ADAMTS14 Knockout PaTu 8988t Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout population in the pancreatic cancer line PaTu 8988t, targeting the ADAMTS14 gene. This loss-of-function model enables study of ADAMTS14-dependent extracellular matrix remodeling and collagen processing. The polyclonal format provides a heterogeneous edited allele pool without clonal selection, suitable for metastatic pancreatic cancer research where ADAMTS14 procollagen N-proteinase activity is key for collagen fibril assembly and tumor microenvironment dynamics.
Derived from a liver metastasis, PaTu 8988t is a pancreatic ductal adenocarcinoma cell line that models metastatic disease. These epithelial cells retain invasive traits and altered matrix interactions, making them ideal for investigating matrix remodeling, adhesion, and signaling in pancreatic cancer. Their metastatic origin provides a relevant context for studying how ADAMTS14 depletion affects tumor cell behavior within the collagen-rich metastatic niche.
ADAMTS14 is a procollagen N-proteinase that cleaves N-propeptides of fibrillar procollagens (types I/II/III), essential for collagen fibril assembly. Its activity is regulated by TGF-??, IL-1??, and mechanical stress. Downstream, collagen maturation influences integrin ??2??1 adhesion, while ADAMTS14 interacts with heparan sulfate proteoglycans and TIMP-3. In TGF-?? signaling, ADAMTS14 impacts Smad2/3 phosphorylation, linking matrix processing to transcriptional programs driving epithelial-mesenchymal transition and tumor progression.
In PaTu 8988t, ADAMTS14 knockout likely impairs procollagen cleavage, causing defective fibrillogenesis and altered matrix, potentially reducing adhesion, migration, and invasion. Given the desmoplastic stroma of pancreatic tumors, loss of ADAMTS14 may diminish integrin ??2??1 signaling by limiting mature collagen ligands, attenuating survival and motility pathways. Thus, this polyclonal knockout is a valuable tool for dissecting ADAMTS14’s metastatic role and testing matrix-targeting therapies.
Applications include collagen processing assays, Western blotting, migration/invasion assays, collagen immunofluorescence, and RT-qPCR for collagen genes. This model supports extracellular matrix remodeling, tumor microenvironment, collagen maturation, and metastasis research. It also enables exploration of ADAMTS14-mediated TGF-?? and integrin signaling. For further details, contact Ascent Research.
