Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
caspase-2 is an evolutionarily conserved caspase with features of both initiator and executioner caspases
evolution
caspase-2 is the most evolutionarily conserved member in the human caspase family
malfunction
-
Casp2-null animals develop normally, and thymocytes and neurons derived from them seem to undergo similar levels of apoptosis to those from wild-type littermates. Nevertheless, several subtle phenotypes are associated with the Casp2-knockout mice: Casp2-knockout females have a slight increase in the number of oocytes and Casp2/ oocytes show reduced apoptosis in response to treatment with doxorubicin. The neurons derived from Casp2-null mice are resistant to beta-amyloid-mediated death, which suggests a role for caspase 2 in neuronal death. Casp2-deficient mice also show signs of premature ageing, including accumulation of oxidative damage. Mouse embryonic fibroblasts from Casp2-deficient animals show a reduced or delayed apoptotic response to some cytotoxic drugs, have an aberrant DNA damage and cell cycle response and are readily transformed when they are challenged by oncogene expression.
malfunction
-
caspase-2 knockout mice do not develop early spontaneous tumors, but loss of caspase-2 in mice is associated with accelerated tumorigenesis driven by transgenic c-Myc on the mu-enhancer, thus caspase-2-deficient embryonic fibroblasts are more efficiently transformed than wild-type cells. Caspase-2-deficient mice have features consistent with accelerated ageing, phenotype, overview
malfunction
-
decreased caspase-2 and RAIDD expression is observed in mantle cell lymphoma tumor samples. In addition, drug resistance in childhood forms of acute lymphoblastic leukemia is correlated with decreased levels of caspase-2. In contrast, increased levels of caspase-2 in acute myelogenous leukemia and adult ALL are associated with decreased patient survival. Possibly inactivation of caspase-2 in tumors occurs through disruption of the pathway through mutation or improper regulation of a protein that regulates caspase-2 activity
malfunction
-
depletion of caspase-2 prevents p21 expression and thereby reverts the gamma-IR-induced senescent phenotype of wild-type HCT116 colon carcinoma cells into apoptosis, knockdown of none of the caspase-2-interacting components RAIDD, RIP or DNA-PKcs is able to mimic these processes, but knockdown of caspase-2 specifically impairs DNA damage-induced p21 expression, and silencing of caspase-2 impairs exogenous expression of p21 constructs containing 3'-UTR sequences, whereas overexpression of a caspase-2 mutant increases p21 levels. Silencing of caspase-2 impairs exogenous expression of p21 constructs containing 3'-UTR sequences
malfunction
cells lacking caspase-2 are protected from cell death induced by Staphylococcus aureus alpha-toxin
malfunction
down-regulation or inactivation of caspase-2 blocks amyloid beta-mediated effects on primary hippocampal cultures
malfunction
down-regulation or inactivation of caspase-2 blocks amyloid beta-mediated effects on primary hippocampal cultures
malfunction
maturation, activation, and cytokine secretion are significantly impaired in Caspase-2 knockout cells infected with Brucella abortus strain RB51 or Salmonella typhimurium strain SL1344
malfunction
the loss of caspase-2 in mice results in an osteopenic phenotype associated with increased numbers of osteoclasts in vivo. Mitochondrial reactive oxygen species are significantly increased in caspase-deficient precursors after receptor activator of nuclear factor kappa-B ligand administration
malfunction
both pharmacological inhibition and shRNA-mediated knockdown of caspase-2 suppresses myogenic differentiation and dramatically impaired myotube formation
malfunction
caspase-2 deficiency leads to increased cellular stress largely because these mice fail to respond to oxidative stress by upregulating their antioxidant defense mechanism
malfunction
decreasing the levels of caspase-2 restores long-term memory in mice that have existing deficits
malfunction
loss of caspase-2 leads to an acceleration of tumor onset in the Emü-Myc mouse lymphoma model
malfunction
loss of caspase-2 leads to enhanced tumor proliferation and progression
metabolism
caspase-2 is a critical mediator in the activation of the RhoA/ROCK-II signaling pathway, leading to the collapse of dendritic spines. Inactive RhoA-GDP but not active RhoA-GTP forms a complex with caspase-2
metabolism
caspase-2 is a critical mediator in the activation of the RhoA/ROCK-II signaling pathway, leading to the collapse of dendritic spines. Inactive RhoA-GDP but not active RhoA-GTP forms a complex with caspase-2
metabolism
caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines. The truncation product, DELTAtau314, resists fibrillation and is present at higher levels in brains from cognitively impaired mice and humans with Alzheimer's disease
metabolism
caspase-2 cleavage of tau at Asp314 impairs cognitive and synaptic function in animal and cellular models of tauopathies by promoting the missorting of tau to dendritic spines. The truncation product, DETAtau314, resists fibrillation and is present at higher levels in brains from cognitively impaired mice and humans with Alzheimer's disease
physiological function
apoptosis induced by doxorubicin and 5-fluorouracil is caspase-2-dependent
physiological function
-
caspase 2 is thought be a downstream caspase
physiological function
-
caspase 2 represses transcription of the survivin gene, a general regulator of cell division and cytoprotection in tumors. This pathway involves caspase 2 proteolytic cleavage of the nuclearfactor kappaB (NFkappaB) activator, RIP1. Loss of RIP1 abolishes transcription of NFkappaB target genes, including survivin, resulting in deregulated mitotic transitions, enhanced apoptosis and suppression of tumorigenicityin vivo. Caspase 2 functions as an endogenous inhibitor of NFkappaB-dependent cell survival.
