Metastatic cancer cells use the actin-bundling process to constantly remodel the actin cytoskeleton for adhesion, migration, and invasion. L-plastin is an actin-bundling protein that belongs to the plastin family. L-plastin has been identified in several malignant tumors of the colon, prostate, and breast and contributes to cancer cell invasion in a phosphorylation-dependent manner. Our initial characterization in PC3 prostate cancer (PCa) cell line derived from bone metastases demonstrated L-plastin expression in PCa cells but not in other PCa cell lines tested. Hence, this study aimed to identify L-plastin’s role in the migration and invasion of PC3 cells. Immunostaining analysis demonstrated a punctate distribution of L-plastin and patchy actin staining in PC3 cells with a minimal colocalization between L-plastin and actin at the invadopodia. However, L-plastin overexpression in PC3 cells increased L-plastin’s colocalization and actin at the invadopodia and during the invasion. In a wound-healing assay, these cells displayed a significant reduction in migration. L-plastin and invadopodia connections were confirmed using the L-plastin knockdown strategy in PC3 cells (PC3/Si). PC3/Si cells demonstrated an increased migration, which corresponded to punctate podosome-like structures. However, a decrease in the number of invadopodia contributed to a significant reduction in the invasion. Additionally, tumorsphere formation was significantly reduced in PC3/Si cells than in PC3 cells. In conclusion, our observations suggest that L-plastin regulates the formation of invadopodia required for prostate cancer invasion. Our results highlight that it could be a novel therapeutic target for androgen-independent metastatic prostate cancer.Up to 350 words. No references allowed. Abstracts may be submitted at a later date.

- Journal
- Articles
- Author Center
- Society
Editorial Board
The ESMED Editorial Board is comprised of experts from around the world.
Meet the community
See what our members have been working on.
Membership
Join ESMED for access to member-only content, congress discounts, and more.
- Policy