TY - JOUR
T1 - Superoxide dismutase 1 modulates expression of transferrin receptor
AU - Danzeisen, Ruth
AU - Achsel, Tilmann
AU - Bederke, Ulrich
AU - Cozzolino, Mauro
AU - Crosio, Claudia
AU - Ferri, Alberto
AU - Frenzel, Malte
AU - Gralla, Edith Butler
AU - Huber, Lea
AU - Ludolph, Albert
AU - Nencini, Monica
AU - Rotilio, Giuseppe
AU - Valentine, Joan Selverstone
AU - Carrì, Maria Teresa
PY - 2006/6
Y1 - 2006/6
N2 - Copper-zinc superoxide dismutase (SOD1) plays a protective role against the toxicity of superoxide, and studies in Saccharomyces cerevisiae and in Drosophila have suggested an additional role for SOD1 in iron metabolism. We have studied the effect of the modulation of SOD1 levels on iron metabolism in a cultured human glial cell line and in a mouse motoneuronal cell line. We observed that levels of the transferrin receptor and the iron regulatory protein 1 were modulated in response to altered intracellular levels of superoxide dismutase activity, carried either by wild-type SOD1 or by an SOD-active amyotrophic lateral sclerosis (ALS) mutant enzyme, G93A-SOD1, but not by a superoxide dismutase inactive ALS mutant, H46R-SOD1. Ferritin expression was also increased by wild-type SOD1 overexpression, but not by mutant SOD1s. We propose that changes in superoxide levels due to alteration of SOD1 activity affect iron metabolism in glial and neuronal cells from higher eukaryotes and that this may be relevant to diseases of the nervous system.
AB - Copper-zinc superoxide dismutase (SOD1) plays a protective role against the toxicity of superoxide, and studies in Saccharomyces cerevisiae and in Drosophila have suggested an additional role for SOD1 in iron metabolism. We have studied the effect of the modulation of SOD1 levels on iron metabolism in a cultured human glial cell line and in a mouse motoneuronal cell line. We observed that levels of the transferrin receptor and the iron regulatory protein 1 were modulated in response to altered intracellular levels of superoxide dismutase activity, carried either by wild-type SOD1 or by an SOD-active amyotrophic lateral sclerosis (ALS) mutant enzyme, G93A-SOD1, but not by a superoxide dismutase inactive ALS mutant, H46R-SOD1. Ferritin expression was also increased by wild-type SOD1 overexpression, but not by mutant SOD1s. We propose that changes in superoxide levels due to alteration of SOD1 activity affect iron metabolism in glial and neuronal cells from higher eukaryotes and that this may be relevant to diseases of the nervous system.
KW - Ferritin
KW - Iron metabolism
KW - Iron regulatory protein
KW - Oxidative stress
KW - Superoxide dismutase
KW - Transferrin receptor
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U2 - 10.1007/s00775-006-0099-4
DO - 10.1007/s00775-006-0099-4
M3 - Article
C2 - 16680451
AN - SCOPUS:33745755199
SN - 0949-8257
VL - 11
SP - 489
EP - 498
JO - Journal of Biological Inorganic Chemistry
JF - Journal of Biological Inorganic Chemistry
IS - 4
ER -