using both molecular and cloning approaches, and in vitro systems have identified a class of highly specific proteases, termed caspases, that appear to have an important role in apoptotic execution. (who.int)
- As effectors of the apoptotic machinery, caspases are considered potential therapeutic targets. (cshl.edu)
- the expression of specific CNS enzyme (enolase), proinflammatory cytokines MIF and apoptotic marker caspase-3 in the umbilical blood of infants delivered for Covid positive mothers. (who.int)
Apoptosis via2
- ICT's FLICA assay kits are used by researchers seeking to quantitate apoptosis via caspase activity in cultured cells and tissues. (immunochemistry.com)
- Taken together, these results suggested that piperine could induce p53-mediated cell cycle arrest and apoptosis via activation of caspase-3 and caspase-9 cascades, as well as increasing the Bax/Bcl-2 ratio. (nih.gov)
Pathway6
- Apoptosis is induced through the mitochondrial pathway resulting in caspase-9 activation and downstream caspase-3 activation. (cdc.gov)
- We observed that the WNV-Cp protein is a pathogenic protein, which drives apoptosis in vitro through the mitochodrial/caspase-9 pathway. (cdc.gov)
- This entry was posted in Caspase Pathway by casp4137 . (caspasepathway.com)
- deficiency in caspases essential for this pathway, caspase-9 or caspase-3, unexpectedly resulted in rapid activation of alternate caspases after injection of Jo2, and therefore failed to protect mice against Jo2 toxicity. (cshl.edu)
- Moreover, both ultraviolet and gamma irradiation, two established inducers of the mitochondrial caspase-activation pathway, also elicited compensatory activation of caspases in cultured caspase-3(-/-) hepatocytes, indicating that the compensatory caspase activation was mediated through the mitochondria. (cshl.edu)
- These data demonstrate that PKC-mediated activation of caspase 3 is an integral and essential part of signaling pathway in RBCs, that may be a regulatory factor of RBC mechanical properties, through regulation of NO metabolism. (unicatt.it)
Activation18
- The FAM FLICA Caspase-8 assay probe allows researchers to assess caspase-8 activation. (immunochemistry.com)
- Peng, Z;Gillissen, B;Richter, A;Sinnberg, T;Schlaak, MS;Eberle, J. Enhanced Apoptosis and Loss of Cell Viability in Melanoma Cells by Combined Inhibition of ERK and Mcl-1 Is Related to Loss of Mitochondrial Membrane Potential, Caspase Activation and Upregulation of Proapoptotic Bcl-2 Proteins . (immunochemistry.com)
- 2007) NF-κB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1 . (emdmillipore.com)
- Using an established in vivo model of Fas-mediated apoptosis, we demonstrate here that elimination of certain caspases was compensated in vivo by the activation of other caspases. (cshl.edu)
- Our findings provide direct experimental evidence for compensatory pathways of caspase activation. (cshl.edu)
- Acute Circadian Disruption Due to Constant Light Promotes Caspase 1 Activation in the Mouse Hippocampus. (bvsalud.org)
- Proteolytic activation of the caspase-3 precursor was detected in hippocampus and CPu but not in cortex at 4-72 hr after ischemia. (unthsc.edu)
- Protein kinase C mediates caspase 3 activation: A role for erythrocyte morphology changes. (unicatt.it)
- Here we extend our previous observations, reporting that RBC morphology is regulated by a series of specific cell signaling events linked to Protein Kinase C (PKC)-mediated activation of caspase 3. (unicatt.it)
- Inhibition of PKC also completely inhibits PMA mediated caspase-3 activation. (unicatt.it)
- Aven interferes with the ability of Apaf-1 to self-associate, suggesting that Aven impairs Apaf-1-mediated activation of caspases. (johnshopkins.edu)
- Consistent with this idea, Aven inhibited the proteolytic activation of caspases in a cell-free extract and suppressed apoptosis induced by Apaf-1 plus caspase-9. (johnshopkins.edu)
- AI was related to silica exposure, upregulation of mFas, and activation of caspase-3 and -8, as well as influenced by smoking status after adjusting for confounding factors. (cdc.gov)
