Protein kinase C isoforms involved in regulation of cell shape and locomotion of human fibrosarcoma HT1080 cells.

Détails

ID Serval
serval:BIB_17162
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Protein kinase C isoforms involved in regulation of cell shape and locomotion of human fibrosarcoma HT1080 cells.
Périodique
International Journal of Cancer
Auteur(s)
Keller H.U., Hunziker I.P., Sordat B., Niggli V., Sroka J.
ISSN
0020-7136
Statut éditorial
Publié
Date de publication
2000
Volume
88
Numéro
2
Pages
195-203
Langue
anglais
Notes
Publication types: Journal Article
Résumé
The role of protein kinase C (PKC) isoforms in the regulation of cell shape [switch between fibroblast-like and crescent shape (CS)] and of locomotion of human fibrosarcoma HT1080 cells has been investigated. The PKC activator phorbol myristate acetate (PMA) induced the transition of elongated fibroblast-like cells into CS cells and stimulated locomotion. Both responses to PMA were inhibited by the PKC inhibitor Ro 31-8220. Analysis of the time course showed that stimulation of shape changes (formation of CS cells) and locomotor activity (increase in the proportion and speed of locomoting cells) was maximal in the early phase of the response (up to 2.5 hr) and significantly decreased later (15 to 21 hr). CS formation and stimulated locomotion correlated closely with a marked redistribution from the cytosol to the membrane of PKC isoforms alpha, beta1 and gamma in the early phase (0.5 to 2 hr) following activation with PMA. The subsequent reduction of the proportion of CS cells and of cell locomotion correlated with down-regulation of these isoforms in the second phase (16 to 21 hr). In contrast, the total amount and distribution of PKC beta2 remained almost unchanged with 10(-8) M PMA up to 21 hr. Furthermore, changes in shape and locomotion did not correlate with the responses of PKC delta to PMA. Inhibition of PMA-stimulated locomotion by the more specific inhibitor Gö 6976 is consistent with a role of PKC alpha and beta1 in this response. Ro 31-8220 alone induced a moderate down-regulation of PKC isoforms alpha and delta, but it also inhibited the more pronounced down-regulation of these isoforms by PMA. Our results indicate that activation of PKC isoforms alpha, gamma and beta1, but not beta2 or delta, stimulates locomotion and formation of CS cells in human fibrosarcoma HT1080 cells.
Mots-clé
Carbazoles/pharmacology, Cell Membrane/enzymology, Cell Movement/drug effects, Cell Movement/physiology, Cell Size/drug effects, Cell Size/physiology, Cytosol/enzymology, Enzyme Inhibitors/pharmacology, Fibrosarcoma, Humans, Indoles/pharmacology, Isoenzymes/metabolism, Kinetics, Protein Kinase C/metabolism, Protein Kinase C-alpha, Protein Kinase C-delta, Tetradecanoylphorbol Acetate/pharmacology, Time Factors, Tumor Cells, Cultured
Pubmed
Web of science
Open Access
Oui
Création de la notice
19/11/2007 13:10
Dernière modification de la notice
20/08/2019 13:46
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