Search results for apoptosis

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Results (30 results from a total of 746)

Identifier: R-HSA-109581
Species: Homo sapiens
Apoptosis is a distinct form of cell death that is functionally and morphologically different from necrosis. Nuclear chromatin condensation, cytoplasmic shrinking, dilated endoplasmic reticulum, and membrane blebbing characterize apoptosis in general. Mitochondria remain morphologically unchanged. In 1972 Kerr et al introduced the concept of apoptosis as a distinct form of "cell-death", and the mechanisms of various apoptotic pathways are still being revealed today.
The two principal pathways of apoptosis are (1) the Bcl-2 inhibitable or intrinsic pathway induced by various forms of stress like intracellular damage, developmental cues, and external stimuli and (2) the caspase 8/10 dependent or extrinsic pathway initiated by the engagement of death receptors
The caspase 8/10 dependent or extrinsic pathway is a death receptor mediated mechanism that results in the activation of caspase-8 and caspase-10. Activation of death receptors like Fas/CD95, TNFR1, and the TRAIL receptor is promoted by the TNF family of ligands including FASL (APO1L OR CD95L), TNF, LT-alpha, LT-beta, CD40L, LIGHT, RANKL, BLYS/BAFF, and APO2L/TRAIL. These ligands are released in response to microbial infection, or as part of the cellular, humoral immunity responses during the formation of lymphoid organs, activation of dendritic cells, stimulation or survival of T, B, and natural killer (NK) cells, cytotoxic response to viral infection or oncogenic transformation.
The Bcl-2 inhibitable or intrinsic pathway of apoptosis is a stress-inducible process, and acts through the activation of caspase-9 via Apaf-1 and cytochrome c. The rupture of the mitochondrial membrane, a rapid process involving some of the Bcl-2 family proteins, releases these molecules into the cytoplasm. Examples of cellular processes that may induce the intrinsic pathway in response to various damage signals include: auto reactivity in lymphocytes, cytokine deprivation, calcium flux or cellular damage by cytotoxic drugs like taxol, deprivation of nutrients like glucose and growth factors like EGF, anoikis, transactivation of target genes by tumor suppressors including p53.
In many non-immune cells, death signals initiated by the extrinsic pathway are amplified by connections to the intrinsic pathway. The connecting link appears to be the truncated BID (tBID) protein a proteolytic cleavage product mediated by caspase-8 or other enzymes.
Identifier: R-HSA-169911
Species: Homo sapiens
A regulated balance between cell survival and apoptosis is essential for normal development and homeostasis of multicellular organisms (see Matsuzawa, 2001). Defects in control of this balance may contribute to autoimmune disease, neurodegeneration and cancer. Protein ubiquitination and degradation is one of the major mechanisms that regulate apoptotic cell death (reviewed in Yang and Yu 2003).
Identifier: R-HSA-9635465
Species: Homo sapiens
Compartment: cytosol
In order to survive and grow within the phagocyte, Mtb has to inhibit programmed cell death. Several proteins are secreted by Mtb that block different pathways leading to complete arrest of apoptosis (Moraco & Kornfeld 2014).
Identifier: R-HSA-9734009
Species: Homo sapiens
Defects in the regulation of the intrinsic pathway for apoptosis are involved in diseases associated with increased cell loss, such as neurodegenerative diseases, as well as in diseases associated with impaired elimination of harmful cells, such as cancer and autoimmunity. For review, please refer to Reed 2001, Lavrik et al. 2009, and Tuzlak et al. 2016.

So far, Reactome has annotated apoptosis defects associated with the loss of function of the CDKN2A gene product p14ARF in cancer, loss of function of TP53 in cancer, and CDK5 dysregulation in neurodegenerative diseases.
Identifier: R-HSA-109606
Species: Homo sapiens
The intrinsic (Bcl-2 inhibitable or mitochondrial) pathway of apoptosis functions in response to various types of intracellular stress including growth factor withdrawal, DNA damage, unfolding stresses in the endoplasmic reticulum and death receptor stimulation. Following the reception of stress signals, proapoptotic BCL-2 family proteins are activated and subsequently interact with and inactivate antiapoptotic BCL-2 proteins. This interaction leads to the destabilization of the mitochondrial membrane and release of apoptotic factors. These factors induce the caspase proteolytic cascade, chromatin condensation, and DNA fragmentation, ultimately leading to cell death. The key players in the Intrinsic pathway are the Bcl-2 family of proteins that are critical death regulators residing immediately upstream of mitochondria. The Bcl-2 family consists of both anti- and proapoptotic members that possess conserved alpha-helices with sequence conservation clustered in BCL-2 Homology (BH) domains. Proapoptotic members are organized as follows:

1. "Multidomain" BAX family proteins such as BAX, BAK etc. that display sequence conservation in their BH1-3 regions. These proteins act downstream in mitochondrial disruption.

2. "BH3-only" proteins such as BID,BAD, NOXA, PUMA,BIM, and BMF have only the short BH3 motif. These act upstream in the pathway, detecting developmental death cues or intracellular damage. Anti-apoptotic members like Bcl-2, Bcl-XL and their relatives exhibit homology in all segments BH1-4. One of the critical functions of BCL-2/BCL-XL proteins is to maintain the integrity of the mitochondrial outer membrane.