- Organic solvent-induced proximal tubular cell toxicity via caspase-3 activation. (cdc.gov)
- The increase in apoptosis was associated with activation of caspase-3, caspase-7, and poly (ADP-ribose) polymerase-1 (PARP-1). (cdc.gov)
- A short recovery period of 6h of cells from SWCNT exposure resulted in reversal of caspase-3 and caspase-7, and a partial reversal of PARP-1 activation. (cdc.gov)
- The activation of PARP-1, caspase-3, and caspase-7 was only partially diminished after a recovery of 6h from the exposure to crocidolite. (cdc.gov)
- The results of this study show that the molecular mechanism for raw SWCNT-mediated toxicity in BEAS-2B cells is through the activation of caspase-3, caspase-7, and PARP-1. (cdc.gov)
Protein3
- Caspase-3 is a caspase protein encoded by the CASP3 gene that interacts with caspase-9 and caspase-8. (caspase-3.com)
- At 8-72 hr after ischemia, caspase-3 mRNA and protein were induced in the hippocampus and caudate-putamen (CPu), accompanied by increased caspase-3-like protease activity. (unthsc.edu)
- In the hippocampus, caspase-3 mRNA and protein were predominantly increased in degenerating CA1 pyramidal neurons. (unthsc.edu)
Precursor1
- Detects human Caspase-8 precursor in Western blots and a 42 kDa doublet generated during apoptosis. (rndsystems.com)
Polyclonal antibody1
- 50 ug blocking peptide for Caspase-7 polyclonal antibody (Cat. (biovision.com)
Specificity1
- The 1.63 Å (1 Å = 0.1 nm) structure of the variant demonstrates that the mutation is accommodated at the dimer interface to generate an enzyme with substantially the same activity and specificity as wild-type caspase-3. (ncsu.edu)
Inhibition5
- The results demonstrate that considering allosteric inhibition of caspase 3 as a shift between discrete ‘off-state’ or ‘on-state’ conformations is insufficient. (ncsu.edu)
- In addition to inducing apoptosis, caspase inhibition contributes to necroptosis and/or autophagy depending on the cell type and cellular context. (molcells.org)
- This can be induced by caspase inhibition under certain circumstances. (molcells.org)
- and (4) studied the effect of caspase-3 inhibition on cell survival and DNA fragmentation in the hippocarnpus in a rat model of transient global ischemia. (unthsc.edu)
- On the other hand, caspase 3 inhibition, lessens the PMA induced-effects on the appearance of RBC morphology alterations, although it enhances PMA-mediated effects on nitric oxide (NO) derived metabolites levels. (unicatt.it)
Assay Kit2
- Detect caspase-8 activity with the FLICA Caspase-8 Assay Kit. (immunochemistry.com)
- Bulk Order Inquiry for FAM-FLICA® Caspase-8 Assay Kit ------- (please add any order requirements, including desired quantity, timing, etc. (immunochemistry.com)
Antibody2
- PVDF membrane was probed with 1 µg/mL of Human Caspase-8 Monoclonal Antibody (Catalog # MAB704), followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007 ). (rndsystems.com)
- The peptide is used for blocking the antibody activity of Caspase-7 (Cat. (biovision.com)
Cysteine2
- Caspase-3, cysteine proteinase, expressed in E.Coli. (immunoportal.com)
- Caspase-3 is a newly characterized mammalian cysteine protease that promotes cell death during brain development, in neuronal cultures, and in other cell types under many different conditions. (unthsc.edu)
Pathways1
- and Caspases Pathways. (cdc.gov)
Initiator1
- The caspase-3 zymogen has essentially zero activity until it is cleaved by initiator caspases during apoptosis. (ncsu.edu)
Membrane-bound2
- Modeling indicated that sustained membrane-bound caspase-8 activity is followed by transient cytosolic activity, which can be interpreted as a molecular timer mechanism reflected by a limited lifetime of active caspase-8. (ebi.ac.uk)
- The relationships between apoptosis index (AI) and silica exposure history, soluble Fas (sFas)/membrane-bound Fas (mFas), and caspase-3/caspase-8 were analyzed. (cdc.gov)
Cells3
