## Background: Integrins are major adhesion receptors that not only regulate cytoskeletal organization, but also trigger a variety of intracellular signal transduction pathways. we examined the effects of increased extracellular matrix (ecm) accumulation on monocyte chemoattractant protein-1 (mcp-1
Degradation of focal adhesion proteins during nocodazole-induced apoptosis in rat-1 cells
β Scribed by Seunghyi Kook; Sang Ryeol Shim; Jae Il Kim; Joo Hong Ahnn; Yong Keun Jung; Sang Gi Paik; Woo Keun Song
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 249 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0263-6484
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β¦ Synopsis
Nocodazole, a microtubule-disrupting agent, induced apoptosis in Rat-1 cells, as indicated by changes in cell morphology, DNA fragmentation, and eventual cell death. During nocodazole-induced apoptosis, normally Β―at cells became rounded in shape and detached from the extracellular matrix. These morphological changes appeared to be closely associated with degradation of focal adhesion proteins, including p130cas, p125 FAK and paxillin. p130cas was also degraded in cells treated with staurosporine or etoposide, suggesting that degradation of focal adhesion proteins is a characteristic feature of apoptosis. Nocodazole-induced apoptosis was antagonized by Bcl-2: degradation of focal adhesion proteins was suppressed and cell viability was enhanced in bcl-2 over-expressing cells, even in the presence of nocodazole. Further study of the molecular mechanism of Bcl-2 activation should provide an understanding of the apoptosis induced by disruption of the microtubule network.
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