Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1997-4-24
pubmed:abstractText
Dephosphorylation of the RB protein has been reported to be associated with apoptosis. In contrast, we show that treatment of HL60 cells with etoposide or cytosine arabinoside or treatment of breast epithelial cells with alpha-FAS is associated with the cleavage of a 5 kDa fragment from the C-terminus of RB, resulting in a truncated product that we have designated as p100cl. This cleavage event coincides with the activation of cysteine proteases at the onset of apoptosis, is blocked by the addition of iodoacetamide to cells prior to the onset of apoptosis, and results in the expression of faster migrating protein species which can mimic dephosphorylated RB. The free 5 kDa fragment is detected only during apoptosis, predicts a cleavage site that we have mapped to a unique CPP32-like recognition sequence which is present at the C-terminus of all reported RB homologues, and results in a truncated RB protein with enhanced E2F binding affinity. While the causality for this cleavage event in the apoptotic process is still under investigation, our findings suggest distinct post-translational pathways for the RB product between cells examined during growth arrest (p105 hypophosphorylated RB) or apoptosis (p100cl).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95, http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Cytarabine, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/E2F Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Etoposide, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma Protein, http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma-Binding Protein 1, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor DP1, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1243-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9121775-Antigens, CD95, pubmed-meshheading:9121775-Antineoplastic Agents, pubmed-meshheading:9121775-Apoptosis, pubmed-meshheading:9121775-Breast Neoplasms, pubmed-meshheading:9121775-Carrier Proteins, pubmed-meshheading:9121775-Cell Cycle Proteins, pubmed-meshheading:9121775-Cysteine Endopeptidases, pubmed-meshheading:9121775-Cytarabine, pubmed-meshheading:9121775-DNA-Binding Proteins, pubmed-meshheading:9121775-E2F Transcription Factors, pubmed-meshheading:9121775-Etoposide, pubmed-meshheading:9121775-Female, pubmed-meshheading:9121775-HL-60 Cells, pubmed-meshheading:9121775-Humans, pubmed-meshheading:9121775-Peptide Fragments, pubmed-meshheading:9121775-Phosphorylation, pubmed-meshheading:9121775-Retinoblastoma Protein, pubmed-meshheading:9121775-Retinoblastoma-Binding Protein 1, pubmed-meshheading:9121775-Transcription Factor DP1, pubmed-meshheading:9121775-Transcription Factors
pubmed:year
1997
pubmed:articleTitle
Apoptosis is associated with cleavage of a 5 kDa fragment from RB which mimics dephosphorylation and modulates E2F binding.
pubmed:affiliation
NCI-Navy Medical Oncology Branch, Division of Clinical Sciences, National Cancer Institute, Bethesda, Maryland 20889, USA.
pubmed:publicationType
Journal Article