ADP-ribosylation of Rho-proteins with botulinum C3 exoenzyme inhibits invasion and schape changes of T-lymphoma cells.

Hendrik Verschueren, Patrick De Baetselier, Jos De Braekeleer, Joëlle Dewit, Klaus Aktories, Ingo Just

Research output: Contribution to journalArticle

23 Citations (Scopus)


C3 exoenzyme from Clostridium botulinum ADP-ribosylates the small GTP-binding protein Rho with a high specificity. The use of C3 has shown that Rho-mediated signaling is involved in the regulation of actin-dependent processes in various cell types. In order to investigate the role of Rho-proteins in lymphocyte crawling, we have analyzed the effects of C3 on a T-cell line derived from the murine BW5147 lymphoma. Pretreatment of the lymphoma cells with C3, in conditions where Rho was actually ADP-ribosylated, strongly inhibited the characteristic shape changes resulting from extension and retraction of pseudopodia. Concomitantly, invasion of the cells through a monolayer of fibroblast-like cells was also inhibited. C3-treatment did not affect the total F-actin content of the cells, as measured by flow cytometry of cells stained with phalloidin. Yet, microscopical observation revealed that the accumulations of F-actin, which were seen in the pseudopodia of untreated cells, were absent after treatment with C3. This suggests that C3 may affect actin polymerization locally. The inhibitory effect of C3 on invasion was not restricted to the murine BW5147 lymphoma cell line, as it occurred also with CCRF-CEM, a human T-cell lymphoma line. Our results demonstrate that invasion-bound motility of lymphocytes depends on a Rho-mediated signal transduction pathway.
Original languageEnglish
Pages (from-to)182-187
JournalEuropean Journal of Cell Biology
Issue number2
Publication statusPublished - 1997

Bibliographical note

European Journal of Cell Biology, 73, 182-187.

Fingerprint Dive into the research topics of 'ADP-ribosylation of Rho-proteins with botulinum C3 exoenzyme inhibits invasion and schape changes of T-lymphoma cells.'. Together they form a unique fingerprint.

Cite this