Abstract
Laminin peptides influence tumor behavior. In this study, we addressed whether laminin peptide C16 (KAFDITYVRLKF, γ1 chain) would increase invadopodia activity of cells from squamous cell carcinoma (CAL27) and fibrosarcoma (HT1080). We found that C16 stimulates invadopodia activity over time in both cell lines. Rhodamine-conjugated C16 decorates the edge of cells, suggesting a possible binding to membrane receptors. Flow cytometry showed that C16 increases activated β1 integrin, and β1 integrin miRNA-mediated depletion diminishes C16-induced invadopodia activity in both cell lines. C16 stimulates Src and ERK 1/2 phosphorylation, and ERK 1/2 inhibition decreases peptide-induced invadopodia activity. C16 also increases cortactin phosphorylation in both cells lines. Based on our findings, we propose that C16 regulates invadopodia activity over time of squamous carcinoma and fibrosarcoma cells, probably through β1 integrin, Src and ERK 1/2 signaling pathways.
Highlights
During tumor progression and metastasis, neoplastic cells may detach from primary tumors and migrate into surrounding tissues and blood vessels [1]
We addressed whether laminin peptide C16 (KAFDITYVRLKF, γ1 chain) would increase invadopodia activity of cells from squamous cell carcinoma (CAL27) and fibrosarcoma (HT1080)
A fluorescent extracellular matrix (ECM) substrate degradation assay showed that C16 increased invadopodia activity in both CAL27 (Figure 1A) and HT1080 (Figure 2A) cells
Summary
During tumor progression and metastasis, neoplastic cells may detach from primary tumors and migrate into surrounding tissues and blood vessels [1]. These events involve tumor cell interactions with extracellular matrix (ECM) and basement membrane, a specialized structure composed mainly of laminins, type IV collagen, nidogen, and heparan sulfate proteoglycans [2]. Matrix metalloproteinases (MMPs) are crucial for basement membrane degradation and tumor dissemination [3, 4]. These enzymes release protein domains with bioactive activities [5]. Fragments and bioactive peptides can be found in most extracellular matrix proteins [6, 7]
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