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Latexin (LXN) is the only known mammalian carboxypeptidase inhibitor, structurally unrelated to plant/parasite carboxypeptidase inhibitors, but related to the tumor suppressor TIG1. It is ubiquitously expressed in cytoplasm and nucleus across various tissues, including brain and prostate, and is inducible by retinoic acid. LXN can be secreted non-classically and primarily functions to inhibit specific carboxypeptidases (CPA1, CPA2, CPA4), modulate inflammation, and suppress cell motility, invasiveness, and clonogenic potential in cancer models. Loss or downregulation of LXN is associated with poor cancer prognosis and increased tumor aggressiveness, marking LXN as a potential biomarker and therapeutic target. Despite its important roles in cancer, inflammation, and stem cell regulation, the full biological role of LXN is not completely characterized.
Enzyme inhibition (Drugs or interventions that modulate LXN would act by altering carboxypeptidase activity, leading to downstream changes in protease-regulated cell processes)
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