Induction of apoptosis by protein kinase C pseudosubstrate lipopeptides in several human cells |
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Authors: | Kader Thiam Estelle Loing Frédéric Gilles Claudie Verwaerde Brigitte Quatannens Claude Auriault Hélène Gras-Masse |
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Institution: | (1) URA CNRS 1854, Institut de Biologie et Institut Pasteur de Lille, 1 Rue du Pr.A. Calmette, BP 447, F-59021 Lille, France;(2) URA CNRS 1309, Institut de Biologie et Institut Pasteur de Lille, 1 Rue du Pr. A. Calmette, BP 447, F-59021 Lille, France;(3) URA CNRS 1160, Institut de Biologie et Institut Pasteur de Lille, 1 Rue du Pr. A. Calmette, BP 447, F-59021 Lille, France |
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Abstract: | Summary Intracellular enzymes or receptors are interesting targets for the pharmacomodulation of cellular metabolism. We have previously
shown that modification of relatively long peptides by a palmitoyl-lysine residue could facilitate their delivery into the
cytoplasm of living cells. Several peptides containing pseudosubstrate sequences of protein kinase C (PKC) have been evaluated
for their ability to modulate phosphorylation of model substrate, neuronal morphology or tumor necrosis factor secretion.
In this work we have evaluated the effect of palmitoyl-modified PKC-pseudosubstrate peptides on induction of apoptosis. We
have established that these peptides are able to induce apoptosis in different human cell types (primary fibroblasts, T- and
B-lymphocyte cell lines) as assessed by (terminal deoxynucleotidyl transferase dUTP nick-end labelling) and DNA fragmentation.
In contrast, control peptides (non-lipidic PKC-pseudosubstrate peptides and irrelevant lipopeptides) had no or little effect
on programmed cell death. This work highlights the pharmacological interest of lipopeptides and argues in favor of the potential
role of PKC(s) in the cell death machinery.
K. Thiam and E. Loing have contributed equally to this work. |
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Keywords: | Apoptosis Protein kinase C Pseudosubstrate sequence Lipopeptide |
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