Transformation-specific decrease of phosphorylation of 80K protein, a substrate of protein kinase C, in NIH3T3 cells

Mamoru Oouchida, Kazumi Yano, Shoko Kawamoto, Kenji Shimizu

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)799-806
Number of pages8
JournalJapanese Journal of Cancer Research
Volume81
Issue number8
Publication statusPublished - Aug 1990
Externally publishedYes

Fingerprint

Protein Kinase C
Phosphorylation
Proteins
ras Genes
Viral Tumor Antigens
Phorbol Esters
Gels
Hormones
Serum

Keywords

  • 80K Protein phosphorylation
  • Phorbol ester
  • Protein kinase C
  • raf transformant H-ras transformant

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

Cite this

Transformation-specific decrease of phosphorylation of 80K protein, a substrate of protein kinase C, in NIH3T3 cells. / Oouchida, Mamoru; Yano, Kazumi; Kawamoto, Shoko; Shimizu, Kenji.

In: Japanese Journal of Cancer Research, Vol. 81, No. 8, 08.1990, p. 799-806.

Research output: Contribution to journalArticle

@article{2c38d3f060c948babca9e022128026f8,
title = "Transformation-specific decrease of phosphorylation of 80K protein, a substrate of protein kinase C, in NIH3T3 cells",
abstract = "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.",
keywords = "80K Protein phosphorylation, Phorbol ester, Protein kinase C, raf transformant H-ras transformant",
author = "Mamoru Oouchida and Kazumi Yano and Shoko Kawamoto and Kenji Shimizu",
year = "1990",
month = "8",
language = "English",
volume = "81",
pages = "799--806",
journal = "Cancer Science",
issn = "1347-9032",
publisher = "Wiley-Blackwell",
number = "8",

}

TY - JOUR

T1 - Transformation-specific decrease of phosphorylation of 80K protein, a substrate of protein kinase C, in NIH3T3 cells

AU - Oouchida, Mamoru

AU - Yano, Kazumi

AU - Kawamoto, Shoko

AU - Shimizu, Kenji

PY - 1990/8

Y1 - 1990/8

N2 - 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.

AB - 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.

KW - 80K Protein phosphorylation

KW - Phorbol ester

KW - Protein kinase C

KW - raf transformant H-ras transformant

UR - http://www.scopus.com/inward/record.url?scp=0025088194&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025088194&partnerID=8YFLogxK

M3 - Article

C2 - 2118892

AN - SCOPUS:0025088194

VL - 81

SP - 799

EP - 806

JO - Cancer Science

JF - Cancer Science

SN - 1347-9032

IS - 8

ER -