Laminin-111 peptide C16 regulates invadopodia activity of malignant cells through β1 integrin, Src and ERK 1/2.

Siqueira AS, Pinto MP, Cruz MC, Smuczek B, Cruz KS, Barbuto JA, Hoshino D, Weaver AM, Freitas VM, Jaeger RG
Oncotarget. 2016 7 (30): 47904-47917

PMID: 27323814 · PMCID: PMC5216987 · DOI:10.18632/oncotarget.10062

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.

MeSH Terms (14)

Carcinoma, Squamous Cell Cell Line, Tumor Fibrosarcoma Head and Neck Neoplasms Humans Integrin beta1 Laminin MAP Kinase Signaling System Mouth Neoplasms Peptide Fragments Podosomes Squamous Cell Carcinoma of Head and Neck src-Family Kinases Transfection

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