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CD93 antigen (CD93) is a heavily glycosylated type I transmembrane glycoprotein encoded by the CD93 gene, consisting of 652 amino acids with a predicted mass of 68 kDa but migrating at 110-126 kDa due to glycosylation. It features a C-type lectin-like domain, epidermal growth factor-like repeats, mucin-like domain, transmembrane domain, and short cytoplasmic tail that interacts with moesin for cytoskeletal linkage. Expressed on hematopoietic stem cells, endothelial cells, monocytes, neutrophils, platelets, microglia, and B cell precursors, CD93 promotes cell adhesion, migration, phagocytosis of apoptotic cells and immune complexes, endothelial dynamics via MMRN2 and fibronectin interactions, and angiogenesis. Though initially thought to be a C1q receptor, direct interaction is unconfirmed; it regulates VEGFR2 and supports tumor vascularization in cancers like glioma and AML
antiangiogenic therapy by inhibiting endothelial cell proliferation migration and sprouting, targeting CD93 for AML cell proliferation inhibition
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