Abstract
Chondroitin sulfate (CS) and dermatan sulfate (DS) are linear anionic polysaccharides that are widely present on the cell surface and in the cell matrix and connective tissue. CS and DS chains are usually attached to core proteins and are present in the form of proteoglycans (PGs). They not only are important structural substances but also bind to a variety of cytokines, growth factors, cell surface receptors, adhesion molecules, enzymes and fibrillary glycoproteins to execute series of important biological functions. CS and DS exhibit variable sulfation patterns and different sequence arrangements, and their molecular weights also vary within a large range, increasing the structural complexity and diversity of CS/DS. The structure-function relationship of CS/DS PGs directly and indirectly involves them in a variety of physiological and pathological processes. Accumulating evidence suggests that CS/DS serves as an important cofactor for many cell behaviors. Understanding the molecular basis of these interactions helps to elucidate the occurrence and development of various diseases and the development of new therapeutic approaches. The present article reviews the physiological and pathological processes in which CS and DS participate through their interactions with different proteins. Moreover, classic and emerging glycosaminoglycan (GAG)-protein interaction analysis tools and their applications in CS/DS-protein characterization are also discussed.
Highlights
Chondroitin sulfate (CS) and dermatan sulfate (DS) are acidic linear anionic polysaccharides in the glycosaminoglycan (GAG) family
The difference between the DS chain and CS chain is that the GlcA is epimerized to iduronic acid (IdoA) in the DS, and the CS and DS structures are usually found in a single CS-DS hybrid polysaccharide chain (Sugahara et al, 2003)
The results show that hepatocyte growth factor (HGF)/scatter factor (SF), KGF/fibroblast growth factor (FGF)-7 and heparin cofactor II (HCII) can preferentially bind to DS oligosaccharide fragments longer than 8-mers, while the binding of RANTES depends on the strength of the charge (Yamaguchi et al, 2006)
Summary
Reviewed by: Dalit Sela-Donenfeld, The Hebrew University of Jerusalem, Israel Chao Cai, Ocean University of China, China Zhongfu Wang, Northwest University, China. CS and DS chains are usually attached to core proteins and are present in the form of proteoglycans (PGs). They are important structural substances and bind to a variety of cytokines, growth factors, cell surface receptors, adhesion molecules, enzymes and fibrillary glycoproteins to execute series of important biological functions. CS and DS exhibit variable sulfation patterns and different sequence arrangements, and their molecular weights vary within a large range, increasing the structural complexity and diversity of CS/DS. The structure-function relationship of CS/DS PGs directly and indirectly involves them in a variety of physiological and pathological processes. The present article reviews the physiological and pathological processes in which CS and DS participate through their interactions with different proteins.
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