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Keratan sulfate (KS), also called keratosulfate, is any of several sulfated glycosaminoglycans that have been found especially in the cornea, cartilage, and bone. It is also synthesized in the central nervous system where it participates both in development and in the glial scar formation following an injury. Keratan sulfates are large, highly hydrated molecules which in joints can act as a cushion to absorb mechanical shock.
Chondroitinase treatment is a treatment of proteoglycans, a protein in the fluid among cells where they affect neural activity. Chondroitinase treatment has been shown to allow adults vision to be restored as far as ocular dominance is concerned. Moreover, there is some evidence that Chondroitinase could be used for the treatment of spinal injuries.
Syndecan-4 is a protein that in humans is encoded by the SDC4 gene. Syndecan-4 is one of the four vertebrate syndecans and has a molecular weight of ~20 kDa. Syndecans are the best-characterized plasma membrane proteoglycans. Their intracellular domain of membrane-spanning core protein interacts with actin cytoskeleton and signaling molecules in the cell cortex. Syndecans are normally found on the cell surface of fibroblasts and epithelial cells. Syndecans interact with fibronectin on the cell surface, cytoskeletal and signaling proteins inside the cell to modulate the function of integrin in cell-matrix adhesion. Also, syndecans bind to FGFs and bring them to the FGF receptor on the same cell. As a co-receptor or regulator, mutated certain proteoglycans could cause severe developmental defects, like disordered distribution or inactivation of signaling molecules.
In enzymology, a chondroitin 4-sulfotransferase is an enzyme that catalyzes the chemical reaction
The enzyme chondroitin AC lyase catalyzes the chemical reaction
The enzyme chondroitin B lyase catalyzes the following process:
The enzyme chondroitin-sulfate-ABC exolyase catalyzes the following process:
The enzyme heparin-sulfate lyase catalyzes the chemical reaction
The enzyme chondro-4-sulfatase (EC 3.1.6.9) catalyzes the reaction
The enzyme chondro-6-sulfatase (EC 3.1.6.10) catalyzes the reaction
Matrix metalloproteinase-16 is an enzyme that in humans is encoded by the MMP16 gene.
Carbohydrate sulfotransferase 2 is an enzyme that in humans is encoded by the CHST2 gene.
Carbohydrate sulfotransferase 1 is an enzyme that in humans is encoded by the CHST1 gene.
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in humans is encoded by the B3GAT3 gene.
Carbohydrate sulfotransferase 15 is an enzyme that in humans is encoded by the CHST15 gene. It belongs to the N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase enzyme class.
Galactose-3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the GAL3ST2 gene.
Carbohydrate sulfotransferase 7 is an enzyme that in humans is encoded by the CHST7 gene.
Unsaturated chondroitin disaccharide hydrolase (EC 3.2.1.180, UGL, unsaturated glucuronyl hydrolase) is an enzyme with systematic name beta-D-4-deoxy-Delta4-GlcAp-(1->3)-beta-D-GalNAc6S hydrolase. This enzyme catalyses the following chemical reaction
Chondroitin ABC lyase is an enzyme with systematic name chondroitin ABC lyase. This enzyme catalyses the following chemical reaction
Ulvan lyase is an enzyme found within the cell-wall of the marine organism Ulvales, and some marine bacterium. A lyase is a class of enzyme that catalyzes the breakdown of chemical bonds through an elimination reaction mechanism, rather than a substitution reaction mechanism. Ulvan lyase belongs to the polysaccharide lyase family, a type of enzyme that primarily functions to cleave glycosidic linkages in polysaccharides.
References
- Yamagata T, Saito H, Habuchi O, Suzuki S (1968). "Purification and properties of bacterial chondroitinases and chondrosulfatases". J. Biol. Chem. 243 (7): 1523–35. PMID 5647268.
- Saito H, Yamagata T, Suzuki S (1968). "Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates". J. Biol. Chem. 243 (7): 1536–42. PMID 4231029.
- Suzuki S, Saito H, Yamagata T, Anno K, Seno N, Kawai Y, Furuhashi T (1968). "Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion". J. Biol. Chem. 243 (7): 1543–50. PMID 5647269.
- Suzuki S; Hashimoto, N; Mochizuki, H; Kato, F; Makiguchi, Y; Horie, K; Suzuki, S (1997). "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides". J. Biol. Chem. 272 (14): 9123–30. doi: 10.1074/jbc.272.14.9123 . PMID 9083041.
- Lauder RM; Nieduszynski, IA; Giannopoulos, M; Weeks, SD; Sadler, IH; Lauder, RM (2005). "Characterization of oligosaccharides from the chondroitin/dermatan sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and hexasaccharides". FEBS J. 272 (24): 6276–86. doi:10.1111/j.1742-4658.2005.05009.x. PMID 16336265.
