Impairment of the collagenase-3 endocytotic receptor system in cells from patients with osteoarthritis.

@article{Walling2003ImpairmentOT,
  title={Impairment of the collagenase-3 endocytotic receptor system in cells from patients with osteoarthritis.},
  author={Hobart W Walling and Liza Jane Raggatt and Donald Irvine and O Y Barmina and J E Toledano and Mary B Goldring and Keith A. Hruska and Huston Davis Adkisson and R E Burdge and Charles J. Gatt and Daniel Harwood and Nicola C Partridge},
  journal={Osteoarthritis and cartilage},
  year={2003},
  volume={11 12},
  pages={854-63}
}
OBJECTIVE Collagenase-3, a matrix metalloproteinase (MMP-13) that can degrade collagen II and aggrecan, is produced by osteoarthritic (OA) chondrocytes and may contribute to matrix destruction in this disease. Our laboratory has previously identified a specific endocytotic receptor for collagenase-3 on osteoblastic and fibroblastic cells, which couples with the low-density lipoprotein receptor-related protein (LRP1) to mediate the internalization and degradation of this enzyme. We hypothesized… CONTINUE READING

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We hypothesized that the activity of this receptor system is reduced in OA chondrocytes which may lead to increased local extracellular levels of collagenase-3 and increased destruction of the cartilage matrix at pericellular sites .
These results suggest a mechanism whereby impaired receptor - mediated removal of collagenase-3 in OA chondrocytes may lead to enhanced local degradation of the cartilage matrix .
Human chondrocytes and synoviocytes were obtained from OA knees at the time of joint replacement surgery and from non - arthritic control specimens following autopsy or surgery .
OA chondrocytes and synoviocytes demonstrated significantly reduced ( 75 - 77% ) binding of recombinant 125I collagenase-3 .
OA chondrocytes and synoviocytes demonstrated significantly reduced ( 75 - 77% ) binding of recombinant 125I collagenase-3 .
Human chondrocytes and synoviocytes were obtained from OA knees at the time of joint replacement surgery and from non - arthritic control specimens following autopsy or surgery .
These results suggest a mechanism whereby impaired receptor - mediated removal of collagenase-3 in OA chondrocytes may lead to enhanced local degradation of the cartilage matrix .
We hypothesized that the activity of this receptor system is reduced in OA chondrocytes which may lead to increased local extracellular levels of collagenase-3 and increased destruction of the cartilage matrix at pericellular sites .
ChondrocyteAnatomic structure is physical part ofCartilage
These results suggest a mechanism whereby impaired receptor - mediated removal of collagenase-3 in OA chondrocytes may lead to enhanced local degradation of the cartilage matrix .
We hypothesized that the activity of this receptor system is reduced in OA chondrocytes which may lead to increased local extracellular levels of collagenase-3 and increased destruction of the cartilage matrix at pericellular sites .
Collagenase-3 , a matrix metalloproteinase ( MMP-13 ) that can degrade collagen II and aggrecan , is produced by osteoarthritic ( OA ) chondrocytes and may contribute to matrix destruction in this disease .
Iodinated collagenase-3 was used to analyze the cell - surface binding , internalization and intracellular degradation of collagenase-3 .
Collagenase-3 , a matrix metalloproteinase ( MMP-13 ) that can degrade collagen II and aggrecan , is produced by osteoarthritic ( OA ) chondrocytes and may contribute to matrix destruction in this disease .
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