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(American Journal of Pathology. 2004;165:227-235.)
© 2004 American Society for Investigative Pathology

Prion Protein Accumulation and Neuroprotection in Hypoxic Brain Damage

Neil F. McLennan*, Paul M. Brennan{dagger}, Alisdair McNeill{dagger}, Ioan Davies{ddagger}, Andrew Fotheringham{ddagger}, Kathleen A. Rennison*, Diane Ritchie§, Francis Brannan{dagger}, Mark W. Head*, James W. Ironside*, Alun Williams§ and Jeanne E. Bell{dagger}

From the National Creutzfeldt-Jakob Disease Surveillance Unit* and Pathology (Neuropathology),{dagger} School of Molecular and Clinical Medicine, University of Edinburgh, Edinburgh; the Biological Gerontology Group,{ddagger} School of Medicine and School of Biological Sciences, University of Manchester, Manchester; and the Neuropathogenesis Unit,§ Institute for Animal Health, Edinburgh, United Kingdom

The function of the normal conformational isoform of prion protein, PrPC, remains unclear although lines of research have suggested a role in the cellular response to oxidative stress. Here we investigate the expression of PrPC in hypoxic brain tissues to examine whether PrPC is in part regulated by neuronal stress. Cases of adult cerebral ischemia and perinatal hypoxic-ischemic injury in humans were compared with control tissues. PrPC immunoreactivity accumulates within neuronal processes in the penumbra of hypoxic damage in adult brain, and within neuronal soma in cases of perinatal hypoxic-ischemic injury, and in situ hybridization analysis suggests an up-regulation of PrP mRNA during hypoxia. Rodents also showed an accumulation of PrPC in neuronal soma within the penumbra of ischemic lesions. Furthermore, the infarct size in PrP-null mice was significantly greater than in the wild type, supporting the proposed role for PrPC in the neuroprotective adaptive cellular response to hypoxic injury.




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