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The lectican family, also known as hyalectans, comprises a group of four chondroitin sulfate proteoglycans (CSPGs): aggrecan, versican, neurocan, and brevican (Yamaguchi, 2000, PMID: 11030571). These proteins are defined by a conserved structural motif consisting of an N-terminal hyaluronan-binding domain and a C-terminal C-type lectin domain, which allow them to bridge various components of the extracellular matrix (ECM) (Aspberg, 2012, PMID: 22535304). Lecticans play pivotal roles in tissue development, cell adhesion, and axon guidance, particularly within the central nervous system and cartilage. In pathological contexts, such as spinal cord injury, neurocan and brevican are major components of the glial scar that inhibits axonal regeneration (Silver & Miller, 2004, PMID: 14758387). Conversely, versican is often upregulated in the tumor microenvironment, where it facilitates cancer cell proliferation and metastasis (Wight, 2017, PMID: 28456614). Therapeutic interventions currently focus on the enzymatic degradation of lectican glycosaminoglycan chains using chondroitinase ABC or the development of antibodies to neutralize specific domains, aiming to restore neural plasticity or inhibit tumor progression (Bradbury & Carter, 2011, PMID: 21691333).
Enzymatic degradation of chondroitin sulfate glycosaminoglycan chains or inhibition of upstream signaling pathways (e.g., TGF-beta, PDGF) to reduce proteoglycan expression and bioactivity.
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