physiological function
-
caspase-2 activation is commonly associated with induction of IFN-beta-induced apoptosis in IFN-beta-sensitive melanoma cells
physiological function
-
caspases-2 and -8 are involved in the presenilin1/gamma-secretase-dependent cleavage of amyloid precursor protein after the induction of apoptosis
physiological function
-
critical role of caspase-2 in mediating rough Brucella abortus induced macrophage cell death
physiological function
-
discussion of the role of caspase-2 and potential contribution of the enzyme to the pathology of human diseases
physiological function
-
overview on the function of caspase-2 in cell death signaling
physiological function
-
The increased expression of PIDD (p53-induced protein with a death domain) induced by p53 forms a complex with RAIDD and caspase-2 (termed a PIDDosome), which activates the protease. The processed caspase-2 acts as a canonical caspase in the mitochondrial-mediated pathway triggering cytochrome c release. Once released to the cytoplasm, cytochrome c binds to APAF-1 to form a wheel-like complex, the apoptosome, resulting in the activation of caspase-9 and subsequent cleavage of downstream caspases including caspase-3.
physiological function
-
caspase-2 is commonly required for DNA damage-induced p21 expression. Caspase-2 regulates p21 expression at the translational level, independently of its enzymatic activity but also not requiring known caspase-2-activating platforms
physiological function
caspase-2 plays important roles in stress-induced apoptosis, cell cycle regulation, and tumor suppression
physiological function
-
role of caspase-2 in apoptosis, and caspase-2 may act as a tumor suppressor, mechanisms through which caspase-2 signals, e.g. involving PIDD, also known as LRDD or leucine-rich repeat and death domain-containing protein, caspase-2 pathways to apoptosis and cell cycle arrest, detailed overview. PIDD activation and more importantly caspase-2 activation is not always synonymous with induction of apoptosis, a threshold of caspase-2 activation must be reached before caspase-2-dependent apoptosis is engaged. Cleavage of Mdm2 is not the sole way caspase-2 can induce growth arrest
physiological function
-
role of caspase-2 in apoptosis, and caspase-2 may act as a tumor suppressor, mechanisms through which caspase-2 signals, e.g. involving PIDD, also known as LRDD or leucine-rich repeat and death domain-containing protein, caspase-2 pathways to apoptosis and cell cycle arrest, detailed overview. PIDD activation and more importantly caspase-2 activation is not always synonymous with induction of apoptosis, a threshold of caspase-2 activation must be reached before caspase-2-dependent apoptosis is engaged. Cleavage of Mdm2 is not the sole way caspase-2 can induce growth arrest
physiological function
-
upon DNA damage, p53 induction of the Caspase-2-PIDDosome creates a positive feedback loop that inhibits Mdm2, a key negative regulator of p53, and reinforces p53 stability and activity, contributing to cell survival and drug resistance, mechanism of Mdm2 inhibition that impacts p53 dynamics upon genotoxic stress, overview
physiological function
Brucella abortus strain RB51- and S2308-induced BMDC cell death is regulated by caspase-2. The enzyme is required for naive T-lymphocyte proliferation following stimulation with RB51-infected bone marrow-derived dendritic cells
physiological function
caspase-2 is implicated in the regulation of cell death that is induced by metabolic imbalance, DNA damage, endoplasmic reticulum (ER) stress, mitotic catastrophe and others. Caspase-2 is implicated in the induction of cell death by pathogenic bacteria, such as Brucella, Staphylococcus aureus and Salmonella. Caspase-2 is controlling aging and cell death in response to DNA damage. The enzyme is also linked to cell death that is induced by aberrant mitosis in cancer cells that transiently arrest in prometaphase after cell fusion. Caspase 2 is crucial for oocyte apoptosis
physiological function
caspase-2 is involved in apoptosis, nuclear factor-kappaB regulation, and tumor suppression. Caspase-2 catalytic site Cys-320 and Ser-139 residues are required for caspase-2 to suppress tumorigenesis in nude mice
physiological function
caspase-2 modulates osteoclastogenesis through down-regulating oxidative stress
physiological function
caspase-2 plays a critical role in mediating the synaptic changes and memory alteration induced by amyloid beta in Alzheimer's disease
physiological function
caspase-2 plays a critical role in mediating the synaptic changes and memory alteration induced by amyloid beta in Alzheimer's disease
physiological function
-
caspase-2 plays a role in lipoapoptosis and is required for cell death
physiological function
