The ITGB3 Knockout CAL-27 Polyclonal Cells product provides a CRISPR/Cas9-edited polyclonal population of CAL-27 human tongue squamous cell carcinoma cells harboring a disrupted ITGB3 gene. This loss-of-function model enables studies of integrin ??3 ablation in an epithelial tumor context without clonal selection, preserving population heterogeneity and reflecting a broad spectrum of editing outcomes across the cell pool.
The parental CAL-27 cell line was originally derived from a tongue squamous cell carcinoma of a 56-year-old male patient. It is widely utilized as a model system for oral cancer research, including investigations of tumor cell adhesion, invasion, and drug response, owing to its well-characterized epithelial phenotype and growth characteristics.
ITGB3 encodes the integrin ??3 subunit, which pairs primarily with ??v (forming ??v??3) or ??IIb to bind extracellular matrix ligands including vitronectin, fibronectin, and fibrinogen. Upon ligand engagement, the integrin recruits talin and kindlin-3, leading to FAK phosphorylation and downstream activation of Src, PI3K/Akt, and MAPK/ERK cascades. These signals regulate Rho GTPases such as Rac1 and RhoA, and influence transcription factors like AP-1 and ETS1, ultimately affecting cell migration, proliferation, and survival. ITGB3 expression is itself regulated by TGF-??, SP1, and ETS1, and the integrin physically interacts with ITGAV, talin, kindlin-3, ??3-endonexin, and other focal adhesion components including vinculin and paxillin.
In CAL-27 oral squamous cell carcinoma cells, ??v??3 integrin contributes to tumor cell adhesion, migration, and invasive behavior. Disruption of ITGB3 abrogates ??v??3-mediated attachment to vitronectin and fibronectin, attenuating FAK and Akt phosphorylation and impairing downstream pro-migratory pathways. This model thus provides a relevant system to dissect the role of integrin ??3 in oral cancer progression, angiogenesis, and potential resistance mechanisms.
Researchers can employ these polyclonal knockout cells in a variety of functional assays, including vitronectin adhesion assays, wound healing and transwell migration studies, and phospho-signaling analyses by Western blotting to probe FAK, Akt, and ERK activation. The cells are suitable for immunofluorescence imaging of focal adhesion dynamics, flow cytometric assessment of integrin surface expression, and co-immunoprecipitation of integrin complexes. Additionally, they can be utilized in xenograft tumor models to evaluate metastatic potential and in drug sensitivity screens for agents targeting integrin signaling, such as cilengitide. For further information, please contact Ascent Research.
