LMO7, or LIM domain only 7, is a multifunctional protein involved in various biological processes. It acts as an E3 ubiquitin ligase and is associated with pathways like TGF-β signaling, glycolysis regulation, and is crucial for maintaining normal cellular functions and tissue homeostasis [1,2,4]. Genetic models, such as gene knockout (KO) mouse models, have been instrumental in studying its functions.

In macrophage-related studies, LMO7 deficiency in macrophages facilitated inflammatory injury in murine colitis. LMO7 directly degraded PFKFB3, inhibiting glycolysis and macrophage activation, indicating its role in modulating macrophage function and IBD pathogenesis [1].

In vascular smooth muscle cells, global or smooth muscle-specific LMO7 deletion in mice enhanced neointimal formation, TGF-β signaling, and ECM deposition, showing its negative feedback regulation of the TGF-β pathway in vascular fibrosis [2].

In pancreatic cancer, LMO7 knockdown or knockout in mouse PC cells significantly suppressed cell proliferation, colony formation, and mobility in vitro and tumor growth and metastasis in vivo, suggesting it promotes cancer progression [3].

In pulmonary fibrosis, knockdown of LMO7 in mice impaired the profibrotic phenotype of fibroblasts, and AAV-mediated Lmo7 shRNA ameliorated BLM-induced lung fibrosis, highlighting its role in driving profibrotic fibroblast polarization [4].

In conclusion, LMO7 plays essential roles in regulating multiple biological processes and is involved in various disease conditions. The use of KO/CKO mouse models has revealed its significance in inflammatory bowel disease, vascular fibrosis, pancreatic cancer, and pulmonary fibrosis, providing insights into potential therapeutic targets for these diseases.