in epithelial cells, caspase-2 is activated as an initiator caspase in a PIDDosome-independent manner to regulate pore-forming toxin-mediated cell death
physiological function
the enzyme is essential for c-Jun transcriptional activation and Bim induction in in neurons subjected to apoptotic stimuli
physiological function
the enzyme is implicated in tumor suppression and plays a role in regulating the cellular response towards oxidative stress. Key cellular processes such as proliferation, aging, maintenance of genome surveillance and the redox system are affected by caspase-2 function
physiological function
the long isoform, casp-2L, promotes apoptosis, whereas the short isoform, casp-2S, inhibits apoptosis. Isoform casp-2S is responsible for inhibiting DNA damage-induced cytoplasmic fodrin cleavage independent of cellular p53 status, and prevents cisplatin-induced membrane blebbing thereby affecting cellular apoptosis
physiological function
caspase-2 acts as a tumor suppressor. Loss of caspase-2 leads to an acceleration of tumor onset in the EMy-Myc mouse lymphoma model
physiological function
caspase-2 functions as a tumor suppressor in Kras-driven lung cancer in vivo. Caspase-2 cleaves and inhibits Mdm2 and thereby promotes the stability of the tumor-suppressor p53
physiological function
caspase-2 is required for skeletal muscle differentiation and myogenesis. The role of caspase-2 is to regulate p21 induction at the onset of differentiation, which may regulate the myogenic program
physiological function
the enzyme is essential for mitochondrial oxidative stress-induced apoptosis
physiological function
the enzyme is involved in tumor suppression
physiological function
the enzyme may be involved in invertebrate immune response, especially in eliminating and degrading invading pathogens
physiological function
the enzyme mediates site-specific retinal ganglion cell death after blunt ocular injury
physiological function
the enzyme protects against oxidative stress in vivo
additional information
caspase-2 is synthesized as an inactive zymogen. The zymogen sequence includes a long prodomain containing a CARD followed by a large domain, a linker, and a small domain. Caspase-2 undergoes autocatalytic activation to remove the prodomain and linker region to generate a stable dimer consisting of the large subunit p19 and the small subunit p12. This p19/p12 dimer self-associates to form the active caspase-2
additional information
-
caspase-2 is synthesized as an inactive zymogen. The zymogen sequence includes a long prodomain containing a CARD followed by a large domain, a linker, and a small domain. Caspase-2 undergoes autocatalytic activation to remove the prodomain and linker region to generate a stable dimer consisting of the large subunit p19 and the small subunit p12. This p19/p12 dimer self-associates to form the active caspase-2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Garcia-Calvo, M.; Peterson, E.P.; Leiting, B.; Ruel, R.; Nicholson, D.W.; Thornberry, N.A.
Inhibition of human caspases by peptide-based and macromolecular inhibitors
J. Biol. Chem.
273
32608-32613
1998
Homo sapiens
brenda
Garcia-Calvo, M.; Peterson, E.P.; Rasper, D.M.; Vaillancourt, J.P.; Zamboni, R.; Nicholson, D.W.; Thornberry, N.A.
Purification and catalytic properties of human caspase family members
Cell Death Differ.
6
362-369
1999
Homo sapiens
brenda
Chang, H.Y.; Yang, X.
Proteases from cell suicide: functions and regulation of caspases
Microbiol. Mol. Biol. Rev.
64
821-846
2000
Homo sapiens, Mus musculus
brenda
Thornberry, N.A.; Rano, T.A.; Peterson, E.P.; et al.
A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
J. Biol. Chem.
272
17907-17911
1997
Homo sapiens
brenda
van de Craen, M.; Vandenabeele, P.; Declercq, W.; van den Brande, I.; van Loo, G.; Molemans, F.; Schotte, P.; van Criekinge, W.; Beyaert, R.; Fiers, W.
Characterization of seven murine caspase family members
FEBS Lett.
403
61-69
1997
Mus musculus (P29594), Mus musculus C3H/An (P29594)
brenda
Talanian, R.V.; Quinlan, C.; Trautz, S.; Hackett, M.C.; Mankovich, J.A.; Banach, D.; Ghayur, T.; Brady, K.D.; Wong, W.W.
Substrate specificities of caspase family proteases
J. Biol. Chem.
272
9677-9682
1997
Homo sapiens
brenda
Flaws, J.A.; Kugu, K.; Trbovich, A.M.; Desanti, A.; Tilly, K.I.; Hirshfield, A.N.; Tilly, J.L.
Interleukin-1 beta-converting enzyme-related proteases (IRPs) and mammalian cell death: dissociation of IRP-induced oligonucleosomal endonuclease activity from morphological apoptosis in granulosa cells of the ovarian follicle
Endocrinology
136
5042-5053
1995
Rattus norvegicus (P55215)
brenda
Wang, L.; Miura M.; Bergeron, L.; Zhu, H.; Yuan, J.
Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
Cell
78
739-750
1994
Homo sapiens (P42575)
brenda
Xue, D.; Shaham, S.; Horvitz, H.R.
The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease
Genes Dev.
