Analysis of opticin binding to collagen fibrils identifies a single binding site in the gap region and a high specificity towards thin heterotypic fibrils containing collagens II, and XI or V/XI

Autor: Paul N. Bishop, Uwe Hansen, David F. Holmes, Peter Bruckner
Rok vydání: 2020
Předmět:
0301 basic medicine
Biochemistry
Negative Staining
Extracellular matrix
Mice
Binding Analysis
0302 clinical medicine
Medicine and Health Sciences
Group-Specific Staining
Power Distribution
Electron Microscopy
Microscopy
Immunoelectron
Mice
Knockout
Staining
Extracellular Matrix Proteins
Microscopy
Multidisciplinary
biology
Chemistry
Fibrillogenesis
medicine.anatomical_structure
Connective Tissue
030220 oncology & carcinogenesis
Medicine
Engineering and Technology
Proteoglycans
Collagen
Anatomy
Protein Binding
Research Article
Uranyl Acetate Staining
Power Grids
Science
Immunoelectron microscopy
macromolecular substances
In Vitro Techniques
Fibril
Research and Analysis Methods
03 medical and health sciences
Microscopy
Electron
Transmission
medicine
Animals
Binding site
Chemical Characterization
Vitreous humour
Binding Sites
Cartilage
Biology and Life Sciences
Proteins
Immunoelectron Microscopy
In vitro
Mice
Inbred C57BL
Vitreous Body
Energy and Power
030104 developmental biology
Biological Tissue
Proteoglycan
Specimen Preparation and Treatment
biology.protein
Biophysics
Cattle
Collagens
Zdroj: PLoS ONE
PLoS ONE, Vol 15, Iss 8, p e0234672 (2020)
ISSN: 1932-6203
Popis: Opticin is a class III member of the extracellular matrix small leucine-rich repeat protein/proteoglycan (SLRP) family found in vitreous humour and cartilage. It was first identified associated with the surface of vitreous collagen fibrils and several other SLRPs are also known to bind collagen fibrils and it some cases alter fibril morphology. The purpose of this study was to investigate the binding of opticin to the collagen II-containing fibrils found in vitreous and cartilage. Electron microscopic studies using gold labelling demonstrated that opticin binds vitreous and thin cartilage collagen fibrils specifically at a single site in the gap region of the collagen D-period corresponding to the e2 stain band; this is the first demonstration of the binding site of a class III SLRP on collagen fibrils. Opticin did not bind thick cartilage collagen fibrils from cartilage or tactoids formedin vitrofrom collagen II, but shows high specificity for thin, heterotypic collagen fibrils containing collagens II, and XI or V/XI. Vitreous collagen fibrils from opticin null and wild-type mice were compared and no difference in fibril morphology or diameter was observed. Similarly,in vitrofibrillogenesis experiments showed that opticin did not affect fibril formation. We propose that when opticin is bound to collagen fibrils, rather than influencing their morphology it instead hinders the binding of other molecules to the fibril surfaces and/or act as an intermediary bridge linking the collagen fibrils to other non-collagenous molecules.
Databáze: OpenAIRE
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