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Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells

Phosphorylation in normal and transformed NIH3T3 cells of the 80K protein, a specific substrate for protein kinase C, was compared by means of two‐dimensional gel analysis. We obtained evidence that NIH3T3 cells transformed by the c‐raf or H‐ras oncogene maintained a decreased level of phosphorylati...

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Detalles Bibliográficos
Autores principales: Oh‐uchida, Mamoru, Yano, Kazumi, Kawamoto, Shoko, Shimizu, Kenji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 1990
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5918085/
https://www.ncbi.nlm.nih.gov/pubmed/2118892
http://dx.doi.org/10.1111/j.1349-7006.1990.tb02648.x
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author Oh‐uchida, Mamoru
Yano, Kazumi
Kawamoto, Shoko
Shimizu, Kenji
author_facet Oh‐uchida, Mamoru
Yano, Kazumi
Kawamoto, Shoko
Shimizu, Kenji
author_sort Oh‐uchida, Mamoru
collection PubMed
description Phosphorylation in normal and transformed NIH3T3 cells of the 80K protein, a specific substrate for protein kinase C, was compared by means of two‐dimensional gel analysis. We obtained evidence that NIH3T3 cells transformed by the c‐raf or H‐ras oncogene maintained a decreased level of phosphorylation of the 80K protein, with or without phorbol ester (TPA)‐stimulation, at all concentrations of serum tested while normal NIH3T3 cells maintained an elevated level of phosphorylation of the 80K protein. Furthermore, NIH3T3 cells transformed by N‐ras, K‐ras, src, mos or polyoma middle T antigen exhibited a decreased level of phosphorylation of the 80K protein. These events were confirmed by an analysis of a hormone‐inducible H‐ras transformant. Thus, phosphorylation of the 80K protein is inversely correlated with cellular transformation.
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spelling pubmed-59180852018-05-11 Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells Oh‐uchida, Mamoru Yano, Kazumi Kawamoto, Shoko Shimizu, Kenji Jpn J Cancer Res Article Phosphorylation in normal and transformed NIH3T3 cells of the 80K protein, a specific substrate for protein kinase C, was compared by means of two‐dimensional gel analysis. We obtained evidence that NIH3T3 cells transformed by the c‐raf or H‐ras oncogene maintained a decreased level of phosphorylation of the 80K protein, with or without phorbol ester (TPA)‐stimulation, at all concentrations of serum tested while normal NIH3T3 cells maintained an elevated level of phosphorylation of the 80K protein. Furthermore, NIH3T3 cells transformed by N‐ras, K‐ras, src, mos or polyoma middle T antigen exhibited a decreased level of phosphorylation of the 80K protein. These events were confirmed by an analysis of a hormone‐inducible H‐ras transformant. Thus, phosphorylation of the 80K protein is inversely correlated with cellular transformation. Blackwell Publishing Ltd 1990-08 /pmc/articles/PMC5918085/ /pubmed/2118892 http://dx.doi.org/10.1111/j.1349-7006.1990.tb02648.x Text en
spellingShingle Article
Oh‐uchida, Mamoru
Yano, Kazumi
Kawamoto, Shoko
Shimizu, Kenji
Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells
title Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells
title_full Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells
title_fullStr Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells
title_full_unstemmed Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells
title_short Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells
title_sort transformation‐specific decrease of phosphorylation of 80k protein, a substrate of protein kinase c, in nih3t3 cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5918085/
https://www.ncbi.nlm.nih.gov/pubmed/2118892
http://dx.doi.org/10.1111/j.1349-7006.1990.tb02648.x
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