Glycosaminoglycan Degradation

Kresse, Hans; GlüSSL, Josef

doi:10.1002/9780470123065.ch4

Cited by 22 publications

(12 citation statements)

References 484 publications

(125 reference statements)

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“…How are CS chains systemically degraded under physiological conditions? Since HYAL1 is ubiquitously expressed and can degrade CS chains to only a limited extent [7,8,9], we estimated that it might depolymerize CS chains under specific pH conditions or by forming a complex with some other assistant protein(s). In fact, the HA-degrading activity of HYAL2 at pH 6.0-7.0 was detected only when the enzyme was co-expressed with CD44 [26].…”

Section: Discussionmentioning

confidence: 99%

“…Hyaluronan (HA)-degrading enzymes, hyaluronidases, are considered to act at the initial stage of the degradation process, because HA is similar in structure to nonsulfated CS, chondroitin (Chn) (Figure 1). Since some hyaluronidases can degrade not only HA but also CS [7,8,9], the cellular degradation of CS is considered to be executed by hyaluronidases. …”

Section: Introductionmentioning

confidence: 99%

“…Although hyaluronidase-1 (HYAL1) and testicular hyaluronidase (SPAM1) have been reported to degrade CS chains to some extent [7,8,9,14,15], their activity toward CS has not been determined precisely. The preferred substrate of HYAL1 and SPAM1 is considered to be HA rather than CS, but the kinetic parameters of these enzymes toward HA and CS have not been compared.…”

Section: Introductionmentioning

confidence: 99%

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Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan

et al. 2012

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Chondroitin sulfate (CS) chains are involved in the regulation of various biological processes. However, the mechanism underlying the catabolism of CS is not well understood. Hyaluronan (HA)-degrading enzymes, the hyaluronidases, are assumed to act at the initial stage of the degradation process, because HA is similar in structure to nonsulfated CS, chondroitin (Chn). Although human hyaluronidase-1 (HYAL1) and testicular hyaluronidase (SPAM1) can degrade not only HA but also CS, they are assumed to digest CS to only a limited extent. In this study, the hydrolytic activities of HYAL1 and SPAM1 toward CS-A, CS-C, Chn, and HA were compared. HYAL1 depolymerized CS-A and HA to a similar extent. SPAM1 degraded CS-A, Chn, and HA to a similar extent. CS is widely distributed from very primitive organisms to humans, whereas HA has been reported to be present only in vertebrates with the single exception of a mollusk. Therefore, a genuine substrate of hyaluronidases appears to be CS as well as HA.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan

et al. 2012

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“…Exoglycosidases have selective activity towards only one anomeric form of glycosidic bond [16,17]. The exoglycosidases are involved in successive reactions, in which the product of a former reaction is the substrate of the following one [18][19][20][21]. Exoglycosidase activity of knee synovial fluid and serum of healthy individuals is demonstrated in Table 1 [22].…”

Section: Synovial Fluid Markers In Ra (Rheumatoid Arthritis) and Oa (mentioning

confidence: 99%

Glycoconjugate markers of joint diseases

Popko

Olszewski

Guszczyn

et al. 2011

Biochemical Society Transactions

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A number of different types of glycoconjugate are found associated with joint tissue and fluids, comprising glycoproteins, glycolipids and glycosaminoglycans. Oligosaccharide chains of glycoconjugates are degraded by exoglycosidases, and the dominant exoglycosidase found in human blood, synovial fluid, the synovial membrane and chondrocytes of articular cartilage is HEX (N-acetyl-β-hexosaminidase). HEX is localized mostly intracellularly in synovial cells. Serum activity of HEX may be used to monitor the course and efficiency of treatment of Lyme arthritis, and activity of HEX, above 10 μkat/kg of protein in the synovial fluid, suggests rheumatoid disease. There is a shortage of HEX inhibitors able to penetrate synoviocytes, so the development of drugs which inhibit synthesis and/or the activity of HEX will be a promising field for future investigations.

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“…To elucidate the initial stage of the catabolic pathways for complex CS/DS polysaccharides, it is necessary to identify and characterize such endoglycosidases. Although CS chains can be degraded by hyaluronidase-1 to some extent (18,19,31), an endoglycosidase which can act on DS has never been identiˆed. How are DS chains degraded under physiological conditions?…”

Section: G Perspectivesmentioning

confidence: 99%

Chondroitin Hydrolase in Caenorhabditis elegans

Yamada

Mizumoto

Sugahara

2009

TIGG

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At the initial stage of cellular degradation of chondroitin sulfate/dermatan sulfate, an endo-type hydrolase is thought to degrade the long chain polysaccharides. Thus far, no endoglycosidases that are speciˆc for chondroitin sulfate/dermatan sulfate have been reported; however, hyaluronan-degrading enzymes, hyaluronidases, are considered responsible. The nematode, Caenorhabditis elegans, is an ideal model for studies in a wide range of fundamental biological disciplines. Studies using the nematode have elucidated the biosynthetic mechanisms and functions of glycosaminoglycans. However, the catabolic pathways for glycosaminoglycans in C. elegans have not been investigated. Since C. elegans contains nonsulfated chondroitin but no hyaluronan, it is an ideal system for studying the hyaluronidase-independent catabolic mechanism of chondroitin/chondroitin sulfate. We have identiˆed a chondroitin-speciˆc endo-type hydrolase in C. elegans for theˆrst time. The discovery of this enzyme suggests the presence of chondroitin sulfate/dermatan sulfate-speciˆc endoglycosidases in mammalian systems.

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Glycosaminoglycan Degradation

Cited by 22 publications

References 484 publications

Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan

Hyaluronidases Have Strong Hydrolytic Activity toward Chondroitin 4-Sulfate Comparable to that for Hyaluronan

Glycoconjugate markers of joint diseases

Chondroitin Hydrolase in Caenorhabditis elegans

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