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Literature summary for 3.4.22.61 extracted from

  • Anathy, V.; Aesif, S.W.; Guala, A.S.; Havermans, M.; Reynaert, N.L.; Ho, Y.S.; Budd, R.C.; Janssen-Heininger, Y.M.
    Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas (2009), J. Cell Biol., 184, 241-252.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information engagement of Fas causes a rapid activation of caspase-8, induction of caspase-8 by Fas ligand, FasL, overview. Increased S-glutathionylation of Fas, caspase-8 activity, and cell death in cells lacking Grx1 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
N-carbobenzyloxy-VAD-fluoromethyl ketone a general caspase inhibitor, that effectively blocks FasL-induced cleavage of caspase-8 and completely prevents FasL-induced degradation of Grx1 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens initial activation of caspase-8 causes degradation of glutaredoxin-1, resulting in S-glutathionylation of Fas at cysteine 294, which subsequently enhances binding of FasL, aggregation of Fas, accumulation of Fas in lipid rafts, DISC assembly, and further activation of caspases, causing a propagation of apoptotic cell death. activation of caspases is required for degradation of glutaredoxin-1 and S-glutathionylation of Fas, engagement of Fas causes a rapid activation of caspase-8. Overexpression of Grx1 prevents increases in S-glutathionylation of Fas and attenuates caspase activation and apoptosis in response to receptor ligation. Cleaved caspase-8 and -3 demonstrate an association between active caspases and Grx1 in cells after ligation of Fas, whereas in control cells, these associations are not observed, regulation, overview ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification procaspase-8 is activated by cleavage to caspase-8 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
C-10 cell
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Homo sapiens
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commercial preparation recombinant enzyme Homo sapiens
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epithelial cell
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Homo sapiens
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lung
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Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutaredoxin-1 + H2O murine or human protein substrate, the putative cleavage site of caspase-8, amino acids 43-46 EFVD and 56-59 AIQD, which has predicted affiffinity toward glutamic and aspartic acid residues Homo sapiens ? cleavage produces a 8 kDA fragment ?
additional information initial activation of caspase-8 causes degradation of glutaredoxin-1, resulting in S-glutathionylation of Fas at cysteine 294, which subsequently enhances binding of FasL, aggregation of Fas, accumulation of Fas in lipid rafts, DISC assembly, and further activation of caspases, causing a propagation of apoptotic cell death. activation of caspases is required for degradation of glutaredoxin-1 and S-glutathionylation of Fas, engagement of Fas causes a rapid activation of caspase-8. Overexpression of Grx1 prevents increases in S-glutathionylation of Fas and attenuates caspase activation and apoptosis in response to receptor ligation. Cleaved caspase-8 and -3 demonstrate an association between active caspases and Grx1 in cells after ligation of Fas, whereas in control cells, these associations are not observed, regulation, overview Homo sapiens ?
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?
additional information caspases contain a reactive cysteine critical for enzymatic activity. Increased S-glutathionylation of Fas, caspase-8 activity, and cell death in cells lacking Grx1 Homo sapiens ?
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