Role of protein kinase C in the deficient gap junctional intercellular communication of K-ras-transformed murine lung epithelial cells.

Abstract:

BACKGROUND:Protein kinase C (PKC) activity is increased and gap junctional intercellular communication (GJIC) is decreased frequently in Ras-transformed cells. We investigated the roles of Ras and PKC in the deficient gap junctional intercellular communication (GJIC) of K-ras-transformed E9 mouse lung carcinoma cells. METHODS:GJIC was measured by fluorescent dye microinjection. Ras activity was blocked with lovastatin or a K-ras antisense oligonucleotide. PKC activity was inhibited with GF 109203X or apigenin or was downregulated by overnight treatment with 12-O-tetradecanoylphorbol-13-acetate. The content and phosphorylation of the gap junction protein, connexin43 (Cx43), was assessed by Western blot. RESULTS:E9 cell GJIC was increased two-three fold by lovastatin, the K-ras antisense oligonucleotide, and PKC inhibition/downregulation. Cx43 content and phosphorylation were unchanged, however. CONCLUSIONS:Oncogenic Ras blocks GJIC in E9 cells through a PKC-dependent mechanism, but this does not directly involve Cx43 expression or phosphorylation.

journal_name

Anticancer Res

journal_title

Anticancer research

authors

Cesen-Cummings K,Warner KA,Ruch RJ

subject

Has Abstract

pub_date

1998-11-01 00:00:00

pages

4343-6

issue

6A

eissn

0250-7005

issn

1791-7530

journal_volume

18

pub_type

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