Amyloid-β increases metallo- and cysteine protease activities in human macrophages.

@article{Castellano2014AmyloidIM,
  title={Amyloid-β increases metallo- and cysteine protease activities in human macrophages.},
  author={Jos{\'e} Castellano and Lina Badimon and Vicenta Llorente-Cort{\'e}s},
  journal={Journal of vascular research},
  year={2014},
  volume={51 1},
  pages={
          58-67
        }
}
BACKGROUND/AIMS Amyloid-β (Aβ) plays a crucial role in the onset and progression of atherosclerosis. Macrophages are a source of matrix metalloproteinases (MMPs), cysteine proteases and transforming growth factor (TGF)-β1 in the vascular wall. The aims of this study were to analyze the capacity of Aβ peptide (1-40) (Aβ40), Aβ peptide (1-42) (Aβ42) and fibrillar Aβ42 (fAβ42) to modulate the expression and activity of MMP-9, MMP-2 and tissue inhibitor of MMP-1 (TIMP-1) in human monocyte-derived… CONTINUE READING

References

Publications referenced by this paper.
SHOWING 1-10 OF 53 REFERENCES

Structural and mechanistic commonalities of amyloid-β and the prion protein

B Da Costa Dias, K Jovanovic, D Gonsalves, SF Weiss
  • Prion
  • 2011

Fibronec - tin fragments mediate matrix metalloproteinase upregulation and cartilage damage through proline rich tyrosine kinase 2 , csrc , NF - κB and protein kinase Cδ

RF Loeser, CB Forsyth, AM Samarel, HJ Im
  • Osteoarthritis Cartilage
  • 2009

Macrophage-mediated degradation of beta-amyloid via an apolipoprotein E isoform-dependent mechanism.

  • The Journal of neuroscience : the official journal of the Society for Neuroscience
  • 2009

Reassessing the amyloid cascade hypothesis of Alzheimer's disease.

  • The international journal of biochemistry & cell biology
  • 2009