{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T13:11:02Z","timestamp":1761743462472},"reference-count":41,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,2,1]]},"abstract":"<jats:p>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-\u03b2-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 \u03bckat\/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.<\/jats:p>","DOI":"10.1042\/bst0390331","type":"journal-article","created":{"date-parts":[[2011,1,26]],"date-time":"2011-01-26T12:25:37Z","timestamp":1296044737000},"page":"331-335","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Glycoconjugate markers of joint diseases"],"prefix":"10.1042","volume":"39","author":[{"given":"Janusz","family":"Popko","sequence":"first","affiliation":[{"name":"Department of Pediatric Orthopedics and Traumatology, Medical University, Bia\u0142ystok, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S\u0142awomir","family":"Olszewski","sequence":"additional","affiliation":[{"name":"Department of Pediatric Orthopedics and Traumatology, Medical University, Bia\u0142ystok, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomasz","family":"Guszczyn","sequence":"additional","affiliation":[{"name":"Department of Pediatric Orthopedics and Traumatology, Medical University, Bia\u0142ystok, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Krzysztof","family":"Zwierz","sequence":"additional","affiliation":[{"name":"Medical Institute, College of Computer Science and Business Administration, \u0141om\u017ca, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S\u0142awomir","family":"Pancewicz","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases and Neuroinfections, Medical University, Bia\u0142ystok, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2011,1,19]]},"reference":[{"key":"2021111823552871700_B1","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1172\/JCI119526","article-title":"Aggrecan degradation in human cartilage: evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints","volume":"100","author":"Lark","year":"1997","journal-title":"J. Clin. Invest."},{"key":"2021111823552871700_B2","doi-asserted-by":"crossref","first-page":"1534","DOI":"10.1172\/JCI119316","article-title":"Enhanced cleavage of type\u00a0II collagen by collagenases in osteoarthritic articular cartilage","volume":"99","author":"Billinghurst","year":"1997","journal-title":"J. Clin. Invest."},{"key":"2021111823552871700_B3","first-page":"644","article-title":"Pannus invasion and cartilage degradation in rheumatoid arthritis: Involvement of MMP-3 and interleukin-1\u03b2","volume":"23","author":"Ainola","year":"2005","journal-title":"Clin. Exp. Rheumatol."},{"key":"2021111823552871700_B4","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1515\/BC.2002.093","article-title":"Lysosomal peptidases and glycosidases in rheumatoid arthritis","volume":"383","author":"Sohar","year":"2002","journal-title":"Biol. Chem."},{"key":"2021111823552871700_B5","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/S0049-0172(98)80019-X","article-title":"Factors related to degradation of articular cartilage in osteoarthritis: a review","volume":"27","author":"Tanaka","year":"1998","journal-title":"Semin. Arthritis Rheum."},{"key":"2021111823552871700_B6","first-page":"782","article-title":"Defining the role of molecular markers to monitor disease, intervention, and cartilage breakdown in osteoarthritis","volume":"24","author":"Lohmander","year":"1997","journal-title":"J. Rheumatol."},{"key":"2021111823552871700_B7","doi-asserted-by":"crossref","first-page":"84","DOI":"10.3109\/17453679509157658","article-title":"The role of molecular markers to monitor disease, intervention and cartilage breakdown in osteoarthritis","volume":"66","author":"Lohmander","year":"1995","journal-title":"Acta Orthop. Scand."},{"key":"2021111823552871700_B8","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/S0889-857X(05)70077-6","article-title":"Synovial fluid markers in osteoarthritis","volume":"25","author":"Myers","year":"1999","journal-title":"Rheum. Dis. Am."},{"key":"2021111823552871700_B9","first-page":"393","article-title":"The origins of polysaccharidases in rheumatoid and osteoarthritis fluids","volume":"2","author":"Stephens","year":"1975","journal-title":"J. Rheumatol."},{"key":"2021111823552871700_B10","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1016\/S0140-6736(78)90917-0","article-title":"Acidic hydrolases in monocytes from patients with inflammatory bowel disease, chronic liver disease, and rheumatoid arthritis","volume":"1","author":"Ganguly","year":"1978","journal-title":"Lancet"},{"key":"2021111823552871700_B11","doi-asserted-by":"crossref","first-page":"69","DOI":"10.3109\/03009747209102998","article-title":"Synovial fluid glycosidase activity","volume":"1","author":"Bartholomew","year":"1972","journal-title":"Scand. J. Rheumatol."