10
1073-1083
1996
Homo sapiens (P42575)
brenda
Kumar, S.; Kinoshita, M.; Noda, M.; Copeland, N.G.; Jenkins, N.A.
Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme
Genes Dev.
8
1613-1626
1994
Mus musculus (P29594), Mus musculus BALB/c (P29594)
brenda
Kumar, S.; Tomooka, Y.; Noda, M.
Identification of a set of genes with developmentally down-regulated expression in the mouse brain
Biochem. Biophys. Res. Commun.
185
1155-1161
1992
Mus musculus (P29594)
brenda
Kaushal, G.P.; Singh, A.B.; Shah, S.V.
Identification of gene family of caspases in rat kidney and altered expression in ischemia-reperfusion injury
Am. J. Physiol.
274
F587-F595
1998
Rattus norvegicus (P55215)
brenda
Johnson, A.L.; Bridgham, J.T.; Bergeron, L.; Yuan, J.
Characterization of the avian Ich-1 cDNA and expression of Ich-1L mRNA in the hen ovary
Gene
192
227-233
1997
Gallus gallus (Q98943), Gallus gallus
brenda
Mancini, M.; Machamer, C.E.; Roy, S.; Nicholson, D.W.; Thornberry, N.A.; Casciola-Rosen, L.A.; Rosen, A.
Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis
J. Cell. Biol.
149
603-612
2000
Homo sapiens
brenda
Colussi, P.A.; Harvey, N.L.; Shearwin-Whyatt, L.M.; Kumar, S.
Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain
J. Biol. Chem.
273
26566-26570
1998
Mus musculus
brenda
Baliga, B.C.; Colussi, P.A.; Read, S.H.; Dias, M.M.; Jans, D.A.; Kumar, S.
Role of prodomain in importin-mediated nuclear localization and activation of caspase-2
J. Biol. Chem.
278
4899-4905
2003
Mus musculus
brenda
Li, H.; Bergeron, L.; Cryns, V.; Pasternack, M.S.; Zhu, H.; Shi, L.; Greenberg, A.; Yuan, J.
Activation of caspase-2 in apoptosis
J. Biol. Chem.
272
21010-21017
1997
Homo sapiens
brenda
Zhivotovsky, B.; Orrenius, S.
Caspase-2 function in response to DNA damage
Biochem. Biophys. Res. Commun.
331
859-867
2005
Homo sapiens (P42575)
brenda
Zheng, S.; Turner, T.T.; Lysiak, J.J.
Caspase 2 activity contributes to the initial wave of germ cell apoptosis during the first round of spermatogenesis
Biol. Reprod.
74
1026-1033
2006
Mus musculus (P29594), Mus musculus, Mus musculus C57BL/6 (P29594)
brenda
Tyagi, A.; Singh, R.P.; Agarwal, C.; Agarwal, R.
Silibinin activates p53-caspase-2 pathway and causes caspase-mediated cleavage of Cip1/p21 in apoptosis induction in bladder transitional-cell papilloma RT4 cells: evidence for a regulatory loop between p53 and caspase-2
Carcinogenesis
27
2269-2280
2006
Homo sapiens (P42575), Homo sapiens
brenda
Kong, J.Y.; Rabkin, S.W.
Cytoskeletal actin degradation induced by lovastatin in cardiomyocytes is mediated through caspase-2
Cell Biol. Int.
28
781-790
2004
Gallus gallus (Q98943)
brenda
Shin, S.; Lee, Y.; Kim, W.; Ko, H.; Choi, H.; Kim, K.
Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8
EMBO J.
24
3532-3542
2005
Homo sapiens (P42575)
brenda
Cheung, H.H.; Lynn Kelly, N.; Liston, P.; Korneluk, R.G.
Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: a role for the IAPs
Exp. Cell Res.
312
2347-2357
2006
Homo sapiens (P42575)
brenda
Ho, P.K.; Jabbour, A.M.; Ekert, P.G.; Hawkins, C.J.
Caspase-2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase-7
FEBS J.
272
1401-1414
2005
Homo sapiens (P42575), Homo sapiens
brenda
Cristobal, J.; Stockert, J.C.; Villanueva, A.; Rello-Varona, S.; Juarranz, A.; Canete, M.
Caspase-2: a possible trigger of apoptosis induced in A-549 tumor cells by ZnPc photodynamic treatment
Int. J. Oncol.
28
1057-1063
2006
Homo sapiens (P42575)
brenda
Wagner, K.W.; Engels, I.H.; Deveraux, Q.L.
Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway
J. Biol. Chem.
279
35047-35052
2004
Homo sapiens (P42575)
brenda
Enoksson, M.; Robertson, J.D.; Gogvadze, V.; Bu, P.; Kropotov, A.; Zhivotovsky, B.; Orrenius, S.
Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids
J. Biol. Chem.
279
49575-49578
2004
Homo sapiens (P42575)
brenda
Iwanaga, N.; Kamachi, M.; Aratake, K.; Izumi, Y.; Ida, H.; Tanaka, F.; Tamai, M.; Arima, K.; Nakamura, H.; Origuchi, T.; Kawakami, A.; Eguchi, K.
