Copper-zinc superoxide dismutase and isolectin B sub(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 in:Neuroscience letters 1997-06, Vol.228 (3), p.163-166
Main Authors: Bidmon, H-J, Oermann, E, Schleicher, A, Kato, K, Kinscherf, R, Buchkremer-Ratzmann, I, Witte, O W, Zilles, K
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container_issue 3
container_start_page 163
container_title Neuroscience letters
container_volume 228
creator Bidmon, H-J
Oermann, E
Schleicher, A
Kato, K
Kinscherf, R
Buchkremer-Ratzmann, I
Witte, O W
Zilles, K
description 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 sub(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 sub(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.
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title Copper-zinc superoxide dismutase and isolectin B sub(4) binding are markers for associative and transhemispheric diaschisis induced by focal ischemia in rat cortex
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