caspase-mediated cell death
apoptose
caspase oor Galisies
caspase
en
(biochemistry) Any of several intracellular proteolytic enzymes that mediate apoptosis
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Caspase
en
family of cysteine proteases
caspase
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If cells receive multiple apoptotic stimuli, caspase-3 activates the Mst1 kinase, which phosphorylates the serine at position 14 in all histone H2B proteins, which helps facilitate chromatin condensation.
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Researchers decided upon the nomenclature of the caspase in 1996.
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Also, it is extensively used in research for the detection of DNA damage, caspase cleavage and apoptosis.
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In many instances, a particular caspase had been identified simultaneously by more than one laboratory; each would then give the protein a different name.
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This release of cytochrome c in turn activates caspase 9, a cysteine protease.
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This proteolytic activity is performed by members of the caspase-protein family who cleave the lamins after aspartic acid (Asp) residues.
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Nevertheless, TRADD binds FADD, which then recruits the cysteine protease caspase-8.
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Caspase 9 can then go on to activate caspase 3 and caspase 7, which are responsible for destroying the cell from within.
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A high concentration of caspase-8 induces its autoproteolytic activation and subsequent cleaving of effector caspases, leading to cell apoptosis.
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Recently, oocytes were used recently to study the biochemical mechanisms of caspase-2 activation; importantly, this mechanism turns out to be conserved in mammals.
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For example, caspase 3 was variously known as CPP32, apopain and Yama.
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MALT1 itself is a caspase-like protein that cleaves A20, an inhibitory protein of NF-κB signaling (which acts by deubiquitylating NF-κB’s ubiquitylation substrates, having an inhibitory effect).
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Some of these mutations have been proposed to be detrimental to cytoskeleton formation as well as an increase in caspase 3 activity, which would lead to increased apoptosis of cells with these mutations.
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This is because NF-κB regulates anti-apoptotic genes especially the TRAF1 and TRAF2 and therefore abrogates the activities of the caspase family of enzymes, which are central to most apoptotic processes.
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Caspases, therefore, were numbered in the order in which they were identified.
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Pro-Caspase-8 and pro-caspase-9 bind to specific adaptor molecules via DED domains and this leads to autoactivation of caspases.
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Granzyme B also cleaves the protein Bid, which recruits the proteins Bax and Bak to change the membrane permeability of the mitochondria, causing the release of cytochrome c (which is one of the parts needed to activate caspase-9 via the apoptosome), Smac/Diablo and Omi/HtrA2 (which suppress the inhibitor of apoptosis proteins (IAPs)), among other proteins.
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ICE was the first mammalian caspase to be characterised because of its similarity to the nematode death gene ced-3, but it appears that the principal role of this enzyme is to mediate inflammation rather than cell death.
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Post-translational myristoylation typically occurs following a caspase cleavage event resulting in the exposure of an internal glycine residue, which would then be available for myristic acid addition.
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Caspases (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death (including apoptosis, pyroptosis and necroptosis) and inflammation.
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Another more recent example of a disabled gene links the deactivation of the caspase 12 gene (through a nonsense mutation) to positive selection in humans.
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Excess progenitor cell proliferation that leads to gross brain abnormalities is often lethal, as seen in caspase-3 or caspase-9 knockout mice which develop exencephaly in the forebrain.
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The brainstem, spinal cord, and peripheral ganglia of these mice develop normally, however, suggesting that the involvement of caspases in PCD during development depends on the brain region and cell type.
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Cells that express mutant caspase-resistant lamins are deficient in nuclear changes related to apoptosis, suggesting that lamins play a role in initiating the events that lead to apoptotic degradation of the nucleus.
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Other mammalian caspases were subsequently identified, in addition to caspases in organisms such as fruit fly Drosophila melanogaster.
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49 sinne gevind in 8 ms. Hulle kom uit baie bronne en word nie nagegaan nie.