Aggrecan degradation in human intervertebral disc and articular cartilage. - Wikidata - wikimedia - TriplyDB

Aggrecan degradation in human intervertebral disc and articular cartilage.

Aggrecan degradation in human intervertebral disc and articular cartilage.

http://www.wikidata.org/entity/Q42987526

about

Degeneration of the intervertebral disc Degenerative suspensory ligament desmitis as a systemic disorder characterized by proteoglycan accumulation The role of interleukin-1 in the pathogenesis of human intervertebral disc degeneration Molecular mechanisms of biological aging in intervertebral discs Diversity of intervertebral disc cells: phenotype and function Expression and regulation of metalloproteinases and their inhibitors in intervertebral disc aging and degeneration Emerging technologies for molecular therapy for intervertebral disk degeneration Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain Leptin plays a catabolic role on articular cartilage Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro.Catabolism of aggrecan, decorin and biglycan in tendon.The presence and absence of lymphatic vessels in the adult human intervertebral disc: relation to disc pathology.Cellular mechanobiology of the intervertebral disc: new directions and approaches.The use of cleavage site specific antibodies to delineate protein processing and breakdown pathways.Age-related changes in the extracellular matrix of nucleus pulposus and anulus fibrosus of human intervertebral disc.Matrix metalloproteinases are not essential for aggrecan turnover during normal skeletal growth and development.Expression of chondrocyte markers by cells of normal and degenerate intervertebral discs Matrix metalloproteinase 8 deficiency in mice exacerbates inflammatory arthritis through delayed neutrophil apoptosis and reduced caspase 11 expression.Region-dependent aggrecan degradation patterns in the rat intervertebral disc are affected by mechanical loading in vivo.Lack of tissue inhibitor of metalloproteinases-3 results in an enhanced inflammatory response in antigen-induced arthritis.Electroacupuncture stimulates remodeling of extracellular matrix by inhibiting apoptosis in a rabbit model of disc degeneration.Physiological loading can restore the proteoglycan content in a model of early IVD degeneration.TNFα transport induced by dynamic loading alters biomechanics of intact intervertebral discs Aquaporin 1 and 5 expression decreases during human intervertebral disc degeneration: Novel HIF-1-mediated regulation of aquaporins in NP cells.An enzyme-sensitive PEG hydrogel based on aggrecan catabolism for cartilage tissue engineering Spine degeneration in a murine model of chronic human tobacco smokers Rat tail static compression model mimics extracellular matrix metabolic imbalances of matrix metalloproteinases, aggrecanases, and tissue inhibitors of metalloproteinases in intervertebral disc degeneration Biglycan and fibromodulin fragmentation correlates with temporal and spatial annular remodelling in experimentally injured ovine intervertebral discs.An in vitro tissue model to study the effect of age on nucleus pulposus cells The role of aggrecan in normal and osteoarthritic cartilage.Biological treatment strategies for disc degeneration: potentials and shortcomings.Serum levels of the proinflammatory cytokine interleukin-6 vary based on diagnoses in individuals with lumbar intervertebral disc diseases.Prevention of disc degeneration with growth factors.Programmed cell death in intervertebral disc degeneration.Genetic polymorphisms associated with intervertebral disc degeneration.Anulus fibrosus tension inhibits degenerative structural changes in lamellar collagen.Chondroadherin fragmentation mediated by the protease HTRA1 distinguishes human intervertebral disc degeneration from normal aging.Intervertebral disc: anatomy-physiology-pathophysiology-treatment.Conserved sequence in the aggrecan interglobular domain modulates cleavage by ADAMTS-4 and ADAMTS-5.

P2860

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P2860

Aggrecan degradation in human intervertebral disc and articular cartilage.

http://www.wikidata.org/entity/Q42987526

description

1997 nî lūn-bûn

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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1997年论文

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1997年论文

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name

Aggrecan degradation in human intervertebral disc and articular cartilage.

@en

Aggrecan degradation in human intervertebral disc and articular cartilage.

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type

label

Aggrecan degradation in human intervertebral disc and articular cartilage.

@en

Aggrecan degradation in human intervertebral disc and articular cartilage.

@nl

prefLabel

Aggrecan degradation in human intervertebral disc and articular cartilage.

@en

Aggrecan degradation in human intervertebral disc and articular cartilage.

@nl

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P1476

Aggrecan degradation in human intervertebral disc and articular cartilage.

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P2093

Alini M

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Mort JS

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Roughley PJ

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Sztrolovics R

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P2860

Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain

Non-proteoglycan forms of biglycan increase with age in human articular cartilage

Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms.

The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B.

Complete coding sequence, deduced primary structure, chromosomal localization, and structural analysis of murine aggrecan.

Proteoglycans: many forms and many functions.

N- and O-linked keratan sulfate on the hyaluronan binding region of aggrecan from mature and immature bovine cartilage.

Cell-mediated catabolism of aggrecan. Evidence that cleavage at the "aggrecanase" site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain.

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235-241

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10.1042/BJ3260235

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326 ( Pt 1)

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