Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-6-17
pubmed:abstractText
The involvement of cell cycle-regulatory proteins in apoptosis of neuronally differentiated PC12 cells induced by the removal of nerve growth factor and serum was examined. Three major findings are presented. (1) Cdc2 kinase protein levels increased fivefold in apoptotic PC12 cells by day 3 of serum and nerve growth factor deprivation. Histone H1 kinase activity was increased significantly in p13(suc1) precipitates of apoptotic PC12 cells, which was due to increased activation and/or expression of cdc2 kinase. (2) The protein levels of cyclin-dependent kinase 4, cyclin D, and proliferating cell nuclear antigen that are normally expressed in the cell cycle were increased during neuronal PC12 cell apoptosis. (3) The levels of the catalytic subunit, but not the regulatory subunit of the calcium/calmodulin-dependent protein phosphatase 2B, decreased significantly concomitant with a significant decrease in protein phosphatase 2B activity early in the apoptotic process. Protein phosphatase 2A activity decreased slightly but significantly after 3 days of serum and nerve growth factor deprivation, and no alterations in protein phosphatase 1 were observed during the apoptotic process. These data demonstrate that certain cell cycle-regulatory proteins are inappropriately expressed and that alterations in specific phosphorylation events, as indicated by the increase in histone H1 kinase activity and the decrease in protein phosphatase 2B activity, are most likely occurring during apoptosis of PC12 cells. These observations support the hypothesis that apoptosis may be due in part to a nondividing cell's uncoordinated attempt to reenter and progress through the cell cycle.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Calcineurin, http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Maturation-Promoting Factor, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Growth Factors, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2, http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Suc1 protein, S pombe
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
2338-47
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9166726-Animals, pubmed-meshheading:9166726-Apoptosis, pubmed-meshheading:9166726-CDC2 Protein Kinase, pubmed-meshheading:9166726-Calcineurin, pubmed-meshheading:9166726-Calmodulin-Binding Proteins, pubmed-meshheading:9166726-Cell Cycle Proteins, pubmed-meshheading:9166726-Cell Differentiation, pubmed-meshheading:9166726-Fungal Proteins, pubmed-meshheading:9166726-Immunoblotting, pubmed-meshheading:9166726-Maturation-Promoting Factor, pubmed-meshheading:9166726-Nerve Growth Factors, pubmed-meshheading:9166726-PC12 Cells, pubmed-meshheading:9166726-Phosphoprotein Phosphatases, pubmed-meshheading:9166726-Precipitin Tests, pubmed-meshheading:9166726-Protein Kinases, pubmed-meshheading:9166726-Protein Phosphatase 1, pubmed-meshheading:9166726-Protein Phosphatase 2, pubmed-meshheading:9166726-Rats, pubmed-meshheading:9166726-Schizosaccharomyces pombe Proteins
pubmed:year
1997
pubmed:articleTitle
Select alterations in protein kinases and phosphatases during apoptosis of differentiated PC12 cells.
pubmed:affiliation
Department of Pharmacology, University of Alabama at Birmingham, U.S.A.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.