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Collagen type II alpha 1 chain (COL2A1) is the primary structural protein of hyaline cartilage and the vitreous humor, forming a triple-helical fibrillar network that provides tensile strength and resistance to compressive forces [4, 9, 12]. It is synthesized by chondrocytes and is essential for normal skeletal development and joint maintenance [6, 12]. Mutations in the COL2A1 gene cause a range of skeletal dysplasias, such as achondrogenesis and Kniest dysplasia, while its degradation is a key feature of osteoarthritis [1, 9, 15]. Additionally, COL2A1 serves as a major autoantigen in rheumatoid arthritis, where its post-translational modifications can trigger pathological immune responses [2, 5]. Therapeutic approaches include the use of undenatured type II collagen to induce oral tolerance, recombinant collagen for tissue engineering, and experimental gene-editing strategies to address genetic mutations [1, 2, 6]. The molecule also interacts with cell surface receptors like discoidin domain receptors (DDRs) and integrins to regulate chondrocyte behavior and matrix homeostasis [4, 11, 15].
Induction of oral tolerance via gut-associated lymphoid tissue to modulate autoimmune responses in rheumatoid arthritis; structural supplementation and promotion of chondrocyte matrix synthesis for cartilage repair [1, 2, 5, 6].
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