Literature DB >> 3196326

Protein kinase C activities and bindings of a phorbol ester tumor promoter in 41 cell lines.

K Chida1, N Kato, S Yamada, T Kuroki.   

Abstract

The activities of protein kinase C (PKC) and the bindings to phorbol-12,13-dibutyrate (PDBu) of 41 cell lines were measured. The activities of PKC varied from 0.2 to 37 mU/10(6) cells in different cell lines, and in general were high in normal or untransformed cells and low in malignant, or transformed cells. The PDBu binding also varied considerably in different cell lines, and was again higher in normal or untransformed cells. In some cell lines, the binding was much higher at 4 degrees C than at 37 degrees C, suggesting rapid down-regulation of the binding. A correlation between PKC activity and PDBu binding was found only within certain cell types, i.e., epithelial cell lines derived from human tumors.

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Year:  1988        PMID: 3196326     DOI: 10.1016/s0006-291x(88)80002-0

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Protein kinase C beta expression in melanoma cells and melanocytes: differential expression correlates with biological responses to 12-O-tetradecanoylphorbol 13-acetate.

Authors:  M B Powell; R K Rosenberg; M J Graham; M L Birch; D T Yamanishi; J A Buckmeier; F L Meyskens
Journal:  J Cancer Res Clin Oncol       Date:  1993       Impact factor: 4.553

2.  Molecular and cellular features of esophageal cancer cells.

Authors:  T Nishihira; Y Hashimoto; M Katayama; S Mori; T Kuroki
Journal:  J Cancer Res Clin Oncol       Date:  1993       Impact factor: 4.553

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

Authors:  M Oh-uchida; K Yano; S Kawamoto; K Shimizu
Journal:  Jpn J Cancer Res       Date:  1990-08
  3 in total

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