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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
46
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pubmed:dateCreated |
2003-11-10
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pubmed:databankReference |
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pubmed:abstractText |
Opticin is a class III member of the extracellular matrix small leucine-rich repeat protein (SLRP) family that was initially identified in the eye in association with the collagen fibrils of the vitreous humor. Recombinant and tissue-extracted forms of bovine opticin were subjected to biochemical and biophysical characterization. Following SDS-PAGE the predominant component produced by both forms was a broad band between 45-52 kDa. There was evidence for two-stage processing and, additionally, a proteolytic cleavage product of approximately 25 kDa. Deconvolution of circular dichroism spectra revealed beta-sheet (41%), beta-turn (21%), and alpha-helix (10%), and thermal denaturation experiments showed a transition with a midpoint of 47 degrees C. Weight-averaged molecular mass measurements using both light scattering and analytical ultracentrifugation demonstrated that opticin exists in solution as a stable dimer of approximately 90 kDa, which can be dissociated into a monomer by denaturation with 2.5 m guanidine hydrochloride or during SDS-polyacrylamide electrophoresis. Opticin remains a dimer after removal of the amino-terminal region by O-sialoglycoprotein endopeptidase digestion, suggesting that dimer formation is mediated by the leucine-rich repeats. Dimerization could have a number of functional consequences, including divalent ligand interactions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
45280-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12951322-Amino Acid Sequence,
pubmed-meshheading:12951322-Animals,
pubmed-meshheading:12951322-Base Sequence,
pubmed-meshheading:12951322-Cattle,
pubmed-meshheading:12951322-Chromatography, Gel,
pubmed-meshheading:12951322-Circular Dichroism,
pubmed-meshheading:12951322-Cloning, Molecular,
pubmed-meshheading:12951322-Collagen,
pubmed-meshheading:12951322-Dimerization,
pubmed-meshheading:12951322-Dogs,
pubmed-meshheading:12951322-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12951322-Extracellular Matrix Proteins,
pubmed-meshheading:12951322-Genetic Vectors,
pubmed-meshheading:12951322-Guanidine,
pubmed-meshheading:12951322-Humans,
pubmed-meshheading:12951322-Ligands,
pubmed-meshheading:12951322-Light,
pubmed-meshheading:12951322-Molecular Sequence Data,
pubmed-meshheading:12951322-Protein Structure, Secondary,
pubmed-meshheading:12951322-Proteoglycans,
pubmed-meshheading:12951322-Recombinant Proteins,
pubmed-meshheading:12951322-Scattering, Radiation,
pubmed-meshheading:12951322-Sequence Homology, Amino Acid,
pubmed-meshheading:12951322-Temperature,
pubmed-meshheading:12951322-Ultracentrifugation,
pubmed-meshheading:12951322-Vitreous Body
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pubmed:year |
2003
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pubmed:articleTitle |
Characterization of opticin and evidence of stable dimerization in solution.
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pubmed:affiliation |
Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences and Research Group in Eye & Vision Science, The Medical School, University of Manchester, Manchester M13 9PT, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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