Identifier: R-HSA-140342
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
DNA fragmentation in response to apoptotic signals is achieved, in part, through the activity of apoptotic nucleases, termed DNA fragmentation factor (DFF) or caspase-activated DNase (CAD) (reviewed in Widlak and Garrard, 2005). In non-apoptotic cells, DFF is a nuclear heterodimer consisting of a 45 kD chaperone and inhibitor subunit (DFF45)/inhibitor of CAD (ICAD-L)] and a 40 kD nuclease subunit (DFF40/CAD)( Liu et al. 1997, 1998; Enari et al. 1998). During apoptosis, activated caspase-3 or -7 cleave DFF45/ICAD releasing active DFF40/CAD nuclease. The activity of DFF is tightly controlled at multiple stages. During translation, DFF45/ICAD, Hsp70, and Hsp40 proteins play a role in insuring the appropriate folding of DFF40 during translation(Sakahira and Nagata, 2002). The nuclease activity of DFF40 is enhanced by the chromosomal proteins histone H1, Topoisomerase II and HMGB1/2(Widlak et al., 2000). In addition, the inhibitors (DFF45/35; ICAD-S/L) are produced in stoichiometric excess (Widlak et al., 2003).
Identifier: R-HSA-168277
Species: Homo sapiens
Influenza A virus induces apoptosis in a variety of ways including activation of host TGF-beta by expression of viral NA, M1 and M2 proteins, and by the binding of viral PB1-F2 to host mitochondrial adenine nucleotide translocator 3 (ANT3).
Identifier: R-HSA-204981
Species: Homo sapiens
Compartment: cytosol, plasma membrane
NADE forms a complex with the 14-3-3epsilon isoform. The last one interacts with caspase 3 through its C terminal region. The NADE:4-3-3epsilon complex negatively regulates p75NTR-mediated apoptosis, probably by down regulating caspase activity.
Identifier: R-HSA-622420
Species: Homo sapiens
Compartment: cytosol
NOD1 was found to coimmunoprecipitate with several procaspases containing long prodomains with CARDs or DEDs, including caspase-1, caspase-2, caspase-4, caspase-8, and caspase-9, but not those with short prodomains like caspase-3 or caspase-7. Deletions of caspase-9 determined that the CARD domain was required for this interaction (Inohara et al. 1999). More recently, NOD1 activation of apoptosis was shown to require the RIP2-dependent activation of caspase-8, this effect being inhibited by CASP8 and FADD-like apoptosis regulator, also called FLICE-inhibitory protein, FLIP or CLARP (da Silva Correia et al. 2007), which is a specific inhibitor of caspase-8 (Irmler et al. 1997).
Identifier: R-HSA-180897
Species: Homo sapiens
In one model of Vpr mediated induction of apoptosis, Vpr acts directly on the mitochondrial permeability transition pore complex through its interaction with adenine nucleotide translocator (ANT). This interaction promotes the permeabiliztion of the mitochondrial membranes resulting in the release of cytochrome c and apoptosis-inducing factors.
Identifier: O15392-1
Species: Homo sapiens
Primary external reference: UniProt: O15392-1
Identifier: O15392-2
Species: Homo sapiens
Primary external reference: UniProt: O15392-2
Identifier: R-HSA-9645722
Species: Homo sapiens
Cancer-derived missense mutations in the CDKN2A gene that affect the C-terminal arginine-rich region of p14ARF (also known as CDKN2A transcription isoform 4, CDKN2A-4, p14 or ARF) impair p14ARF binding to the mitochondrial matrix protein C1QBP and interfere with p53-mediated apoptosis. Many mutations in the CDKN2A locus that affect C-terminal arginines of p14ARF are silent in p16INK4A (CDKN2A-1) (Itahana and Zhang 2008).
Identifier: R-HSA-168878
Species: Homo sapiens
Compartment: mitochondrial inner membrane, mitochondrial intermembrane space
Influenza A virus induces apoptosis in a variety of ways including binding of viral PB1-F2 to host mitochondrial adenine nucleotide translocator 3 (ANT3).
Identifier: Q96PG8
Species: Homo sapiens
Primary external reference: UniProt: Q96PG8
Identifier: Q92843
Species: Homo sapiens
Primary external reference: UniProt: Q92843

BIK

Identifier: Q13323
Species: Homo sapiens
Primary external reference: UniProt: Q13323
Identifier: Q96IZ0
Species: Homo sapiens
Primary external reference: UniProt: Q96IZ0
Identifier: Q9H175
Species: Homo sapiens
Primary external reference: UniProt: Q9H175
Identifier: R-HSA-6803205
Species: Homo sapiens
The exact mechanisms of action of several other pro-apoptotic TP53 (p53) targets, such as TP53I3 (PIG3), RABGGTA, BCL2L14, BCL6, NDRG1 and PERP, remain uncertain (Attardi et al. 2000, Guo et al. 2001, Samuels-Lev et al. 2001, Contente et al. 2002, Ihrie et al. 2003, Bergamaschi et al. 2004, Stein et al. 2004, Phan and Dalla-Favera 2004, Jen and Cheung 2005, Margalit et al. 2006, Zhang et al. 2007, Saito et al. 2009, Davies et al. 2009, Giam et al. 2012).
Identifier: Q96CA5
Species: Homo sapiens
Primary external reference: UniProt: Q96CA5
Identifier: Q07817-1
Species: Homo sapiens
Primary external reference: UniProt: Q07817-1
Identifier: Q9HD36
Species: Homo sapiens
Primary external reference: UniProt: Q9HD36

HYI

Identifier: Q5T013
Species: Homo sapiens
Primary external reference: UniProt: Q5T013
Identifier: O60936
Species: Homo sapiens
Primary external reference: UniProt: O60936
Identifier: O95382
Species: Homo sapiens
Primary external reference: UniProt: O95382
Identifier: Q6FI81-1
Species: Homo sapiens
Primary external reference: UniProt: Q6FI81-1
Identifier: Q96S65
Species: Homo sapiens
Primary external reference: UniProt: Q96S65
Identifier: Q92785
Species: Homo sapiens
Primary external reference: UniProt: Q92785
Identifier: P55060
Species: Homo sapiens
Primary external reference: UniProt: P55060
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