4.5 Article

Cleavage of tensin during cytoskeleton disruption in YTX-induced apoptosis

Journal

TOXICOLOGY IN VITRO
Volume 21, Issue 1, Pages 9-15

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.tiv.2006.07.012

Keywords

tensin; yessotoxin; apoptosis; F-actin cytoskeleton; fibrillar adhesions; focal adhesion complexes

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Yessotoxin (YTX) is a marine algal toxin previously shown to induce apoptosis in L6 and BC3H1 myoblast cell lines. Disassembly of the F-actin cytoskeleton and cleavage of tensin, a cytoskeletal protein localised at the focal adhesion contacts, appear during this apoptotic process. Tensin binds to actin filaments at the focal adhesion contacts and it links the actin cytoskeleton to the extracellular matrix (ECM). This binding occurs via integrin receptors and it makes tensin a potential link between the actin cytoskeleton and signal transduction. This study evaluates disruption in the F-actin cytoskeleton and change of tensin in myoblast cell lines exposed to 100 nM YTX up to 72 h. YTX treatment cleaves tensin and makes it translocate to the cell centre. Tensin has normally a role in the maintenance of cell shape and YTX-treatment may therefore alter the shape of the cells. YTX exposure also induces formation of lamellas associated with pseudopodia. Alternative linkages and cytoskeletal proteins anchoring the actin filaments to focal contacts remain to be identified. (c) 2006 Elsevier Ltd. All rights reserved.

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