The ADAMTS14 Knockout UM-UC-3 Polyclonal Cells constitute a heterogeneous population of UM-UC-3 bladder carcinoma cells modified by CRISPR/Cas9 to disrupt the ADAMTS14 gene. As a polyclonal knockout product, this population avoids clonal selection artifacts and provides a direct loss-of-function model for studying ADAMTS14-dependent processes in the native UM-UC-3 background.
The UM-UC-3 cell line, a human bladder transitional cell carcinoma isolate from a male patient, exhibits epithelial morphology and harbors wild-type TP53 along with an activating FGFR3 mutation. This genetic profile is representative of a subset of bladder cancers and supports investigation of oncogenic signaling, ECM biology, and matrix-dependent tumor cell behavior.
ADAMTS14 is a secreted procollagen N-propeptidase that cleaves the N-propeptide of procollagen I, enabling proper collagen fibril assembly and ECM maturation. It is transcriptionally regulated by TGFB1, IL1B, TNF, and mechanical stress, and its activity influences downstream effectors such as mature collagen type I fibers, ECM stiffness, and integrin-mediated adhesion. The protein interacts with procollagen I, collagen type I, and heparan sulfate proteoglycans, and participates in a pathway comprising TGF-beta, SMAD2/3, and integrin alpha2beta1.
In the UM-UC-3 bladder carcinoma context, ADAMTS14 disruption is expected to perturb procollagen I processing, yielding altered collagen fiber organization, modified ECM stiffness, and changed integrin signaling. These ECM alterations are particularly relevant to bladder cancer progression, where matrix remodeling supports invasion and metastasis. This polyclonal knockout model thus allows dissection of ADAMTS14’s role in tumor cell?CECM crosstalk and may inform studies of fibrotic ECM pathologies.
This knockout population is suitable for analyzing ECM composition through western blotting of procollagen I processing products, immunofluorescence of collagen fibers, and sirius red staining. Functional assays such as cell adhesion, migration, and RT-qPCR profiling of ECM-related genes can explore consequences of ADAMTS14 loss. Mass spectrometry-based proteomics can identify ADAMTS14 substrates and ECM changes, while the cells can be used to screen compounds targeting collagen processing or integrin-dependent signaling. Please contact Ascent Research for further information.
