title: Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form.
abstract: Lysosomes contain most of the cell's 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 non-redox-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.
authors.affiliation: Division of Pharmacology, Faculty of Health Sciences, Linköping University, Linköping, Sweden.
authors.forename: Tino
authors.initials: T
authors.lastname: Kurz
authors.forename: Ulf T
authors.initials: UT
authors.lastname: Brunk
mesh_terms: D001343:Autophagy / Q000187:drug effects*; D005293:Ferritins / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D007502:Iron Chelating Agents / Q000494:pharmacology*; D008247:Lysosomes / Q000187:drug effects* / Q000378:metabolism*; D010084:Oxidation-Reduction / Q000187:drug effects; D018384:Oxidative Stress / Q000187:drug effects
chemical_list: D018840:HSP70 Heat-Shock Proteins; D007502:Iron Chelating Agents; D005293:Ferritins; D007501:Iron