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Bcl-2 phosphorylation in the BH4 domain precedes caspase-3 activation and cell death after neonatal cerebral hypoxic-ischemic injury

Journal article
Authors Ulrika Hallin
Eisaku Kondo
Yasuhiko Ozaki
Henrik Hagberg
Futoshi Shibasaki
Klas Blomgren
Published in Neurobiol Dis
Volume 21
Issue 3
Pages 478-86
Publication year 2006
Published at Institute of Neuroscience and Physiology, Department of Physiology
Institute of Neuroscience and Physiology, Department of Clinical Neuroscience and Rehabilitation
Institute of Clinical Sciences
Pages 478-86
Language en
Links www.ncbi.nlm.nih.gov/entrez/query.f...
Keywords Animals, Animals, Newborn, Apoptosis/*physiology, Biological Markers, Blotting, Western, Caspase 3, Caspases/*metabolism, Disease Models, Animal, Enzyme Activation/physiology, Female, Fluorescent Antibody Technique, Hypoxia-Ischemia, Brain/*physiopathology, Male, Neurons/metabolism/pathology, Phosphorylation, Proto-Oncogene Proteins c-bcl-2/*metabolism, Rats, Rats, Wistar, Serine/chemistry/immunology/metabolism
Subject categories Medical and Health Sciences

Abstract

To date, there are very few in vivo studies addressing the role of Bcl-2 phosphorylation. In a model of neonatal hypoxic-ischemic (HI) brain injury, we characterized the spatial and temporal phosphorylation of Bcl-2 at serine-24 (PS24-Bcl-2), using a site-specific antibody. Very few cells positive for PS24-Bcl-2 were found in control animals, but the number increased during reperfusion in all investigated brain areas in the ipsilateral hemisphere after HI, particularly in the border region between intact and damaged tissue. The highest numbers were encountered 24 h post-HI. Phosphorylation of Bcl-2 at serine-24 coincided with cytochrome c release after hypoxia-ischemia and preceded caspase-3 activation. Injured neurons displayed a predominantly nuclear, but also mitochondrial, localization of PS24-Bcl-2 immunoreactivity. In conclusion, phosphorylation of Bcl-2 at serine 24 was induced by hypoxia-ischemia, presumably resulting in loss of its anti-apoptotic function.

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