Abstract
Chondroitin sulfate (CS) and dermatan sulfate (DS) are widely distributed on the cell surface and in the extracellular matrix in the form of proteoglycan, where they participate in various biological processes. The diverse functions of CS/DS can be mainly attributed to their high structural variability. However, their structural complexity creates a big challenge for structural and functional studies of CS/DS. CS/DS-degrading enzymes with different specific activities are irreplaceable tools that could be used to solve this problem. Depending on the site of action, CS/DS-degrading enzymes can be classified as glycosidic bond-cleaving enzymes and sulfatases from animals and microorganisms. As discussed in this review, a few of the identified enzymes, particularly those from bacteria, have wildly applied to the basic studies and applications of CS/DS, such as disaccharide composition analysis, the preparation of bioactive oligosaccharides, oligosaccharide sequencing, and potential medical application, but these do not fulfill all of the needs in terms of the structural complexity of CS/DS.
Highlights
Unsaturated unitsGlcAβ1-3GalNAc GlcAβ1-3GalNAc(4S) glucuronic acid (GlcA)(2S)β1-3GalNAc(4S) GlcAβ1-3GalNAc(6S) GlcA(2S)β1-3GalNAc(6S) GlcAβ1-3GalNAc(4S,6S) GlcAβ1-3GalNAc(4S)
National Glycoengineering Research Center and Shandong Provincial Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Jinan, China
As the side chains of PGs, Chondroitin sulfate (CS) is composed of repeating disaccharides consisting of D-glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) with different sulfation patterns, once the GlcA residues are isomerized to L-iduronic acid (IdoA) residues CS is converted to dermatan sulfate (DS), called CS-B, and CS and DS domains are usually detected in one chain as co-hybrid structure CS/DS (Sugahara et al, 2003; Figure 1)
Summary
GlcAβ1-3GalNAc GlcAβ1-3GalNAc(4S) GlcA(2S)β1-3GalNAc(4S) GlcAβ1-3GalNAc(6S) GlcA(2S)β1-3GalNAc(6S) GlcAβ1-3GalNAc(4S,6S) GlcAβ1-3GalNAc(4S). The CSase AC I from Flavobacterium heparinum and CSase AC II from Arthrobacter aurescens are well-known CS/DS lyases showing endolytic and exolytic activities, respectively (Yamagata et al, 1968; Hiyama and Okada, 1975). The CSase B from Flavobacterium heparinum is the only commercialized lyase with specific endolytic activity to DS (Yamagata et al, 1968). C26 and Sphingomonas paucimobilis, respectively, both of which have lower molecular weights but similar broad-spectrum activities against CS, DS and HA compared with CSase ABC (Zhu et al, 2017; Fu et al, 2018) Most of these studies have mainly focused on Frontiers in Cell and Developmental Biology | www.frontiersin.org
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