Regulation of alternative splicing of caspase-2 through an intracellular signaling pathway in response to pro-apoptotic stimuli
J. Lab. Clin. Med.
145
105-110
2005
Homo sapiens (P42575)
brenda
Bonzon, C.; Bouchier-Hayes, L.; Pagliari, L.J.; Green, D.R.; Newmeyer, D.D.
Caspase-2-induced apoptosis requires bid cleavage: a physiological role for bid in heat shock-induced death
Mol. Biol. Cell
17
2150-2157
2006
Mus musculus (P29594), Mus musculus, Xenopus laevis (Q9IB67)
brenda
Logette, E.; Le Jossic-Corcos, C.; Masson, D.; Solier, S.; Sequeira-Legrand, A.; Dugail, I.; Lemaire-Ewing, S.; Desoche, L.; Solary, E.; Corcos, L.
Caspase-2, a novel lipid sensor under the control of sterol regulatory element binding protein 2
Mol. Cell. Biol.
25
9621-9631
2005
Homo sapiens (P42575), Homo sapiens
brenda
Tu, S.; McStay, G.P.; Boucher, L.M.; Mak, T.; Beere, H.M.; Green, D.R.
In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
Nat. Cell Biol.
8
72-77
2006
Mus musculus (P29594)
brenda
Filomenko, R.; Prvotat, L.; Rb, C.; Cortier, M.; Jeannin, J.F.; Solary, E.; Bettaieb, A.
Caspase-10 involvement in cytotoxic drug-induced apoptosis of tumor cells
Oncogene
2006
1-11
2006
Homo sapiens (P42575)
-
brenda
Peluffo, M.C.; Bussmann, L.; Stouffer, R.L.; Tesone, M.
Expression of caspase-2, -3, -8 and -9 proteins and enzyme activity in the corpus luteum of the rat at different stages during the natural estrous cycle
Reproduction
132
465-475
2006
Rattus norvegicus (P55215)
brenda
Lysiak, J.J.; Zheng, S.; Woodson, R.; Turner, T.T.
Caspase-9-dependent pathway to murine germ cell apoptosis: mediation by oxidative stress, BAX, and caspase 2
Cell Tissue Res.
328
411-419
2007
Mus musculus
brenda
VanOosten, R.L.; Earel, J.K.; Griffith, T.S.
Histone deacetylase inhibitors enhance Ad5-TRAIL killing of TRAIL-resistant prostate tumor cells through increased caspase-2 activity
Apoptosis
12
561-571
2007
Homo sapiens
brenda
Sapet, C.; Simoncini, S.; Loriod, B.; Puthier, D.; Sampol, J.; Nguyen, C.; Dignat-George, F.; Anfosso, F.
Thrombin-induced endothelial microparticle generation: identification of a novel pathway involving ROCK-II activation by caspase-2
Blood
108
1868-1876
2006
Homo sapiens
brenda
Taghiyev, A.F.; Guseva, N.V.; Glover, R.A.; Rokhlin, O.W.; Cohen, M.B.
TSA-induced cell death in prostate cancer cell lines is caspase-2 dependent and involves the PIDDosome
Cancer Biol. Ther.
5
1199-1205
2006
Homo sapiens
brenda
Jangi, S.M.; Diaz-Perez, J.L.; Ochoa-Lizarralde, B.; Martin-Ruiz, I.; Asumendi, A.; Perez-Yarza, G.; Gardeazabal, J.; Diaz-Ramon, J.L.; Boyano, M.D.
H1 histamine receptor antagonists induce genotoxic and caspase-2-dependent apoptosis in human melanoma cells
Carcinogenesis
27
1787-1796
2006
Homo sapiens
brenda
Hanoux, V.; Pairault, C.; Bakalska, M.; Habert, R.; Livera, G.
Caspase-2 involvement during ionizing radiation-induced oocyte death in the mouse ovary
Cell Death Differ.
14
671-681
2007
Mus musculus
brenda
Yeung, B.H.; Huang, D.C.; Sinicrope, F.A.
PS-341 (bortezomib) induces lysosomal cathepsin B release and a caspase-2-dependent mitochondrial permeabilization and apoptosis in human pancreatic cancer cells
J. Biol. Chem.
281
11923-11932
2006
Homo sapiens
brenda
Mohan, J.; Gandhi, A.A.; Bhavya, B.C.; Rashmi, R.; Karunagaran, D.; Indu, R.; Santhoshkumar, T.R.
Caspase-2 triggers Bax-Bak-dependent and -independent cell death in colon cancer cells treated with resveratrol
J. Biol. Chem.
281
17599-17611
2006
Homo sapiens, Mus musculus
brenda
Cao, X.; Bennett, R.L.; May, W.S.
c-Myc and caspase-2 are involved in activating Bax during cytotoxic drug-induced apoptosis
J. Biol. Chem.
283
14490-14496
2008
Homo sapiens
brenda
Upton, J.P.; Austgen, K.; Nishino, M.; Coakley, K.M.; Hagen, A.; Han, D.; Papa, F.R.; Oakes, S.A.
Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress
Mol. Cell. Biol.
28
3943-3951
2008
Mus musculus
brenda
Ho, L.H.; Read, S.H.; Dorstyn, L.; Lambrusco, L.; Kumar, S.
Caspase-2 is required for cell death induced by cytoskeletal disruption
Oncogene
27
3393-3404
2008
Mus musculus
brenda
Baptiste-Okoh, N.; Barsotti, A.M.; Prives, C.
A role for caspase 2 and PIDD in the process of p53-mediated apoptosis
Proc. Natl. Acad. Sci. USA
105
1937-1942
2008
Homo sapiens
brenda
Karki, P.; Dahal, G.R.; Shin, S.Y.; Lee, J.S.; Cho, B.; Park, I.S.
Efficient cleavage of Bid and procaspase-7 by caspase-2 at lower pH
Protein Pept. Lett.
15
1044-1049
2008
Homo sapiens
brenda
Chae, S.S.; Yoo, C.B.; Jo, C.; Yun, S.M.; Jo, S.A.; Koh, Y.H.
Caspases-2 and -8 are involved in the presenilin1/gamma-secretase-dependent cleavage of amyloid precursor protein after the induction of apoptosis
J. Neurosci. Res.
88
1926-1933
2010
Homo sapiens
brenda
Chan, K.M.; Rajab, N.F.; Siegel, D.; Din, L.B.; Ross, D.; Inayat-Hussain, S.H.
Goniothalamin induces coronary artery smooth muscle cells apoptosis: the p53-dependent caspase-2 activation pathway
Toxicol. Sci.
116
533-548
2010
Homo sapiens
brenda
Kitevska, T.; Spencer, D.M.; Hawkins, C.J.
Caspase-2: controversial killer or checkpoint controller?
Apoptosis
14
829-848
2009
Homo sapiens (P42575)
brenda
Lee, J.C.; Su, C.L.; Chen, L.L.; Won, S.J.
Formosanin C-induced apoptosis requires activation of caspase-2 and change of mitochondrial membrane potential
Cancer Sci.
100
503-513
2009
Homo sapiens
brenda
Krumschnabel, G.; Sohm, B.; Bock, F.; Manzl, C.; Villunger, A.
The enigma of caspase-2: The laymens view
Cell Death Differ.
16
195-207
2009
Homo sapiens, Mus musculus
brenda
Shi, M.; Vivian, C.J.; Lee, K.J.; Ge, C.; Morotomi-Yano, K.; Manzl, C.; Bock, F.; Sato, S.; Tomomori-Sato, C.; Zhu, R.; Haug, J.S.; Swanson, S.K.; Washburn, M.P.; Chen, D.J.; Chen, B.P.; Villunger, A.; Florens, L.; Du, C.
DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance
Cell
136
508-520
2009
Homo sapiens, Mus musculus
brenda
Nutt, L.K.; Buchakjian, M.R.; Gan, E.; Darbandi, R.; Yoon, S.Y.; Wu, J.Q.; Miyamoto, Y.J.; Gibbons, J.A.; Gibbon, J.A.; Andersen, J.L.; Freel, C.D.; Tang, W.; He, C.; Kurokawa, M.; Wang, Y.; Margolis, S.S.; Fissore, R.A.; Kornbluth, S.
Metabolic control of oocyte apoptosis mediated by 14-3-3zeta-regulated dephosphorylation of caspase-2
Dev. Cell
16
856-866
2009
Xenopus laevis
brenda
Narine, K.A.; Keuling, A.M.; Gombos, R.; Tron, V.A.; Andrew, S.E.; Young, L.C.
Defining the DNA mismatch repair-dependent apoptotic pathway in primary cells: evidence for p53-independence and involvement of centrosomal caspase 2
DNA Repair
9
161-168
2010
Mus musculus
brenda
Andersen, J.L.; Johnson, C.E.; Freel, C.D.; Parrish, A.B.; Day, J.L.; Buchakjian, M.R.; Nutt, L.K.; Thompson, J.W.; Moseley, M.A.; Kornbluth, S.
Restraint of apoptosis during mitosis through interdomain phosphorylation of caspase-2
EMBO J.
28
3216-3227
2009
Homo sapiens, Xenopus laevis
brenda
Manzl, C.; Krumschnabel, G.; Bock, F.; Sohm, B.; Labi, V.; Baumgartner, F.; Logette, E.; Tschopp, J.; Villunger, A.
Caspase-2 activation in the absence of PIDDosome formation
J. Cell Biol.
185
291-303
2009
Mus musculus
brenda
Bouchier-Hayes, L.
The role of caspase-2 in stress-induced apoptosis
J. Cell. Mol. Med.
14
1212-1224
2010
Homo sapiens, Mus musculus
brenda
Kamiya, T.; Okabayashi, T.; Yokota, S.; Kan, Y.; Ogino, J.; Yamashita, T.; Fujii, N.; Jimbow, K.
