In vivo and in vitro evidence for extracellular caspase activity released from apoptotic cells

dc.contributor.authorHentze, Hannes
dc.contributor.authorSchwoebel, Frank
dc.contributor.authorLund, Søren
dc.contributor.authorKehl, Marius
dc.contributor.authorErtel, Wolfgang
dc.contributor.authorWendel, Albrecht
dc.contributor.authorJäättelä, Marja
dc.contributor.authorLeist, Marcel
dc.date.accessioned2020-10-08T13:59:53Z
dc.date.available2020-10-08T13:59:53Z
dc.date.issued2001-05-25eng
dc.description.abstractWhile caspases play an established role as intracellular executors of apoptosis, little is known about extracellular activities of this ubiquitously expressed family of proteases. We demonstrate here that recombinant caspase-3 retained enzymatic activity in various extracellular fluids. Experiments with cell lines, primary cells, and mice with fulminant CD95-triggered hepatitis showed that significant amounts of DEVD-aminofluoromethylcoumarine-cleaving activity, indicative of active effector caspases, were released into the medium/plasma during apoptosis. Furthermore, caspase activities were detected in liquor samples from human head trauma patients. These findings warrant closer investigation of DEVDase activity as a diagnostic marker, and of potential extracellular substrates for caspases.eng
dc.description.versionpublishedeng
dc.identifier.doi10.1006/bbrc.2001.4918eng
dc.identifier.pmid11355887eng
dc.identifier.urihttps://kops.uni-konstanz.de/handle/123456789/51266
dc.language.isoengeng
dc.rightsterms-of-use
dc.rights.urihttps://rightsstatements.org/page/InC/1.0/
dc.subjectapoptosis, necrosis, caspase, liver, redox, protease assay, plasma, serum, extracellulareng
dc.subject.ddc570eng
dc.titleIn vivo and in vitro evidence for extracellular caspase activity released from apoptotic cellseng
dc.typeJOURNAL_ARTICLEeng
dspace.entity.typePublication
kops.citation.bibtex
@article{Hentze2001-05-25vitro-51266,
  year={2001},
  doi={10.1006/bbrc.2001.4918},
  title={In vivo and in vitro evidence for extracellular caspase activity released from apoptotic cells},
  number={5},
  volume={283},
  issn={0006-291X},
  journal={Biochemical and Biophysical Research Communications},
  pages={1111--1117},
  author={Hentze, Hannes and Schwoebel, Frank and Lund, Søren and Kehl, Marius and Ertel, Wolfgang and Wendel, Albrecht and Jäättelä, Marja and Leist, Marcel}
}
kops.citation.iso690HENTZE, Hannes, Frank SCHWOEBEL, Søren LUND, Marius KEHL, Wolfgang ERTEL, Albrecht WENDEL, Marja JÄÄTTELÄ, Marcel LEIST, 2001. In vivo and in vitro evidence for extracellular caspase activity released from apoptotic cells. In: Biochemical and Biophysical Research Communications. Elsevier. 2001, 283(5), pp. 1111-1117. ISSN 0006-291X. eISSN 1090-2104. Available under: doi: 10.1006/bbrc.2001.4918deu
kops.citation.iso690HENTZE, Hannes, Frank SCHWOEBEL, Søren LUND, Marius KEHL, Wolfgang ERTEL, Albrecht WENDEL, Marja JÄÄTTELÄ, Marcel LEIST, 2001. In vivo and in vitro evidence for extracellular caspase activity released from apoptotic cells. In: Biochemical and Biophysical Research Communications. Elsevier. 2001, 283(5), pp. 1111-1117. ISSN 0006-291X. eISSN 1090-2104. Available under: doi: 10.1006/bbrc.2001.4918eng
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    <dcterms:abstract xml:lang="eng">While caspases play an established role as intracellular executors of apoptosis, little is known about extracellular activities of this ubiquitously expressed family of proteases. We demonstrate here that recombinant caspase-3 retained enzymatic activity in various extracellular fluids. Experiments with cell lines, primary cells, and mice with fulminant CD95-triggered hepatitis showed that significant amounts of DEVD-aminofluoromethylcoumarine-cleaving activity, indicative of active effector caspases, were released into the medium/plasma during apoptosis. Furthermore, caspase activities were detected in liquor samples from human head trauma patients. These findings warrant closer investigation of DEVDase activity as a diagnostic marker, and of potential extracellular substrates for caspases.</dcterms:abstract>
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kops.sourcefield.plainBiochemical and Biophysical Research Communications. Elsevier. 2001, 283(5), pp. 1111-1117. ISSN 0006-291X. eISSN 1090-2104. Available under: doi: 10.1006/bbrc.2001.4918eng
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