Journal ArticleDOI
Not all lubricin isoforms are substituted with a glycosaminoglycan chain.
Megan S. Lord,Ruby P. Estrella,Christine Y. Chuang,Peter Youssef,Niclas G. Karlsson,Carl R. Flannery,John M. Whitelock +6 more
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TLDR
The structure of the glycosaminoglycan chain that decorated lubricin in human synovial fluid was investigated to provide insight into its biological role and demonstrate that lubricin present in humansynovials fluid was a heterogeneous population with both glycoprotein and proteoglycan forms.Abstract:
Lubricin, also referred to as superficial zone protein, has been reported to be a proteoglycan. However, the structure of its glycosaminoglycan chain has not been well characterized, and this study was undertaken to investigate the structure of the glycosaminoglycan chain that decorated lubricin in human synovial fluid to provide insight into its biological role. Lubricin was detected as a major band at approximately 360 kDa which co-migrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a chondroitin sulfate (CS)-containing proteoglycan that was detected by both monoclonal antibodies (MAb) 2-B-6 and MAb 3-B-3 after chondroitinase ABC treatment and keratan sulfate (KS) that was detected by MAb 5-D-4. Further analysis of lubricin-containing fractions that eluted from an anion exchange column indicated that the major population of lubricin could be separated from the CS and KS stubs which indicated that this fraction of lubricin was not decorated with glycosaminoglycan chain and was the ...read more
Citations
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Journal ArticleDOI
Articular Joint Lubricants during Osteoarthritis and Rheumatoid Arthritis Display Altered Levels and Molecular Species
Marta Krystyna Kosinska,Taryn E. Ludwig,Gerhard Liebisch,Ruiyan Zhang,Hans-Christian Siebert,Jochen Wilhelm,Ulrich Kaesser,Reinhard B. Dettmeyer,Heiko Klein,Bernd Ishaque,Markus Rickert,Gerd Schmitz,Tannin A. Schmidt,Juergen Steinmeyer +13 more
TL;DR: The levels, composition, and MW distribution of all currently known lubricants in SF—HA, lubricin, PLs—vary with joint disease and stage of OA, providing the framework to develop new optimal compounded lubricants to reduce joint destruction.
Journal ArticleDOI
Distribution of proteins within different compartments of tendon varies according to tendon type
Chavaunne T. Thorpe,Kabelan J. Karunaseelan,Jade Ng Chieng Hin,Graham P. Riley,Helen L. Birch,Peter D. Clegg,Hazel R. C. Screen +6 more
TL;DR: The hypothesis that the distribution of elastin and proteoglycans differs between energy‐storing and positional tendons, and that protein distribution varies between the fascicular matrix and the interfascicular matrix, is tested, demonstrating enrichment of lubricin in the interfASCicular matrix in both tendon types, where it is likely to facilitate interfascic sliding.
Journal ArticleDOI
Human Synovial Lubricin Expresses Sialyl Lewis x Determinant and Has L-selectin Ligand Activity
Chunsheng Jin,Anna-Karin H. Ekwall,Johan Bylund,Lena Björkman,Ruby P. Estrella,John M. Whitelock,Thomas Eisler,Maria Bokarewa,Niclas G. Karlsson +8 more
TL;DR: It was found that PMN recruited to inflamed synovial area and fluid in rheumatoid arthritis patients kept a coat of lubricin, suggesting that lubricin is able to bind to PMN via an L-selectin-dependent and -independent manner and may play a role in PMN-mediated inflammation.
Journal ArticleDOI
Molecular weight characterization of PRG4 proteins using multi-angle laser light scattering (MALLS)
TL;DR: The observed decrease in M(W)'s of monomeric PRG4 species upon RA may be due to the release of post-translationally cleaved fragments, and further study of these species will provide insight into thePRG4 molecular structure and function relationship.
Journal ArticleDOI
Altered joint tribology in osteoarthritis: Reduced lubricin synthesis due to the inflammatory process. New horizons for therapeutic approaches
TL;DR: In this article, a review aimed to consolidate the current evidence that implicates the inflammatory process in the attenuation of synovial lubrication and joint tissue homeostasis in OA.
References
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Journal ArticleDOI
The secreted glycoprotein lubricin protects cartilage surfaces and inhibits synovial cell overgrowth
David K. Rhee,Jose Marcelino,MacArthur Baker,Yaoqin Gong,Patrick Smits,Véronique Lefebvre,Gregory D. Jay,Matthew C. Stewart,Hongwei Wang,Matthew L. Warman,John D. Carpten,John D. Carpten +11 more
TL;DR: It is concluded that lubricin has multiple functions in articulating joints and tendons that include the protection of surfaces and the control of synovial cell growth.
Journal ArticleDOI
A novel proteoglycan synthesized and secreted by chondrocytes of the superficial zone of articular cartilage.
Barbara L. Schumacher,Joel A. Block,Thomas M. Schmid,Margaret B. Aydelotte,Klaus E. Kuettner +4 more
TL;DR: A novel proteoglycan (PG) has been identified in culture medium from thin slices of the superficial zone of bovine articular cartilage and may serve as a functional metabolic marker for chondrocytes of the shallow zone of articular Cartilage.
Journal ArticleDOI
Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues
TL;DR: It is demonstrated that chondroitin sulphates exhibit remarkable connective tissue specificity and furthermore there is evidence that some proteoglycans may predominantly carry only one type of chondDetroitin sulphate chain.
Journal ArticleDOI
Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan
TL;DR: The 1/20/5-D-4 monoclonal antibody appears to recognize a common determinant in their polysaccharide moieties, consistent with several biochemical analyses showing the absence of keratan sulfate in proteoglycan synthesised by this tissue.
Journal ArticleDOI
MINI REVIEW Keratan sulfate: structure, biosynthesis, and function
TL;DR: Findings have served to expand the concept of what keratan sulfate is and the potential roles it may play in the cellular biology of diverse tissues.
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