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Article: Electrophoretic separation and characterization of urinary glycosaminoglycans and their roles in urolithiasis

TitleElectrophoretic separation and characterization of urinary glycosaminoglycans and their roles in urolithiasis
Authors
Issue Date2007
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/carres
Citation
Carbohydrate Research, 2007, v. 342 n. 1, p. 79-86 How to Cite?
AbstractUrinary polyanions recovered from the urine samples of kidney stone-formers and normal controls were subjected to preparative agarose gel electrophoresis, which yielded fractions 1-5 in a decreasing order of mobility. In both groups, chondroitin sulfates were identified in the fast-moving fractions and heparan sulfates in the slow-moving fractions. Furthermore, two types of heparan sulfates were identified based on their electrophoretic mobility: slow-moving and fast-moving. The fractionated urinary polyanions were then tested in an in vitro calcium oxalate crystallization assay and compared at the same uronic acid concentration, whereby, the chondroitin sulfates of stone-formers and heparan sulfates of normals enhanced crystal nucleation. Fraction 5 of the normals, containing glycoproteins (14-97 kDa) and associated glycosaminoglycans, were found to effectively inhibit crystallization. Papainization of this fraction in stone-formers revealed crystal-suppressive effects of glycoproteins, which was not seen in similar fractions of normals. It was concluded that glycoproteins could modulate the crystal-enhancing glycosaminoglycans such as chondroitin sulfates of stone-formers but not in normals. The differing crystallization activities of electrophoretic fraction 1 of normals and stone-formers revealed the presence of another class of glycosaminoglycan-hyaluronan. Hence, in the natural milieu, different macromolecules combine to have an overall outcome in the crystallization of calcium oxalate. © 2006 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68235
ISSN
2015 Impact Factor: 1.817
2015 SCImago Journal Rankings: 0.612
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGohel, MDIen_HK
dc.contributor.authorShum, DKYen_HK
dc.contributor.authorTam, PCen_HK
dc.date.accessioned2010-09-06T06:02:38Z-
dc.date.available2010-09-06T06:02:38Z-
dc.date.issued2007en_HK
dc.identifier.citationCarbohydrate Research, 2007, v. 342 n. 1, p. 79-86en_HK
dc.identifier.issn0008-6215en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68235-
dc.description.abstractUrinary polyanions recovered from the urine samples of kidney stone-formers and normal controls were subjected to preparative agarose gel electrophoresis, which yielded fractions 1-5 in a decreasing order of mobility. In both groups, chondroitin sulfates were identified in the fast-moving fractions and heparan sulfates in the slow-moving fractions. Furthermore, two types of heparan sulfates were identified based on their electrophoretic mobility: slow-moving and fast-moving. The fractionated urinary polyanions were then tested in an in vitro calcium oxalate crystallization assay and compared at the same uronic acid concentration, whereby, the chondroitin sulfates of stone-formers and heparan sulfates of normals enhanced crystal nucleation. Fraction 5 of the normals, containing glycoproteins (14-97 kDa) and associated glycosaminoglycans, were found to effectively inhibit crystallization. Papainization of this fraction in stone-formers revealed crystal-suppressive effects of glycoproteins, which was not seen in similar fractions of normals. It was concluded that glycoproteins could modulate the crystal-enhancing glycosaminoglycans such as chondroitin sulfates of stone-formers but not in normals. The differing crystallization activities of electrophoretic fraction 1 of normals and stone-formers revealed the presence of another class of glycosaminoglycan-hyaluronan. Hence, in the natural milieu, different macromolecules combine to have an overall outcome in the crystallization of calcium oxalate. © 2006 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/carresen_HK
dc.relation.ispartofCarbohydrate Researchen_HK
dc.subject.meshAdulten_HK
dc.subject.meshCalcium Oxalate - isolation & purification - urineen_HK
dc.subject.meshChondroitin Sulfates - isolation & purification - urineen_HK
dc.subject.meshCrystallizationen_HK
dc.subject.meshElectrophoresis, Agar Gelen_HK
dc.subject.meshElectrophoresis, Cellulose Acetateen_HK
dc.subject.meshGlycoproteins - metabolismen_HK
dc.subject.meshHeparitin Sulfate - isolation & purification - urineen_HK
dc.subject.meshHumansen_HK
dc.subject.meshKidney Calculien_HK
dc.subject.meshMiddle Ageden_HK
dc.subject.meshUrinary Calculi - urineen_HK
dc.subject.meshUrolithiasisen_HK
dc.titleElectrophoretic separation and characterization of urinary glycosaminoglycans and their roles in urolithiasisen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0008-6215&volume=342&issue=1&spage=79&epage=86&date=2007&atitle=Electrophoretic+separation+and+characterization+of+urinary+glycosaminoglycans+and+their+roles+in+urolithiasis.en_HK
dc.identifier.emailShum, DKY:shumdkhk@hkucc.hku.hken_HK
dc.identifier.authorityShum, DKY=rp00321en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.carres.2006.11.001en_HK
dc.identifier.pmid17145044-
dc.identifier.scopuseid_2-s2.0-33845507298en_HK
dc.identifier.hkuros128900en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845507298&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume342en_HK
dc.identifier.issue1en_HK
dc.identifier.spage79en_HK
dc.identifier.epage86en_HK
dc.identifier.isiWOS:000243628500009-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridGohel, MDI=7004532182en_HK
dc.identifier.scopusauthoridShum, DKY=7004824447en_HK
dc.identifier.scopusauthoridTam, PC=7202539419en_HK

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