2.50
Hdl Handle:
http://hdl.handle.net/10541/75656
Title:
Opticin binds to heparan and chondroitin sulfate proteoglycans.
Authors:
Hindson, V John; Gallagher, John T; Halfter, Willi; Bishop, Paul N
Abstract:
PURPOSE: The extracellular matrix glycoprotein opticin is a small leucine-rich repeat proteoglycan/protein family member that was discovered associated with vitreous humor collagen fibrils. Opticin is present throughout the vitreous, but is particularly concentrated at the internal limiting lamina, where it colocalizes with type XVIII collagen. The present study investigated whether opticin interacts directly with the heparan sulfate (HS) proteoglycan type XVIII collagen. METHODS: Solid-phase opticin binding assays were performed with immobilized type XVIII collagen and heparin albumin. Surface plasmon resonance (SPR) was used to investigate the binding of opticin to heparin and HS. RESULTS: Opticin bound to type XVIII collagen via its HS chains. SPR showed that opticin bound to porcine intestinal mucosa HS and heparin with moderately high affinity (K(D) 73 and 43 nM, respectively). Binding inhibition studies showed that hexasaccharides of heparin had a lower affinity for opticin than larger oligosaccharides; the sulfate groups of heparin contributed variably to opticin binding, with the group at ring position two of iduronate contributing least; and chondroitin sulfate A and B bound to opticin, whereas binding to chondroitin sulfate C and hyaluronan was not observed. CONCLUSIONS: Opticin binds to heparin, HS, chondroitin 4-sulfate, and dermatan sulfate, the binding affinity being dependent on sulfation pattern and oligosaccharide chain length. Opticin may provide a link between cortical vitreous collagen fibrils and the inner limiting lamina by binding HS proteoglycans and stabilize vitreous gel structure by binding chondroitin sulfate proteoglycans.
Affiliation:
Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences and Academic Unit of Eye & Vision Science, School of Medicine, University of Manchester, United Kingdom.
Citation:
Opticin binds to heparan and chondroitin sulfate proteoglycans. 2005, 46 (12):4417-23 Invest. Ophthalmol. Vis. Sci.
Journal:
Investigative Ophthalmology & Visual Science
Issue Date:
Dec-2005
URI:
http://hdl.handle.net/10541/75656
DOI:
10.1167/iovs.05-0883
PubMed ID:
16303928
Type:
Article
Language:
en
ISSN:
0146-0404
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorHindson, V John-
dc.contributor.authorGallagher, John T-
dc.contributor.authorHalfter, Willi-
dc.contributor.authorBishop, Paul N-
dc.date.accessioned2009-07-24T15:30:19Z-
dc.date.available2009-07-24T15:30:19Z-
dc.date.issued2005-12-
dc.identifier.citationOpticin binds to heparan and chondroitin sulfate proteoglycans. 2005, 46 (12):4417-23 Invest. Ophthalmol. Vis. Sci.en
dc.identifier.issn0146-0404-
dc.identifier.pmid16303928-
dc.identifier.doi10.1167/iovs.05-0883-
dc.identifier.urihttp://hdl.handle.net/10541/75656-
dc.description.abstractPURPOSE: The extracellular matrix glycoprotein opticin is a small leucine-rich repeat proteoglycan/protein family member that was discovered associated with vitreous humor collagen fibrils. Opticin is present throughout the vitreous, but is particularly concentrated at the internal limiting lamina, where it colocalizes with type XVIII collagen. The present study investigated whether opticin interacts directly with the heparan sulfate (HS) proteoglycan type XVIII collagen. METHODS: Solid-phase opticin binding assays were performed with immobilized type XVIII collagen and heparin albumin. Surface plasmon resonance (SPR) was used to investigate the binding of opticin to heparin and HS. RESULTS: Opticin bound to type XVIII collagen via its HS chains. SPR showed that opticin bound to porcine intestinal mucosa HS and heparin with moderately high affinity (K(D) 73 and 43 nM, respectively). Binding inhibition studies showed that hexasaccharides of heparin had a lower affinity for opticin than larger oligosaccharides; the sulfate groups of heparin contributed variably to opticin binding, with the group at ring position two of iduronate contributing least; and chondroitin sulfate A and B bound to opticin, whereas binding to chondroitin sulfate C and hyaluronan was not observed. CONCLUSIONS: Opticin binds to heparin, HS, chondroitin 4-sulfate, and dermatan sulfate, the binding affinity being dependent on sulfation pattern and oligosaccharide chain length. Opticin may provide a link between cortical vitreous collagen fibrils and the inner limiting lamina by binding HS proteoglycans and stabilize vitreous gel structure by binding chondroitin sulfate proteoglycans.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshBinding Sites-
dc.subject.meshBinding, Competitive-
dc.subject.meshCollagen Type XVIII-
dc.subject.meshExtracellular Matrix Proteins-
dc.subject.meshHeparan Sulfate Proteoglycans-
dc.subject.meshProtein Binding-
dc.subject.meshProteochondroitin Sulfates-
dc.subject.meshProteoglycans-
dc.subject.meshRabbits-
dc.titleOpticin binds to heparan and chondroitin sulfate proteoglycans.en
dc.typeArticleen
dc.contributor.departmentWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences and Academic Unit of Eye & Vision Science, School of Medicine, University of Manchester, United Kingdom.en
dc.identifier.journalInvestigative Ophthalmology & Visual Scienceen

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