},{"key":"2021111823552871700_B12","doi-asserted-by":"crossref","first-page":"2163","DOI":"10.1002\/art.11093","article-title":"Synovial fluid exoglycosidases are predictors of rheumatoid arthritis and are effective in cartilage glycosaminoglycan depletion","volume":"48","author":"Ortutay","year":"2003","journal-title":"Arthritis Rheum."},{"key":"2021111823552871700_B13","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1002\/art.1780351110","article-title":"Quantitation of chondroitin 4-sulfate and chondroitin 6-sulfate in pathologic joint fluid","volume":"35","author":"Shinmei","year":"1992","journal-title":"Arthritis Rheum."},{"key":"2021111823552871700_B14","first-page":"71","article-title":"Matrix proteins: potentials as body fluid markers of changes in the metabolism of cartilage and bone in arthritis","volume":"22","author":"Saxne","year":"1995","journal-title":"J. Rheumatol."},{"key":"2021111823552871700_B15","first-page":"PO95","article-title":"Glycosaminoglycans and aminohexoses in synovial fluid of injured knee joint","volume":"12","author":"\u015aredzi\u0144ska","year":"2001","journal-title":"Osteop. Int."},{"key":"2021111823552871700_B16","first-page":"35","article-title":"Content of individual glycosaminoglycans in synovial fluid of patients with osteoarthritis and rheumatoid arthritis","volume":"13","author":"\u015aredzi\u0144ska","year":"2002","journal-title":"Prog. Osteoarthol."},{"key":"2021111823552871700_B17","first-page":"82","article-title":"Endoglycosidases and glycoamidases","volume":"50","author":"Stypu\u0142kowska","year":"2004","journal-title":"Post\u0119py Biochemii"},{"key":"2021111823552871700_B18","first-page":"217","article-title":"Glycosaminoglycan degradation","volume":"60","author":"Kresse","year":"1987","journal-title":"Adv. Enzymol. Relat. Areas Mol. Biol."},{"key":"2021111823552871700_B19","doi-asserted-by":"crossref","first-page":"2236","DOI":"10.1128\/jb.174.7.2236-2240.1992","article-title":"Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum","volume":"174","author":"Messer","year":"1992","journal-title":"J. Bacteriol."},{"key":"2021111823552871700_B20","first-page":"275","article-title":"Metabolism of glycoconjugates in human gastric mucosa a review","volume":"46","author":"Zwierz","year":"1989","journal-title":"Acta Med. Hung."},{"key":"2021111823552871700_B21","doi-asserted-by":"crossref","first-page":"739","DOI":"10.18388\/abp.1999_4146","article-title":"Isoenzymes of N-acetyl-\u03b2-hexosaminidase","volume":"46","author":"Zwierz","year":"1999","journal-title":"Acta Biochim. Polon."},{"key":"2021111823552871700_B22","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1080\/03009740500474529","article-title":"The activity of exoglycosidases in the synovial membrane and knee fluid of patients with rheumatoid arthritis and juvenile idiopathic arthritis","volume":"35","author":"Popko","year":"2006","journal-title":"Scand. J. Rheumat."},{"key":"2021111823552871700_B23","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/0009-8981(65)90147-6","article-title":"The fluorimetric estimation of N-acetyl-\u03b2-glucosaminidase and \u03b2-galactosidase in blood plasma","volume":"12","author":"Woolen","year":"1965","journal-title":"Clin. Chem. Acta"},{"key":"2021111823552871700_B24","first-page":"675","article-title":"Activity of N-acetyl-\u03b2-hexosaminidase in serum and joint fluid of the knees of patients with juvenile idiopatic arthritis","volume":"21","author":"Popko","year":"2003","journal-title":"Clin. Exp. Rheumatol."},{"key":"2021111823552871700_B25","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1177\/9.3.242","article-title":"The localization of N-acetyl-\u03b2glucosaminidase in tissues","volume":"9","author":"Pugh","year":"1961","journal-title":"J. Histochem. Cytochem."},{"key":"2021111823552871700_B26","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1111\/j.2042-7158.1998.tb06874.x","article-title":"Why do we need new treatments for rheumatoid arthritis?","volume":"50","author":"Chikanza","year":"1998","journal-title":"J. Pharm. Pharmacol."},{"key":"2021111823552871700_B27","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1002\/1529-0131(200006)43:6<1307::AID-ANR13>3.0.CO;2-3","article-title":"Profile of glycosaminoglycan-degrading glycosidases and glycoside sulfatases secreted by human articular chondrocytes in homeostasis and inflammation","volume":"43","author":"Shikhman","year":"2000","journal-title":"Arthritis Rheum."},{"key":"2021111823552871700_B28","first-page":"63","article-title":"Marked elevation of serum N-acetyl-\u03b2-D-hexosaminidase activity in rheumatoid arthritis","volume":"18","author":"Berenbaum","year":"2000","journal-title":"Clin. Exp. Rheumatol."