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Human recombinant caspase 2-3-7

ABSTRACT: COFRADIC identification of human recombinant caspase-2, -3, -7 cleavage sites

INSTRUMENT(S): instrument model

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Magdalena Wejda

PROVIDER: PRD000557 | Pride | 2012-08-15

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	PRIDE_Exp_Complete_Ac_19136.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_19136.pride.mztab.gz	Mztab
	PRIDE_Exp_Complete_Ac_19136.xml.gz	Xml

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Publications

Degradomics reveals that cleavage specificity profiles of caspase-2 and effector caspases are alike.

Wejda Magdalena M Impens Francis F Takahashi Nozomi N Van Damme Petra P Gevaert Kris K Vandenabeele Peter P

The Journal of biological chemistry 20120723 41

Caspase-2 is considered an initiator caspase because its long prodomain contains a CARD domain that allows its recruitment and activation in several complexes by homotypic death domain-fold interactions. Because little is known about the function and specificity of caspase-2 and its physiological substrates, we compared the cleavage specificity profile of recombinant human caspase-2 with those of caspase-3 and -7 by analyzing cell lysates using N-terminal COmbined FRActional DIagonal Chromatogra ...[more]

PMID: 22825847

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Mass Spectra of a caspase 7 cleavage fragment of SATB2

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Time-resolved analysis of proteolytic products of ANXA1 by recombinant HTRA1

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Granzyme M targets topoisomerase II alpha to trigger cell cycle arrest and caspase-dependent apoptosis in cancer cells

Project description:Cytotoxic lymphocyte protease granzyme M (GrM) is a potent inducer of tumor cell death in vitro and in vivo. The apoptotic phenotype and mechanism by which it induces cell death however, remain poorly understood and controversial. Here, we show that GrM-induced cell death was largely caspase-dependent with various hallmarks of classical apoptosis, coinciding with caspase-independent G2/M cell cycle arrest. Using positional proteomics in HeLa cells, we identified the nuclear enzyme topoisomerase II alpha (topoII alpha) as a physiological substrate of GrM. Cleavage of topoII alpha by GrM at Leu1280 dissected topoII aplha functional domains from the nuclear localization signals, leading to nuclear exit of topoII alpha catalytic activity into the cytoplasm, and rendering it nonfunctional. Similar to the apoptotic phenotype of GrM, topoII aplha depletion in tumor cells led to cell cycle arrest in G2/M, mitochondrial perturbations, caspase activation, and apoptosis. We conclude that cytotoxic lymphocyte GrM targets topoII aplha to trigger cell cycle arrest and caspase-dependent apoptosis. Raw data files were processed with Mascot distiller 2.3. The mgf files were searched with Mascot daemon 2.3. The quantification was also done by Mascot Distiller. All data was stored in ms_lims. Fixed modifications: methionine oxidation, trideutero-acetylation of lysine, carbamidomethylation of cysteine. Variable modifications: acetylation of peptide N-terminus, trideutero-acetylation of peptide N-terminus, pyroglutamate formation of N-terminal glutamine Enzyme: semi-Arg-C/P with one missed cleavage allowed. Precursor mass tolerance: 10 ppm. Peptide fragment mass tolerance: 0.5 Da Quantitation method: triple SILAC arginine +6 Da and +10 Da

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Non-lethal stress-induced discrete proteolysis is caspase-3/7 dependent

Project description:Cells are in constant adaptation to environmental changes to insure their proper functioning. When exposed to stresses, cells activate specific pathways to elicit adaptive modifications. Those changes can be mediated by selective modulation of gene and protein expression as well as by post-translational modifications, such as phosphorylation and proteolytic processing. Protein cleavage, as a controlled and limited post-translational modification, is involved in diverse physiological processes such as the maintenance of protein homeostasis, activation of repair pathways, apoptosis and the regulation of proliferation. Here we assessed by quantitative proteomics the proteolytic landscape in two cell lines subjected to low cisplatin concentrations used as a mild non-lethal stress paradigm. This landscape was compared to the one obtained in the same cells stimulated with cisplatin concentrations inducing apoptosis. These analyses were performed in wild-type cells and in cells lacking the two main executioner caspases: caspase-3 and caspase-7. Ninety proteins were found to be cleaved at one or a few sites (discrete cleavage) in low stress conditions compared to four hundred and forty in apoptotic cells. Many of the cleaved proteins in stressed cells were also found to be cleaved in apoptotic conditions. As expected in apoptotic cells, ~80% of the cleavage events were dependent on caspase 3/caspase 7. Strikingly, upon exposure to non-lethal stresses, no discrete cleavage was detected in cells lacking caspase-3 and caspase-7. This indicates that the proteolytic landscape in stressed viable cells fully depends on the activity of executioner caspases. These results suggest that the so-called executioner caspases fulfill important stress adaptive responses distinct from their role in apoptosis.

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Integration of Innate Immune Signaling by 2 Caspase-8-Mediated Cleavage of N4BP1

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