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Gliomedin is a cell adhesion protein encoded by the GLDN gene and contains both olfactomedin-like and collagen-like domains[5][6][7]. It exists in both transmembrane and secreted forms and is a crucial ligand for neuronal cell adhesion molecules NRCAM and neurofascin[3][4][6][7]. Gliomedin is primarily expressed by myelinating Schwann cells at the nodes of Ranvier in the peripheral nervous system, where it orchestrates the molecular assembly and maintenance of these nodes by mediating the interactions between Schwann cell microvilli and axonal proteins, which is essential for clustering sodium channels required for saltatory action potential conduction[3][4][6][7]. Mutations in GLDN cause lethal congenital contracture syndrome 11 in humans, and autoantibodies targeting gliomedin are associated with multifocal motor neuropathy[5][6]. There are currently no known direct pharmacological inhibitors or therapeutics targeting gliomedin, but it serves as a disease biomarker and potential target in certain neuropathic conditions[6].
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