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TGF-alpha-induced breakdown of stress fibers and degradation of tropomyosin in NRK cells is blocked by a proteasome inhibitor.

Abstract：

:Treatment of NRK cells with TGF-alpha in the presence of serum initiates disassembly of cytoskeletal stress fibers and suppresses the synthesis of tropomyosin isoforms (TMs) 1, 2, and 3 but not TMs 4 and 5 (Cooper et al., Cancer Res. 47, 4493-4500, 1987). In order to determine how the loss of tropomyosin is induced and what role it plays in cytoskeletal disruption, the turnover of tropomyosin was studied in the presence of the transforming growth factor and protease inhibitors. Cells were pulse-labeled with [35S]methionine and chased in the absence or the presence of the growth factor. It was found that TMs 1, 2, and 3 are degraded at about twice the rate of TMs 4 and 5 in control cells and that the rate of degradation of TMs 1-3 is accelerated by the growth factors. Degradation of TMs in control and growth factor-treated cells is blocked by a membrane-permeable inhibitor of cysteine proteases (LLnL) that acts upon calpains and proteasomes, and the cells maintain a flattened shape with a normal complement of stress fibers. Application of inhibitors that block calpains but not proteasomes does not block TM degradation. Treatments (suspension culture or cytochalasin B) that disrupt stress fibers without application of the growth factors also accelerate TM degradation, suggesting that acceleration of TM degradation is a consequence of its release from stress fibers during their breakdown. The normally more rapid turnover of the TM isoforms 1-3 that are lost in the phenotypically transformed cells could serve to facilitate the cytoskeletal reorganization that follows the activation of signal transduction pathways by the transforming growth factors observed in this study or during other rearrangements of the cytoskeleton such as occur during cell migration or mitosis.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Warren RH

doi

10.1006/excr.1997.3728

subject

Has Abstract

pub_date

1997-10-10 00:00:00

pages

294-303

issue

1

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(97)93728-9

journal_volume

236

pub_type

杂志文章

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