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Chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycan (GAG) chains are complex, linear polysaccharides covalently attached to core proteins to form chondroitin sulfate proteoglycans (CSPGs). These chains are major components of the extracellular matrix (ECM) and the perineuronal nets in the central nervous system, where they play a dual role in maintaining structural integrity and regulating cell signaling through interactions with growth factors and surface receptors. In the context of injury, particularly spinal cord and brain trauma, CS/DS GAGs are upregulated by reactive astrocytes to form a glial scar, which acts as a potent physical and chemical barrier to axonal regeneration. In oncology, altered sulfation patterns of these GAG chains are frequently observed, contributing to tumor cell proliferation, adhesion, and metastasis by modulating the tumor microenvironment. Therapeutic interventions typically involve the use of chondroitinase enzymes to degrade these chains or the development of small molecules and antibodies to block their inhibitory or pro-tumorigenic interactions.
Enzymatic degradation of the polysaccharide chains to remove inhibitory signals; competitive binding to block growth factor or receptor interactions; inhibition of GAG chain biosynthesis or sulfation.
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