The 70 kDa heat shock protein suppresses matrix metalloproteinases in astrocytes

Jong Eun Lee, Yeun Jung Kim, Jong Youl Kim, Won Taek Lee, Midori A. Yenari, Rona G. Giffard

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)


The 70 kDa heat shock protein (Hsp70) is synthesized in response to a variety of stresses, including ischemia, and is thought to act as a molecular chaperone to prevent protein denaturation and facilitate: protein folding. Matrix metalloproteinases (MMPs), a family of serine proteases, are also upregulated by ischemia and are thought to promote cell death and tissue injury.We examined the influence of Hsp70 on expression and activity of MMPs. Astrocyte cultures were prepared from neonatal mice and transfected with retroviral vectors containing hsp70 or lacZ or mock infected, then exposed to oxygen-glucose deprivation followed by reperfusion. Zymograms and Western blots showed that Hsp70 over-expression suppressed MMP-2 and MMP-9. These findings suggest that Hsp70 may protect by regulating MMPs.

Original languageEnglish
Pages (from-to)499-502
Number of pages4
Issue number3
Publication statusPublished - 2004 Mar

All Science Journal Classification (ASJC) codes

  • General Neuroscience


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