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Article: Glomerular endothelial glycocalyx constitutes a barrier to protein permeability

TitleGlomerular endothelial glycocalyx constitutes a barrier to protein permeability
Authors
Issue Date2007
Citation
Journal of the American Society of Nephrology, 2007, v. 18 n. 11, p. 2885-2893 How to Cite?
AbstractGlycocalyx, composed of glycoproteins including proteoglycans, coats the luminal surface of the glomerular capillaries. Human heparanase degrades heparan sulphate glycosaminoglycans and is upregulated in proteinuric states. In this study, we analyze the structure of the human glomerular endothelial cell glycocalyx in vitro and examine its functional relevance, especially after treatment with human heparanase. Electron microscopy of conditionally immortalized glomerular endothelial cells revealed a 200-nm thick glycocalyx over the plasma membrane, which was also demonstrated by confocal microscopy. Neuraminidase treatment removed the majority of glycocalyx, reduced trans-endothelial electrical resistance by 59%, and increased albumin flux by 207%. Heparinase III and human heparanase specifically cleaved heparan sulphate: this caused no change in trans-endothelial electrical resistance, but increased the albumin passage across the monolayers by 40% and 39%, respectively. Therefore, we have characterized the glomerular endothelial cell glycocalyx and have shown that it contributes to the barrier to flux of albumin across the cell layer. These results suggest an important role for this glycocalyx in the restriction of glomerular protein passage in vivo and suggest ways in which human heparanase levels may be linked to proteinuria in clinical disease. Copyright © 2007 by the American Society of Nephrology.
Persistent Identifierhttp://hdl.handle.net/10722/195456
ISSN
2015 Impact Factor: 8.491
2015 SCImago Journal Rankings: 4.699
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSingh, A-
dc.contributor.authorSatchell, SC-
dc.contributor.authorNeal, CR-
dc.contributor.authorMcKenzie, EA-
dc.contributor.authorTooke, JE-
dc.contributor.authorMathieson, PW-
dc.date.accessioned2014-02-28T06:12:11Z-
dc.date.available2014-02-28T06:12:11Z-
dc.date.issued2007-
dc.identifier.citationJournal of the American Society of Nephrology, 2007, v. 18 n. 11, p. 2885-2893-
dc.identifier.issn1046-6673-
dc.identifier.urihttp://hdl.handle.net/10722/195456-
dc.description.abstractGlycocalyx, composed of glycoproteins including proteoglycans, coats the luminal surface of the glomerular capillaries. Human heparanase degrades heparan sulphate glycosaminoglycans and is upregulated in proteinuric states. In this study, we analyze the structure of the human glomerular endothelial cell glycocalyx in vitro and examine its functional relevance, especially after treatment with human heparanase. Electron microscopy of conditionally immortalized glomerular endothelial cells revealed a 200-nm thick glycocalyx over the plasma membrane, which was also demonstrated by confocal microscopy. Neuraminidase treatment removed the majority of glycocalyx, reduced trans-endothelial electrical resistance by 59%, and increased albumin flux by 207%. Heparinase III and human heparanase specifically cleaved heparan sulphate: this caused no change in trans-endothelial electrical resistance, but increased the albumin passage across the monolayers by 40% and 39%, respectively. Therefore, we have characterized the glomerular endothelial cell glycocalyx and have shown that it contributes to the barrier to flux of albumin across the cell layer. These results suggest an important role for this glycocalyx in the restriction of glomerular protein passage in vivo and suggest ways in which human heparanase levels may be linked to proteinuria in clinical disease. Copyright © 2007 by the American Society of Nephrology.-
dc.languageeng-
dc.relation.ispartofJournal of the American Society of Nephrology-
dc.titleGlomerular endothelial glycocalyx constitutes a barrier to protein permeability-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1681/ASN.2007010119-
dc.identifier.pmid17942961-
dc.identifier.scopuseid_2-s2.0-35848940725-
dc.identifier.volume18-
dc.identifier.issue11-
dc.identifier.spage2885-
dc.identifier.epage2893-
dc.identifier.isiWOS:000250737600016-
dc.identifier.f1000717955785-

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