Inhibition of protein kinase C-dependent protein phosphorylation correlates with increased polarity and locomotion in Walker 256 carcinosarcoma cells.

Abstract:

:Signal transduction pathways controlling tumor cell locomotion are not yet well understood. We have studied the role of protein kinase C (PKC)-dependent protein phosphorylation associated with changes in cell shape and locomotor activity of Walker carcinosarcoma cells in culture. We show that the inhibitory effect of phorbol-12-myristate-13-acetate (PMA), an activator of PKC, on cell polarity and locomotion can be suppressed by the PKC-selective inhibitor Ro 31-8220. PMA induces increased phosphorylation of at least 2 proteins, of 65 and 80 kDa, in intact Walker carcinosarcoma cells. These bands are enriched in cytosolic fractions isolated from cells incubated with 32PO4. Pre-incubation with Ro 31-8220 inhibits the PMA-induced phosphorylation of both bands in a concentration-dependent manner. This effect is very likely not due to inhibition of translocation of PKC to the membrane as Ro 31-8220 enhances, rather than inhibits, PMA-induced transfer of PKC beta(II) to the particulate fraction. We have carried out a quantitative analysis of phosphorylation of the 80-kDa band. Ro 31-8220 reverses both PMA-induced phosphorylation of this band and PMA-induced suppression of cell polarity in parallel. Increased phosphorylation of proteins via PKC may thus be a stop signal for locomoting Walker carcinosarcoma cells.

journal_name

Int J Cancer

authors

Niggli V,Zimmermann A,Keller H

doi

10.1002/(SICI)1097-0215(19960208)65:4<473::AID-IJC

subject

Has Abstract

pub_date

1996-02-08 00:00:00

pages

473-8

issue

4

eissn

0020-7136

issn

1097-0215

pii

10.1002/(SICI)1097-0215(19960208)65:4<473::AID-IJC

journal_volume

65

pub_type

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