Copper-zinc superoxide dismutase and isolectin B 4 binding are markers for associative and transhemispheric diaschisis induced by focal ischemia in rat cortex

Copper/zinc-superoxide dismutase (Cu/Zn-SOD) belongs to a class of enzymes, identified as essential and highly effective endogenous scavengers of cytotoxic oxygen radicals. These radicals contribute to postlesional neurotoxicity. In order to determine the superoxide-scavenging potential of regions a...

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Published inNeuroscience letters Vol. 228; no. 3; pp. 163 - 166
Main Authors Bidmon, Hans-J, Oermann, Evelyn, Schleicher, Axel, Kato, Kanefusa, Kinscherf, Ralf, Buchkremer-Ratzmann, Irmgard, Witte, Otto W, Zilles, Karl
Format Journal Article
LanguageEnglish
Published Elsevier Ireland Ltd 13.06.1997
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Summary:Copper/zinc-superoxide dismutase (Cu/Zn-SOD) belongs to a class of enzymes, identified as essential and highly effective endogenous scavengers of cytotoxic oxygen radicals. These radicals contribute to postlesional neurotoxicity. In order to determine the superoxide-scavenging potential of regions affected by unilateral cortical photothrombosis, we studied the changes in the distribution of Cu/Zn-SOD and the appearance of activated microglia by immunohistochemistry and isolectin B 4 binding. Four hours postlesion, Cu/Zn-SOD increased significantly within a homotopic area of the contralateral hemisphere and in ipsilateral thalamic nuclei, whereas isolectin B 4-positive microglia were upregulated at days 5 and 7 postlesion within the same regions. The contralateral increase in the amount of the superoxide-scavenging Cu/Zn-SOD indicates that this enzyme is induced by a retrograde reaction carried through callosal connections.
ISSN:0304-3940
1872-7972
DOI:10.1016/S0304-3940(97)00389-3