A novel giant peroxisomal superoxide dismutase motif-containing protein.
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A novel giant peroxisomal superoxide dismutase motif-containing protein. / Toutzaris, Diamandis; Lewerenz, Jan; Albrecht, Philipp; Jensen, Laran T; Letz, Julia; Geerts, Andreas; Golz, Stefan; Methner, Axel.
in: FREE RADICAL BIO MED, Jahrgang 48, Nr. 6, 6, 2010, S. 811-820.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - A novel giant peroxisomal superoxide dismutase motif-containing protein.
AU - Toutzaris, Diamandis
AU - Lewerenz, Jan
AU - Albrecht, Philipp
AU - Jensen, Laran T
AU - Letz, Julia
AU - Geerts, Andreas
AU - Golz, Stefan
AU - Methner, Axel
PY - 2010
Y1 - 2010
N2 - Oxidative glutamate toxicity in the neuronal cell line HT22 is a model for neuronal cell death by oxidative stress. In this model, extracellular glutamate blocks cystine uptake via the glutamate/cystine antiporter system x(c)(), eventually leading to depletion of the antioxidant glutathione and cell death. We used subtractive suppression hybridization and a screening procedure using various HT22 sublines to identify transcripts relevantly upregulated in resistance to oxidative glutamate toxicity. One of these coded for a novel protein of 3440 amino acids comprising a superoxide dismutase (SOD) motif, which we named TIGR for "transcript increased in glutamate resistance." TIGR is mainly expressed in the nervous system in cortical pyramidal and hippocampal neurons. Intracellularly, TIGR colocalizes with catalase, strongly suggesting a peroxisomal localization. Overexpression of TIGR but not of a mutant lacking two conserved histidine residues in the SOD motif increased SOD activity and protected against oxidative stress in mammalian cells, but had no direct SOD activity in yeast. We conclude that this novel giant peroxisomal protein is implicated in resistance to oxidative stress. Despite the presence of a SOD motif, which is necessary for protection in mammalian cells, the protein is not a functional SOD, but might be involved in SOD activity.
AB - Oxidative glutamate toxicity in the neuronal cell line HT22 is a model for neuronal cell death by oxidative stress. In this model, extracellular glutamate blocks cystine uptake via the glutamate/cystine antiporter system x(c)(), eventually leading to depletion of the antioxidant glutathione and cell death. We used subtractive suppression hybridization and a screening procedure using various HT22 sublines to identify transcripts relevantly upregulated in resistance to oxidative glutamate toxicity. One of these coded for a novel protein of 3440 amino acids comprising a superoxide dismutase (SOD) motif, which we named TIGR for "transcript increased in glutamate resistance." TIGR is mainly expressed in the nervous system in cortical pyramidal and hippocampal neurons. Intracellularly, TIGR colocalizes with catalase, strongly suggesting a peroxisomal localization. Overexpression of TIGR but not of a mutant lacking two conserved histidine residues in the SOD motif increased SOD activity and protected against oxidative stress in mammalian cells, but had no direct SOD activity in yeast. We conclude that this novel giant peroxisomal protein is implicated in resistance to oxidative stress. Despite the presence of a SOD motif, which is necessary for protection in mammalian cells, the protein is not a functional SOD, but might be involved in SOD activity.
M3 - SCORING: Zeitschriftenaufsatz
VL - 48
SP - 811
EP - 820
JO - FREE RADICAL BIO MED
JF - FREE RADICAL BIO MED
SN - 0891-5849
IS - 6
M1 - 6
ER -
