Molecular structure of the ground substance of hyaline cartilage.

This schematic diagram shows the relationship of hyaluronate proteoglycan aggregates to type II collagen fibrils and chondrocytes in the ground substance of hyaline cartilage. A hyaluronic acid molecule forming a linear aggregate with many proteoglycan monomers joined to a core protein to form a proteoglycan monomer (Fig. 7.1). Each linear hyaluronic acid molecule is associated with approximately 80 proteoglycan monomers, which are bound to the hyaluronic acid by link proteins to form large hyaluronate proteoglycan aggregates. These aggregates are bound to the thin collagen matrix fibrils by electrostatic interactions and cross-linking glycoproteins.

• Noncollagenous proteins. The cartilage matrix also contains other proteoglycans that do not form aggregates, as well as noncollagenous and nonproteoglycan-1 inked glycoproteins. These small regulatory and structural proteins influence interactions between the chondrocytes and the matrix and have clinical value as markers of cartilage turnover and degeneration. Examples of such proteins are anchorin CII, tenascin, and fibronectin, which help anchor chondrocytes to the matrix.

\__-—--------isogenous group is interwoven with a network of collagen fibrils. Proteoglycan monomers are linked electrostatically to the collagen fibrils as well as by cross-linking glycoproteins. Chondrocytes, the principal cells of hyaline cartilage, appear in isogenous groups.

proteoglycan monomer collagen type chondrocyte proteoglycan monomer collagen type chondrocyte

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