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Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans?

Proteolytic degradation of articular cartilage macromolecules, including the large aggregating cartilage proteoglycan (aggrecan) and small leucine-rich proteoglycans (SLRPs), is a prominent pathophysiological feature of arthritic diseases such as osteoarthritis (OA). Molecular profiling and monitori...

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Detalles Bibliográficos
Autor principal: Flannery, Carl R
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1526605/
https://www.ncbi.nlm.nih.gov/pubmed/16563183
http://dx.doi.org/10.1186/ar1925
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author Flannery, Carl R
author_facet Flannery, Carl R
author_sort Flannery, Carl R
collection PubMed
description Proteolytic degradation of articular cartilage macromolecules, including the large aggregating cartilage proteoglycan (aggrecan) and small leucine-rich proteoglycans (SLRPs), is a prominent pathophysiological feature of arthritic diseases such as osteoarthritis (OA). Molecular profiling and monitoring of soluble/circulating proteoglycan catabolites that may be released from the cartilage matrix therefore represents an attractive strategy for evaluating OA disease progression and intervention. The recent identification of discrete metalloproteinase-sensitive SLRP cleavage sites, and complementary neoepitope-bearing SLRP catabolites, extends decisive insight into the functional regulation of extracellular matrix integrity, and proffers poignant leads to assist in disclosing and appraising applicable biomarkers of cartilage degeneration during arthritis.
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spelling pubmed-15266052006-08-04 Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans? Flannery, Carl R Arthritis Res Ther Commentary Proteolytic degradation of articular cartilage macromolecules, including the large aggregating cartilage proteoglycan (aggrecan) and small leucine-rich proteoglycans (SLRPs), is a prominent pathophysiological feature of arthritic diseases such as osteoarthritis (OA). Molecular profiling and monitoring of soluble/circulating proteoglycan catabolites that may be released from the cartilage matrix therefore represents an attractive strategy for evaluating OA disease progression and intervention. The recent identification of discrete metalloproteinase-sensitive SLRP cleavage sites, and complementary neoepitope-bearing SLRP catabolites, extends decisive insight into the functional regulation of extracellular matrix integrity, and proffers poignant leads to assist in disclosing and appraising applicable biomarkers of cartilage degeneration during arthritis. BioMed Central 2006 2006-03-13 /pmc/articles/PMC1526605/ /pubmed/16563183 http://dx.doi.org/10.1186/ar1925 Text en Copyright © 2006 BioMed Central Ltd
spellingShingle Commentary
Flannery, Carl R
Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans?
title Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans?
title_full Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans?
title_fullStr Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans?
title_full_unstemmed Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans?
title_short Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans?
title_sort usurped slrps: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans?
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1526605/
https://www.ncbi.nlm.nih.gov/pubmed/16563183
http://dx.doi.org/10.1186/ar1925
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