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Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases.

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We have used myelin basic protein immobilized in sodium dodecyl sulfate-polyacrylamide gels to identify protein kinases after gel electrophoresis, followed by protein kinase reactions. This technique has permitted us to detect three protein kinases in serum-deprived cells transformed by p60src. On

Vinblastine-dependent down-modulation of TNF receptors in human osteosarcoma cells is mediated by protein kinase C activity.

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The binding of tumor necrosis factor (TNF) to a human osteogenic sarcoma cell line (Saos-2) was investigated. These cells express two types of receptors as determined by specific monoclonal antibodies. Vinblastine induced a down-modulation of these receptors weaker than the one produced by phorbol

Expression cDNA cloning of a serine kinase transforming gene.

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By ectopic expression of cDNAs derived from a Ewing sarcoma cell line in NIH3T3 cells, we isolated a transforming gene (est). Sequence analysis revealed homology to the cot oncogene, which encodes a novel serine kinase. Whereas the cot product was truncated at its carboxy-terminal end as a result of

Serum amyloid A gene expression under acute-phase conditions involves participation of inducible C/EBP-beta and C/EBP-delta and their activation by phosphorylation.

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Serum amyloid A (SAA) is a plasma protein whose synthesis is markedly increased in the liver during the inflammatory process. Previous analysis of SAA promoter function implicated the involvement of the CCAAT/enhancer-binding protein (C/EBP) in controlling this process. In this study, using

Cooperation between phosphorylation and acetylation processes in transcriptional control.

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We previously reported that the activation of the M promoter of the human choline acetyltransferase (ChAT) gene by butyrate and trapoxin in transfected CHP126 cells is blocked by PD98059, a specific mitogen-activated protein kinase kinase (MEK) inhibitor (E. Espinos and M. J. Weber, Mol. Brain Res.

Regulation of the TNF-alpha receptor in human osteosarcoma cells: role of microtubules and of protein kinase C.

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The effect of the tumor promoter 4 beta-phorbol 12-myristate 13-acetate and of the phosphatases inhibitor okadaic acid on the binding of tumor necrosis factor-alpha (TNF-alpha) to a human osteogenic sarcoma cell line (Saos-2) was investigated. Both substances prevented almost completely TNF binding

Rapamycin inhibits IGF-1 stimulated cell motility through PP2A pathway.

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Serine/threonine (Ser/Thr) protein phosphatase 2A (PP2A) has been implicated as a novel component of the mammalian target of rapamycin (mTOR) signaling pathway. Recently we have demonstrated that mTOR regulates cell motility in part through p70 S6 kinase 1 (S6K1) and eukaryotic initiation factor 4E

Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase.

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The abundant, cytoplasmic 90-kDa heat-shock protein associates transiently with the Rous sarcoma virus oncogenic protein tyrosine kinase, pp60v-src, directs its cellular trafficking and negatively regulates its kinase activity. Here we report that the serine/threonine phosphatase inhibitor, okadaic

Transcription of alpha2 integrin gene in osteosarcoma cells is enhanced by tumor promoters.

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Integrin alpha2beta1 is a heterodimeric transmembrane receptor for collagens. In osteogenic cells the expression of alpha2beta1 integrin is induced by both Kirsten sarcoma virus and chemical transformation. The association of alpha2 integrin with transformed cell phenotype was studied further by

Synergistic cytotoxic effect between serine-threonine phosphatase inhibitors and 5-fluorouracil: a novel concept for modulation of cytotoxic effect.

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OBJECTIVE The present study was undertaken to look for an agent or agents able to modulate the cytotoxic effect of 5-fluorouracil (FUra) and to investigate the role of serine-threonine phosphatase inhibitors on the cytotoxic effect of FUra. METHODS The cytotoxicities of FUra and protein phosphatase

Transformation-resistant mos revertant is unable to activate MAP kinase kinase in response to v-mos or v-raf.

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To study the mechanism by which v-mos induces cell transformation, we generated a transformed rat cell line (DTM) containing two functional copies of mos, one encoding the p37v-mos of the m1 wild-type strain of Moloney murine sarcoma virus (Mo-MuSV) and the other the p85gag-mos fusion protein of the

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