- To determine how a death ligand stimulus is effectively translated into caspase-8 activity, we assessed this activity over time in single cells with compartmentalized probes that are cleaved by caspase-8 and used multiscale modeling to simultaneously describe single-cell and population data with an ensemble of single-cell models. (ebi.ac.uk)
- Besides, piperine had the ability to cause cell cycle arrest in G2/M phase and to activate caspase-3 and caspase-9 cascades in A549 cells. (nih.gov)
- Monocytes and macrophages are sentinel immune cells in the blood and tissue, respectively, that sense invasive infection to form inflammasomes that activate caspase-1 and gasdermin D (GSDMD) pores, leading to inflammatory death (pyroptosis) and processing and release of IL-1 family cytokines, potent inflammatory mediators. (bvsalud.org)
Induces1
- A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis. (ncsu.edu)
Contributes1
- These data strongly suggest that caspase-3 activity contributes to delayed neuronal death after transient ischemia. (unthsc.edu)
Binds1
- The FLICA reagent FAM-LETD-FMK enters each cell and irreversibly binds to activated caspase-8. (immunochemistry.com)
Fluorescent1
- The remaining green fluorescent signal is a direct measure of the active caspase-8 enzyme activity present in the cell at the time the reagent was added. (immunochemistry.com)
Hippocampus1
- In addition to decreased circadian power and reduced locomotor activity , we found cleaved caspase 1 significantly elevated in the hippocampus of mice exposed to LL. (bvsalud.org)
Significantly1
- AI, mFas, and caspase-3 were significantly higher in lung lavage fluids from silicosis patients than those of observers or healthy volunteers, but the level of sFas demonstrated a decreasing trend. (cdc.gov)
Regulators1
- Ced-4 and Apaf-1 belong to a major class of apoptosis regulators that contain caspase-recruitment (CARD) and nucleotide-binding oligomerization domains. (elsevierpure.com)
Enzyme1
- Conversely, formation of the K242–E246 salt bridge in caspase-3 is needed for an accurate, stable conformation of loop L4 and proper active site formation in the mature enzyme. (ncsu.edu)
Cascade1
- DN caspase-9 (provided courtesy of Emad S. Alnmeri, Thomas Jefferson University, Philadelphia, PA) has been reported to inhibit the caspase cascade ( 5 ). (cdc.gov)
Variants1
- Structural studies of the caspase-3 variants show the involvement of K242 in hydrophobic interactions that stabilize helix 5, near the dimer interface, and the role of E246 appears to be to neutralize the positive charge of K242 within the hydrophobic cluster. (ncsu.edu)
Active3
- Association with another p18/p10 heterodimer generates active caspase-8. (rndsystems.com)
- Interactions between loops 2, 2′ and 4, known as the loop bundle, stabilize the active site of caspase-3. (ncsu.edu)
- Human and some mouse caspases are active in apoptosis and cell death and even in necrosis and inflammation. (caspase-3.com)
Activity2
- Sb-gRAMP physically combines with the caspase-like TPR-CHAT peptidase to form the CRISPR-guided caspase (Craspase) complex, suggesting a potential mechanism of target RNA-induced protease activity to gain viral immunity. (tudelft.nl)
- Stability measurements show that only the K242A single mutant decreases stability of the dimer, whereas both single mutants and the double mutant demonstrate much lower activity compared to wild-type caspase-3. (ncsu.edu)
Inflammation1
- Caspases play important roles in apoptosis and inflammation. (immunochemistry.com)
Human1
- Detection of Human Caspase‑8 by Western Blot. (rndsystems.com)
Long2
- Nod-1 was found to bind to multiple caspases with long prodomains, but specifically activated caspase-9 and promoted caspase- 9-induced apoptosis. (elsevierpure.com)
- Une quantification par cytométrie en flux trois couleurs des cellules CD34+/Annexine+/PI, une analyse FISH, un marquage immunocytochimique des préparations cytospines de la moelle osseuse et des cultures de cellules souches à long terme ont été réalisés. (who.int)
Specific1
- Specific bands were detected for Caspase-8 at approximately 55 and 42 kDa (as indicated). (rndsystems.com)