Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-6-17
pubmed:abstractText
We characterized the activation of interleukin-1beta-converting enzyme (ICE)-like proteases (caspases) in human neuroblastoma cells (SH-SY5Y) following challenge with staurosporine, an established agent known to induce apoptosis. Time course analyses of lactate dehydrogenase release detected a significant increase in cell death as early as 6 h that continued at least until 24 h following staurosporine treatment. Western blot analyses using anti-poly(ADP-ribose) polymerase (anti-PARP) and anti-CPP32 antibodies revealed proteolytic processing of CPP32 (an ICE homologue) as well as fragmentation of PARP as early as 3 h following staurosporine challenge. Furthermore, the hydrolysis of the CPP32 substrate acetyl-DEVD-7-amido-4-methylcoumarin was detected as early as 3 h and became maximal at 6 h after staurosporine challenge, suggesting a delayed and sustained period of CPP32-like activation. In addition, we used the first immunohistochemical examination of CPP32 and PARP in cells following an apoptotic challenge. The localization of CPP32 in untreated SH-SY5Y cells was exclusively restricted to the cytoplasm. Following staurosporine challenge there was a condensing of CPP32 immunofluorescence from the cytoplasm to a region adjacent to the plasma membrane. In contrast, PARP immunofluorescence was evenly distributed in the nucleus in untreated SH-SY5Y cells and on staurosporine challenge was found to be associated with condensed chromatin. It is important that a pan ICE inhibitor [carbobenzoxy-Asp-CH2OC(O)-2,6-dichlorobenzene] was able to attenuate lactate dehydrogenase release and PARP and CPP32 cleavage and altered immunohistochemical staining patterns for PARP and CPP32 following staurosporine challenge.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid, http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Caspase 1, http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3, http://linkedlifedata.com/resource/pubmed/chemical/Caspases, http://linkedlifedata.com/resource/pubmed/chemical/Coumarins, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors, http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes, http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides, http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases, http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine, http://linkedlifedata.com/resource/pubmed/chemical/acetyl-aspartyl-glutamyl-valyl-aspar..., http://linkedlifedata.com/resource/pubmed/chemical/benzyloxycarbonyl-Asp-CH2OC(O)-2,6-d...
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
68
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2328-37
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9166725-Antibody Specificity, pubmed-meshheading:9166725-Apoptosis, pubmed-meshheading:9166725-Aspartic Acid, pubmed-meshheading:9166725-Caspase 1, pubmed-meshheading:9166725-Caspase 3, pubmed-meshheading:9166725-Caspases, pubmed-meshheading:9166725-Coumarins, pubmed-meshheading:9166725-Cysteine Endopeptidases, pubmed-meshheading:9166725-DNA, pubmed-meshheading:9166725-Enzyme Inhibitors, pubmed-meshheading:9166725-Enzyme Precursors, pubmed-meshheading:9166725-Fluorescent Antibody Technique, pubmed-meshheading:9166725-Fluorescent Dyes, pubmed-meshheading:9166725-Humans, pubmed-meshheading:9166725-Hydrolysis, pubmed-meshheading:9166725-Neuroblastoma, pubmed-meshheading:9166725-Neurons, pubmed-meshheading:9166725-Oligopeptides, pubmed-meshheading:9166725-Poly(ADP-ribose) Polymerases, pubmed-meshheading:9166725-Protease Inhibitors, pubmed-meshheading:9166725-Staurosporine, pubmed-meshheading:9166725-Tumor Cells, Cultured
pubmed:year
1997
pubmed:articleTitle
Characterization of CPP32-like protease activity following apoptotic challenge in SH-SY5Y neuroblastoma cells.
pubmed:affiliation
Department of Immunopathology, Parke-Davis Pharmaceutical Research, Warner-Lambert Company, Ann Arbor, Michigan 48105, U.S.A.
pubmed:publicationType
Journal Article