Increased caspase-2 activity is associated with induction of apoptosis in IFN-beta sensitive melanoma cell lines
J. Interferon Cytokine Res.
30
349-357
2010
Homo sapiens
brenda
Bouchier-Hayes, L.; Oberst, A.; McStay, G.P.; Connell, S.; Tait, S.W.; Dillon, C.P.; Flanagan, J.M.; Beere, H.M.; Green, D.R.
Characterization of cytoplasmic caspase-2 activation by induced proximity
Mol. Cell
35
830-840
2009
Homo sapiens
brenda
Kumar, S.
Caspase 2 in apoptosis, the DNA damage response and tumour suppression: enigma no more?
Nat. Rev. Cancer
9
897-903
2009
Mus musculus
brenda
Olsson, M.; Vakifahmetoglu, H.; Abruzzo, P.M.; Hoegstrand, K.; Grandien, A.; Zhivotovsky, B.
DISC-mediated activation of caspase-2 in DNA damage-induced apoptosis
Oncogene
28
1949-1959
2009
Homo sapiens
brenda
Krumschnabel, G.; Manzl, C.; Villunger, A.
Caspase-2: killer, savior and safeguard-emerging versatile roles for an ill-defined caspase
Oncogene
28
3093-3096
2009
Mus musculus
brenda
Guha, M.; Xia, F.; Raskett, C.M.; Altieri, D.C.
Caspase 2-mediated tumor suppression involves survivin gene silencing
Oncogene
29
1280-1292
2010
Homo sapiens
brenda
Chen, F.; He, Y.
Caspase-2 mediated apoptotic and necrotic murine macrophage cell death induced by rough Brucella abortus
PLoS ONE
4
e6830
2009
Mus musculus
brenda
Inayat-Hussain, S.H.; Chan, K.M.; Rajab, N.F.; Din, L.B.; Chow, S.C.; Kizilors, A.; Farzaneh, F.; Williams, G.T.
Goniothalamin-induced oxidative stress, DNA damage and apoptosis via caspase-2 independent and Bcl-2 independent pathways in Jurkat T-cells
Toxicol. Lett.
193
108-114
2010
Homo sapiens
brenda
Vakifahmetoglu-Norberg, H.; Zhivotovsky, B.
The unpredictable caspase-2: what can it do?
Trends Cell Biol.
20
150-159
2010
Mus musculus
brenda
Sohn, D.; Budach, W.; Jaenicke, R.U.
Caspase-2 is required for DNA damage-induced expression of the CDK inhibitor p21(WAF1/CIP1)
Cell Death Differ.
18
1664-1674
2011
Homo sapiens
brenda
Bouchier-Hayes, L.; Green, D.R.
Caspase-2: the orphan caspase
Cell Death Differ.
19
51-57
2012
Homo sapiens, Mus musculus
brenda
Tang, Y.; Wells, J.A.; Arkin, M.R.
Structural and enzymatic insights into caspase-2 protein substrate recognition and catalysis
J. Biol. Chem.
286
34147-34154
2011
Homo sapiens (P42575), Homo sapiens
brenda
Oliver, T.G.; Meylan, E.; Chang, G.P.; Xue, W.; Burke, J.R.; Humpton, T.J.; Hubbard, D.; Bhutkar, A.; Jacks, T.
Caspase-2-mediated cleavage of Mdm2 creates a p53-induced positive feedback loop
Mol. Cell
43
57-71
2011
Homo sapiens
brenda
Jean, Y.Y.; Ribe, E.M.; Pero, M.E.; Moskalenko, M.; Iqbal, Z.; Marks, L.J.; Greene, L.A.; Troy, C.M.
Caspase-2 is essential for c-Jun transcriptional activation and Bim induction in neuron death
Biochem. J.
455
15-25
2013
Rattus norvegicus (P55215)
brenda
Callaway, D.A.; Riquelme, M.A.; Sharma, R.; Lopez-Cruzan, M.; Herman, B.A.; Jiang, J.X.
Caspase-2 modulates osteoclastogenesis through down-regulating oxidative stress
Bone
76
40-48
2015
Mus musculus (P29594)
brenda
Imre, G.; Rajalingam, K.
Role for caspase-2 during pore-forming toxin-mediated apoptosis
Cell Cycle
11
3709-3710
2012
Mus musculus (P29594)
brenda
Vakifahmetoglu-Norberg, H.; Norberg, E.; Perdomo, A.B.; Olsson, M.; Ciccosanti, F.; Orrenius, S.; Fimia, G.M.; Piacentini, M.; Zhivotovsky, B.
Caspase-2 promotes cytoskeleton protein degradation during apoptotic cell death
Cell Death Dis.
4
e940
2013
Homo sapiens (P42575)
brenda
Ren, K.; Lu, J.; Porollo, A.; Du, C.
Tumor-suppressing function of caspase-2 requires catalytic site Cys-320 and site Ser-139 in mice
J. Biol. Chem.
287
14792-14802
2012
Mus musculus (P29594), Mus musculus
brenda
Wejda, M.; Impens, F.; Takahashi, N.; Van Damme, P.; Gevaert, K.; Vandenabeele, P.