},{"key":"2021111823552871700_B29","first-page":"690","article-title":"Activity of N-acetyl-\u03b2-hexosaminidase and its isoenzymes in serum and synovial fluid from patients with different arthropathies","volume":"24","author":"Popko","year":"2006","journal-title":"Clin. Exp. Rheumatol."},{"key":"2021111823552871700_B30","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1080\/00365540903036220","article-title":"Activity of lysosomal exoglycosidases in serum and synovial fluid in patients with chronic Lyme and rheumatoiod arthritis","volume":"41","author":"Pancewicz","year":"2009","journal-title":"Scand. J. Infect. Dis."},{"key":"2021111823552871700_B31","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1007\/s12013-008-9018-3","article-title":"Profile of exoglycosidases in synovial cell cultures derived from human synovial membrane","volume":"51","author":"Popko","year":"2008","journal-title":"Cell. Biochem. Biophys."},{"key":"2021111823552871700_B32","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/978-1-4615-5833-0_7","article-title":"Lysosomal metabolism of glycoconjugates","volume":"27","author":"Winchester","year":"1996","journal-title":"Subcell. Biochem."},{"key":"2021111823552871700_B33","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1515\/CCLM.2006.177","article-title":"Optimization of an enzymatic method for the determination of lysosomal N-acetyl-\u03b2-D-hexosaminidase and \u03b2-glucuronidase in synovial fluid","volume":"44","author":"Marciniak","year":"2006","journal-title":"Clin. Chem. Lab. Med."},{"key":"2021111823552871700_B34","first-page":"161","article-title":"Inhibition of human overian carcinoma cell- and hexosaminidase-mediated degradation of extracellular matrix by sugar analogs","volume":"12","author":"Woynarowska","year":"1992","journal-title":"Anticancer Res."},{"key":"2021111823552871700_B35","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1007\/BF00270528","article-title":"Interleukin-1\u03b2 and interleukin-1\u03b1 stimulate the N-acetyl-\u03b2-glucosaminidase activity of human synovial cells","volume":"7","author":"Clarris","year":"1987","journal-title":"Rheumatol. Int."},{"key":"2021111823552871700_B36","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0009-8981(94)90285-2","article-title":"Cathepsin B and N-acetyl-\u03b2-D-glucosaminidase in human synovial cells in culture: effects of interleukin-1","volume":"228","author":"Lecomte","year":"1994","journal-title":"Clin. Chim. Acta"},{"key":"2021111823552871700_B37","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/0300-9084(87)90048-4","article-title":"Partial characterization of intracellular and secreted glycosidases from rabbit articular chondrocytes in culture","volume":"69","author":"Solavagione","year":"1987","journal-title":"Biochimie"},{"key":"2021111823552871700_B38","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.clim.2004.12.009","article-title":"The fibroblast-like synovial cell in rheumatoid arthritis: a key player in inflammation and joint destruction","volume":"115","author":"Mor","year":"2005","journal-title":"Clin. Immunol."},{"key":"2021111823552871700_B39","doi-asserted-by":"crossref","first-page":"6187","DOI":"10.1021\/ja00016a039","article-title":"Enzyme-catalyzed aldol condensation for asymmetric synthesis of azasusugars; synnthesis, evaluation and modeling of glycosidase inhibitors","volume":"114","author":"Kajimoto","year":"1991","journal-title":"J. Am. Chem. Soc."},{"key":"2021111823552871700_B40","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/S1074-5521(01)00045-X","article-title":"Hexosaminidase inhibitors as new drug candidates for the therapy of osteoarthritis","volume":"8","author":"Liu","year":"2001","journal-title":"Chem. Biol."},{"key":"2021111823552871700_B41","first-page":"112","article-title":"The pirymethamine influence on hexosominidase gene expression in synovial cell culture: preliminary report","volume":"184","author":"Olszewski","year":"2010","journal-title":"Pol. Merk. Lek."}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/39\/1\/331\/551391\/bst0390331.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/39\/1\/331\/551391\/bst0390331.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,18]],"date-time":"2021-11-18T23:56:03Z","timestamp":1637279763000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/39\/1\/331\/85142\/Glycoconjugate-markers-of-joint-diseases"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,1,19]]},"references-count":41,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2011,1,19]]},"published-print":{"date-parts":[[2011,2,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bst0390331","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,1,19]]}}}