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 Cancerjournal_title
International journal of cancerauthors
Niggli V,Zimmermann A,Keller Hdoi
10.1002/(SICI)1097-0215(19960208)65:4<473::AID-IJCsubject
Has Abstractpub_date
1996-02-08 00:00:00pages
473-8issue
4eissn
0020-7136issn
1097-0215pii
10.1002/(SICI)1097-0215(19960208)65:4<473::AID-IJCjournal_volume
65pub_type
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journal_title:International journal of cancer
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journal_title:International journal of cancer
pub_type: 杂志文章,多中心研究
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更新日期:2003-08-20 00:00:00
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