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NRP2-Mo83 is a novel, soluble splice isoform of the non-tyrosine kinase receptor Neuropilin-2 (NRP2). Identified in high-expressing tumor cell lines and human serum, this isoform is characterized as a monomeric secreted protein, distinguishing it from the dimeric soluble isoform s9NRP2. Recombinant NRP2-Mo83 exhibits significant antiangiogenic and antitumorigenic properties, demonstrating dose-dependent inhibition of tumor cell growth in bladder carcinoma and inhibition of human endothelial cell (HUVEC) proliferation. The protein undergoes extensive post-translational modifications, including N- and O-glycosylation and polysialation, and its structure is stabilized by calcium ions. NRP2-Mo83 appears to be downregulated during bladder tumorigenesis, suggesting a potential role as an endogenous tumor suppressor and a candidate for therapeutic development in oncology.
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