Degradomics reveals that cleavage specificity profiles of caspase-2 and effector caspases are alike
J. Biol. Chem.
287
33983-33995
2012
Homo sapiens (P42575), Homo sapiens
brenda
Johnson, E.S.; Lindblom, K.R.; Robeson, A.; Stevens, R.D.; Ilkayeva, O.R.; Newgard, C.B.; Kornbluth, S.; Andersen, J.L.
Metabolomic profiling reveals a role for caspase-2 in lipoapoptosis
J. Biol. Chem.
288
14463-14475
2013
Xenopus laevis
brenda
Fava, L.; Bock, F.; Geley, S.; Villunger, A.
Caspase-2 at a glance
J. Cell Sci.
125
5911-5915
2012
Mus musculus (P29594)
brenda
Pozueta, J.; Lefort, R.; Ribe, E.M.; Troy, C.M.; Arancio, O.; Shelanski, M.
Caspase-2 is required for dendritic spine and behavioural alterations in J20 APP transgenic mice
Nat. Commun.
4
1939
2013
Mus musculus (P29594), Mus musculus, Rattus norvegicus (P55215)
brenda
Olsson, M.; Forsberg, J.; Zhivotovsky, B.
Caspase-2: the reinvented enzyme
Oncogene
34
1877-1882
2015
Mus musculus (P29594), Mus musculus
brenda
Li, X.; He, Y.
Caspase-2-dependent dendritic cell death, maturation, and priming of T cells in response to Brucella abortus infection
PLoS ONE
7
e43512
2012
Mus musculus (P29594)
brenda
Han, C.; Zhao, R.; Kroger, J.; Qu, M.; Wani, A.A.; Wang, Q.E.
Caspase-2 short isoform interacts with membrane-associated cytoskeleton proteins to inhibit apoptosis
PLoS ONE
8
e67033
2013
Homo sapiens (P42575)
brenda
Boonstra, K.; Bloemberg, D.; Quadrilatero, J.
Caspase-2 is required for skeletal muscle differentiation and myogenesis
Biochim. Biophys. Acta Mol. Cell Res.
1865
95-104
2018
Mus musculus (P29594)
brenda
Lim, J.; Kim, H.K.; Kim, S.H.; Rhee, K.J.; Kim, Y.S.
Caspase-2 mediates triglyceride (TG)-induced macrophage cell death
BMB Rep.
50
510-515
2017
Mus musculus (P29594)
brenda
Peintner, L.; Dorstyn, L.; Kumar, S.; Aneichyk, T.; Villunger, A.; Manzl, C.
The tumor-modulatory effects of caspase-2 and Pidd1 do not require the scaffold protein Raidd
Cell Death Differ.
22
1803-1811
2015
Mus musculus (P29594), Mus musculus
brenda
Terry, M.; Arya, R.; Mukhopadhyay, A.; Berrett, K.; Clair, P.; Witt, B.; Salama, M.; Bhutkar, A.; Oliver, T.
Caspase-2 impacts lung tumorigenesis and chemotherapy response in vivo
Cell Death Differ.
22
719-730
2015
Homo sapiens (P42575), Homo sapiens
brenda
Lopez-Cruzan, M.; Sharma, R.; Tiwari, M.; Karbach, S.; Holstein, D.; Martin, C.R.; Lechleiter, J.D.; Herman, B.
Caspase-2 resides in the mitochondria and mediates apoptosis directly from the mitochondrial compartment
Cell Death Dis.
2
16005
2016
Mus musculus (P29594)
brenda
Ye, S.; Gao, Y.; Wang, S.; Li, Q.; Li, R.; Li, H.
Characterization and expression analysis of a caspase-2 in an invertebrate echinoderm sea cumber Apostichopus japonicus
Fish Shellfish Immunol.
48
266-272
2016
Apostichopus japonicus (A0A139YJB0), Apostichopus japonicus
brenda
Thomas, C.N.; Thompson, A.M.; McCance, E.; Berry, M.; Logan, A.; Blanch, R.J.; Ahmed, Z.
Caspase-2 mediates site-specific retinal ganglion cell death after blunt ocular injury
Invest. Ophthalmol. Vis. Sci.
59
4453-4462
2018
Rattus norvegicus (P55215)
brenda
Zhao, X.; Kotilinek, L.A.; Smith, B.; Hlynialuk, C.; Zahs, K.; Ramsden, M.; Cleary, J.; Ashe, K.H.
Caspase-2 cleavage of tau reversibly impairs memory
Nat. Med.
22
1268-1276
2016
Mus musculus (P29594), Homo sapiens (P42575), Homo sapiens
brenda
Shalini, S.; Puccini, J.; Wilson, C.; Finnie, J.; Dorstyn, L.; Kumar, S.
Caspase-2 protects against oxidative stress in vivo
Oncogene
34
4995-5002
2015
Mus musculus (P29594)
brenda