4.4 Article

Heparan sulfate mediates amyloid-beta internalization and cytotoxicity

期刊

GLYCOBIOLOGY
卷 20, 期 5, 页码 533-541

出版社

OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwp205

关键词

A beta; cytotoxicity; heparanase; heparan sulfate; heparin

资金

  1. Swedish Research Council [K2009-67X-21128-01-3]
  2. European commission for Systemic Amyloidoses (EURAMY)
  3. Mizutani Foundation for Glycoscience
  4. Polysackaridforskning Foundation (Uppsala, Sweden)
  5. Demensfrbundet (Stockholm)
  6. Stohnes Stiftelse (Bromma, Sweden)
  7. Landstinget i Uppsala Lan

向作者/读者索取更多资源

Heparan sulfate (HS) has been found associated with amyloid deposits, including the toxic amyloid-beta (A beta) peptide aggregates in cerebral vasculature and neuronal tissues in patients with Alzheimer's disease. However, the pathophysiological significance of the HS-A beta interaction has remained unclear. In the present study, we applied cell models to gain insight into the roles of HS in relation to A beta toxicity. Wild-type Chinese hamster ovary (CHO-WT) cells showed loss of viability following exposure to A beta 40, whereas the HS-deficient cell line, pgsD-677, was essentially resistant. Immunocytochemical analysis showed A beta internalization by CHO-WT, but not pgsD-677 cells. A beta 40 toxicity was also attenuated in human embryonic kidney cells overexpressing heparanase. Finally, addition of heparin to human umbilical vein endothelial cells prevented internalization of added A beta 40 and protected against A beta toxicity. Taken together, these findings suggest that cell-surface HS mediates A beta internalization and toxicity.

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