Hyaluronic acid proteoglycan interaction

Hardingham, T. E., Muir, H. The specific interaction of hyaluronic acid with cartilage proteoglycans. Biochim. Biophys. Acta 279, 401 (1972)... 

Link protein strengthens the noncovalent interaction between the core protein and hyaluronic acid in proteoglycan aggregates. 

Proteoglycan aggregates are typically found in the extracellular matrix of connective tissue. The noncovalent attachment of each proteoglycan to hyaluronic acid via the core protein is mediated by two linker proteins (not shown). Proteoglycans interact with numerous fibrous proteins in the extracellular matrix such as collagen, elastin, and fibronectin (a glycoprotein involved in cell adhesion). 

Figure 3 Proposed interactions between mechanical strain, proteoglycans (PGs), and transforming growth factor (TGF)-P in the extracellular environment of the airway wall. Excessive mechanical strain stimulates fibroblasts to increase PG secretion and deposition. The altered viscoelastic properties of the matrix subsequently modulate transmission of the mechanical signal to the airway structural cell and, thereby, protect the cell from mechanical strain-induced injury. In addition, increases in decorin may result in enhanced binding of TGF-P and thereby influence the effects of this cytokine on the fibroblast. Finally, changes in small PGs, such as decorin and lumican, may affect formation of collagen fibrils. CS, chondroitin sulfate HA, hyaluronic acid.

The electric birefringence technique has been shown to be suitable for investigations of cartilage proteoglycans and their interactions with hyaluronic acid. ... 

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