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Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form
Linköping University, Department of Medicine and Health Sciences, Pharmacology . Linköping University, Faculty of Health Sciences.
Linköping University, Department of Medicine and Health Sciences, Pharmacology . Linköping University, Faculty of Health Sciences.
2009 (English)In: AUTOPHAGY, ISSN 1554-8627 , Vol. 5, no 1, 93-95 p.Article in journal (Refereed) Published
Abstract [en]

Lysosomes contain most of the cells supply of labile iron, which makes them sensitive to oxidative stress. To keep lysosomal labile iron at a minimum, a cellular strategy might be to autophagocytose iron-binding proteins that temporarily would chelate iron in a nonredox-active form. Previously we have shown that autophagy of metallothioneins, as well as of non-Fe-saturated ferritin, meets this goal. Here we add another stress-regulated protein to the list, namely HSP70.

Place, publisher, year, edition, pages
2009. Vol. 5, no 1, 93-95 p.
Keyword [en]
apoptosis, autophagy, HSP70, iron, lysosomes, reactive oxygen species (ROS)
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-16884OAI: oai:DiVA.org:liu-16884DiVA: diva2:174431
Available from: 2009-02-22 Created: 2009-02-20 Last updated: 2009-02-22

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Kurz, TinoBrunk , Ulf

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