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Vol. 12, Issue 7, 1973-1982, July 2001
and Low E-Cadherin Expression Contribute to High
Migratory Activity of Colon Carcinoma Cells
Institute of Immunology, Witten/Herdecke University, 58448 Witten,
Germany
The protein kinase C (PKC) is a family of serine/threonine kinases
that are key regulatory enzymes involved in growth, differentiation, cytoskeletal reorganization, tumor promotion, and migration. We investigated the functional involvement of PKC isotypes and of E-cadherin in the regulation of the locomotion of six human
colon-adenocarcinoma cell lines. The different levels of the PKC 
and the E-cadherin expression have predictable implications in the
spontaneous locomotory activity. With the use of PKC -specific
inhibitors (safingol, Go6976) as well as the PKC 
-specific
inhibitor rottlerin, we showed that only PKC plays a major role in
the regulation of tumor cell migration. The results were verified by
knocking out the translation of PKC isozymes with the use of an
antisense oligonucleotide strategy. After stimulation with phorbol
ester we observed a translocation and a colocalization of the activated
PKC at the plasma membrane to the surrounding extracellular matrix.
Furthermore, we investigated the functional involvement of E-cadherin
in the locomotion with the use of a blocking antibody. A high level of
PKC expression together with a low E-cadherin expression was
strongly related to a high migratory activity of the colon carcinoma
cells. This correlation was independent of the differentiation grade of
the tumor cell lines.
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