Linked Life Data

10825181

Source:http://linkedlifedata.com/resource/pubmed/id/10825181

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2000-9-14
pubmed:abstractText
The c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) pathway is activated by numerous cellular stresses. Although it has been implicated in mediating apoptosis and growth factor signaling, its role in regulating cell growth is not yet clear. Here, the influence of JNK on basal (unstimulated) growth of human tumor glioblastoma T98G cells was investigated using highly specific JNK antisense oligonucleotides to inhibit JNK expression. Transient depletion of either JNK1 or JNK2 suppressed cell growth associated with an inhibition of DNA synthesis and cell cycle arrest in S phase. The growth-inhibitory potency of JNK2 antisense ((JNK)2 IC(50) = 0.14 micrometer) was greater than that of JNK1 antisense ((JNK)1 IC(50) = 0.37 micrometer), suggesting that JNK2 plays a dominant role in regulating growth of T98G cells. Indeed, JNK2 antisense-treated populations exhibited greater inhibition of DNA synthesis and accumulation of S-phase cells than did the JNK1 antisense-treated cultures, with a significant proportion of these cells detaching from the tissue culture plate. JNK2 (but not JNK1) antisense-treated cultures exhibited marked elevation in the expression of the cyclin-dependent kinase inhibitor p21(cip1/waf1) accompanied by inhibition of Cdk2/Cdc2 kinase activities. Taken together, these results indicate that JNK is required for growth of T98G cells in nonstress conditions and that p21(cip1/waf1) may contribute to the sustained growth arrest of JNK2-depleted T98G cultures.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24767-75
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10825181-Cell Cycle, pubmed-meshheading:10825181-Cell Division, pubmed-meshheading:10825181-DNA, Neoplasm, pubmed-meshheading:10825181-Gene Expression Regulation, Neoplastic, pubmed-meshheading:10825181-Glioblastoma, pubmed-meshheading:10825181-Humans, pubmed-meshheading:10825181-JNK Mitogen-Activated Protein Kinases, pubmed-meshheading:10825181-Kinetics, pubmed-meshheading:10825181-Mitogen-Activated Protein Kinase 8, pubmed-meshheading:10825181-Mitogen-Activated Protein Kinase 9, pubmed-meshheading:10825181-Mitogen-Activated Protein Kinases, pubmed-meshheading:10825181-Oligodeoxyribonucleotides, Antisense, pubmed-meshheading:10825181-S Phase, pubmed-meshheading:10825181-Thionucleotides, pubmed-meshheading:10825181-Transcription, Genetic, pubmed-meshheading:10825181-Tumor Cells, Cultured
pubmed:year
2000
pubmed:articleTitle
c-Jun N-terminal kinase is essential for growth of human T98G glioblastoma cells.
pubmed:affiliation
Cell Stress and Aging Section, Laboratory of Biological Chemistry, Gerontology Research Center, NIA, National Institutes of Health, Baltimore, Maryland 21224, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't