Activation of matrix metalloproteinases 2, 9, and 13 by activated protein C in human osteoarthritic cartilage chondrocytes. (Q53064724)

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8 March 2020

title

Activation of matrix metalloproteinases 2, 9, and 13 by activated protein C in human osteoarthritic cartilage chondrocytes (English)

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8 March 2020

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8 March 2020

Christopher B Little

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8 March 2020

author name string

Miriam T Jackson

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8 March 2020

Margaret M Smith

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8 March 2020

Christopher J Jackson

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8 March 2020

publication date

1 June 2014

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8 March 2020

published in

Arthritis & Rheumatology

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8 March 2020

volume

66

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8 March 2020

issue

6

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8 March 2020

page(s)

1525-1536

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Gene expression of matrix metalloproteinases 1, 3, and 9 by chondrocytes in osteoarthritic human knee articular cartilage is zone and grade specific

8 March 2020

cites work

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Elevation of activated protein C in synovial joints in rheumatoid arthritis and its correlation with matrix metalloproteinase 2

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Protein C activation on endothelial cells by prothrombin activation products generated in situ: meizothrombin is a better protein C activator than alpha-thrombin

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Activation of cartilage matrix metalloproteinases by activated protein C.

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Matrix metalloproteinases are involved in C-terminal and interglobular domain processing of cartilage aggrecan in late stage cartilage degradation

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Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro

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Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro.

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The alpha 2 chain of collagen type VI sequesters latent proforms of matrix-metalloproteinases and modulates their activation and activity.

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Discoidin domain receptor 2 is associated with the increased expression of matrix metalloproteinase-13 in synovial fibroblasts of rheumatoid arthritis.

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Laminin alpha 3 LG4 module induces matrix metalloproteinase-1 through mitogen-activated protein kinase signaling.

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Cytokine induced metalloproteinase expression and activity does not correlate with focal susceptibility of articular cartilage to degeneration.

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Matrix metalloproteinase and proinflammatory cytokine production by chondrocytes of human osteoarthritic cartilage: associations with degenerative changes

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Freshly isolated osteoarthritic chondrocytes are catabolically more active than normal chondrocytes, but less responsive to catabolic stimulation with interleukin-1beta

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Activation of the 92-kDa gelatinase by stromelysin and 4-aminophenylmercuric acetate. Differential processing and stabilization of the carboxyl-terminal domain by tissue inhibitor of metalloproteinases (TIMP).

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Activation of endothelial cell protease activated receptor 1 by the protein C pathway

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