Heavy Chain Transfer by Tumor Necrosis Factor-stimulated Gene 6 to the Bikunin Proteoglycan

Lamkin, Elliott K.; Cheng, Georgina; Calabro, Anthony; Hascall, Vincent C.; Joo, Eun Ji; Li, Lingyun; Linhardt, Robert J.; Lauer, Mark E.

doi:10.1074/jbc.m114.636258

Cited by 12 publications

(14 citation statements)

References 17 publications

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“…It is noteworthy that bikunin, which is a CS proteoglycan drug prepared from normal human urine and is used to treat acute pancreatitis, 44 contains a single CS chain comprised of 0S (~66%) and 4S (~33%) disaccharide units. 17,23,45–47 These results suggest that bikunin comprises only a portion of the CS present in human urine.…”

Section: Resultsmentioning

confidence: 86%

“…7 The fine structures, as well as the chain sizes, of GAGs have a profound impact on their biological activities. 8,9,15–17 Thus, it is critically important to develop the means of GAG analysis, particularly in their natural environment, such as in tissues 18,19 and in biological fluids. Urine, while representing an easy to access biological fluid, presents a particular challenge to analysis, because normal urine contains variable and extremely low levels of excreted GAGs, in addition to other sulfated metabolites.…”

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confidence: 99%

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Analysis of Total Human Urinary Glycosaminoglycan Disaccharides by Liquid Chromatography–Tandem Mass Spectrometry

Sun

Overdier³

et al. 2015

Anal. Chem.

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The determination of complex analytes, present at low concentrations, in biological fluids poses a diffcult challenge. This study relies on an optimized method of recovery, enzymatic treatment, and disaccharide analysis by liquid chromatography–tandem mass spectrometry to rapidly determine low concentrations of glycosaminoglycans in human urine. The approach utilizes multiple reaction monitoring (MRM) of glycosaminoglycan disaccharides obtained from treating urine samples with recombinant heparin lyases and chondroitin lyase. This rapid and sensitive method allows the analysis of glycosaminoglycan content and disaccharide composition in urine samples having concentrations 10-to 100-fold lower than those typically analyzed from patients with metabolic diseases, such as mucopolysaccharidosis. The current method facilitates the analysis low (ng/mL) levels of urinary glycosaminoglycans present in healthy individuals and in patients with pathological conditions, such as inflammation and cancers, that can subtly alter glycosaminoglycan content and composition.

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Section: Resultsmentioning

confidence: 86%

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confidence: 99%

Analysis of Total Human Urinary Glycosaminoglycan Disaccharides by Liquid Chromatography–Tandem Mass Spectrometry

Sun

Overdier³

et al. 2015

Anal. Chem.

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“…TSG-6 can also bind weakly (180 n m ) and metal ion-independently to the bikunin·CS component of IαI ( 40 , 46 ); this is probably mediated (at least in part) through the recognition of the CS chain by the Link module ( 47 ). Interestingly, this CS moiety has been clearly implicated as being necessary for HC·TSG-6 formation ( 40 ), requiring a particular sulfation pattern in the glycosaminoglycan linkage region in order for IαI to act as a substrate ( 24 ); chondroitin ( 91 , 92 ) and the CS chain of bikunin·CS ( 93 ), which has non-sulfated “chondroitin-like” regions ( 23 ), can act as weak substrates for HC transfer. At the moment, we do not know the temporal sequence of this CS·bikunin-binding event relative to the metal ion-dependent interaction between the TSG-6 CUB module and an IαI HC (described in the present study).…”

Section: Discussionmentioning

confidence: 99%

Metal Ion-dependent Heavy Chain Transfer Activity of TSG-6 Mediates Assembly of the Cumulus-Oocyte Matrix

Briggs

Birchenough

Ali

et al. 2015

Journal of Biological Chemistry

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Background: TSG-6 (TNF-stimulated gene-6)-dependent transfer of heavy chains from inter-α-inhibitor onto hyaluronan is critical for ovulation.Results: A calcium ion and chelating glutamate within TSG-6 mediate formation of the covalent heavy chain-TSG-6 intermediate.Conclusion: TSG-6 transferase activity rather than hyaluronan binding drives cumulus expansion.Significance: The role of metal ions in hyaluronan-heavy chain formation has been determined.

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“…[83] This transfer of the HCs to HA occurs by a process of trans-esterification catalyzed by the enzyme TSG-6 [84] and apparently stabilizes the HA countering its depolymerization by free radicals released by inflammatory cells during OA and rheumatoid arthritis (RA). These are absent in murine aggrecan with no obvious detrimental effect on cartilage function and aggrecan turnover.…”

Section: Ks Rich Regionmentioning

confidence: 99%

Glycosaminoglycan and Proteoglycan Biotherapeutics in Articular Cartilage Protection and Repair Strategies: Novel Approaches to Visco‐supplementation in Orthobiologics

Hayes

Melrose

2019

Advanced Therapeutics

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The aim of this study is to review developments in glycosaminoglycan and proteoglycan research relevant to cartilage repair biology and in particular the treatment of osteoarthritis (OA). Glycosaminoglycans decorate a diverse range of extracellular matrix and cell associated proteoglycans conveying structural organization and physico-chemical properties to tissues. They play key roles mediating cellular interactions with bioactive growth factors, cytokines, and morphogenetic proteins, and structural fibrillar collagens, cell interactive and extracellular matrix proteoglycans, and glycoproteins which define tissue function. Proteoglycan degradation detrimentally affects tissue functional properties. Therapeutic strategies have been developed to counter these degenerative changes. Neo-proteoglycans prepared from chondroitin sulfate or hyaluronan and hyaluronan or collagen-binding peptides emulate the interactive, water imbibing, weight bearing, and surface lubricative properties of native proteoglycans. Many neo-proteoglycans outperform native proteoglycans in terms of water imbibition, matrix stabilization, and resistance to proteolytic degradation. The biospecificity of recombinant proteoglycans however, provides precise attachment to native target molecules. Visco-supplements augmented with growth factors/therapeutic cells, hyaluronan, and lubricin (orthobiologicals) have the capacity to lubricate and protect cartilage, control inflammation, and promote cartilage repair and regeneration of early cartilage lesions and may represent a more effective therapeutic approach to the treatment of mild to moderate OA and deserve further study.Similar protective perineural net structures assembled from the lectican proteoglycan family and HA also occur in the CNS/PNS. These so called perineuronal nets are visualized by immunolocalization of MAb 1B5 (+) epitope in rat brain (e) and pericellular 1B5(+) epitope expression by isolated neurons (f). Scale bars 100 µm.

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Heavy Chain Transfer by Tumor Necrosis Factor-stimulated Gene 6 to the Bikunin Proteoglycan

Cited by 12 publications

References 17 publications

Analysis of Total Human Urinary Glycosaminoglycan Disaccharides by Liquid Chromatography–Tandem Mass Spectrometry

Analysis of Total Human Urinary Glycosaminoglycan Disaccharides by Liquid Chromatography–Tandem Mass Spectrometry

Metal Ion-dependent Heavy Chain Transfer Activity of TSG-6 Mediates Assembly of the Cumulus-Oocyte Matrix

Glycosaminoglycan and Proteoglycan Biotherapeutics in Articular Cartilage Protection and Repair Strategies: Novel Approaches to Visco‐supplementation in Orthobiologics

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