Document Detail


Contribution of calpain activation to early stages of hippocampal damage during oxygen-glucose deprivation.
MedLine Citation:
PMID:  18207136     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Calpains are Ca(2+)-activated enzymes which cleave cytoskeletal and other proteins, contributing to neuronal damage in conditions of pathological intracellular Ca(2+) elevation, including stroke. However, the consequences of calpain overactivation have typically been observed hours after insult. To identify the earliest events attributable to calpain activation, and thus potentially isolate calpain substrates involved in acute neuronal damage, we dynamically recorded the effects of calpain inhibition in an in vitro model of stroke. Extracellular DC potentials and fEPSPs were monitored together with changes of light transmittance (as a measure of cell and mitochondrial swelling) and Rh 123 fluorescence (to monitor mitochondrial membrane potential; DeltaPsi(m)) in hippocampal slices obtained from P12-P17 rats. No differences were observed in the latencies of fEPSP disruption or onset of extracellular DC shifts associated with hypoxic spreading depression (HSD) evoked by oxygen-glucose deprivation (OGD) under control conditions or in the presence of calpain inhibitor III (MDL 28170). However, a significant difference was observed in transmitted light signals during OGD with calpain inhibition. Given the potential contribution of mitochondrial swelling to changes in light transmittance, these experiments were also conducted in the presence of cyclosporin A to block opening of the mitochondrial permeability transition pore (MPTP). Our results indicate that differences in OGD-induced changes of light transmittance in the presence of MDL 28170 are not likely the result of MPTP blockade or changes in dendritic beading. We propose that calpain inhibition may alter changes in light transmittance by limiting conformational changes of mitochondria.
Authors:
Michael Grammer; Dong Li; Nirubhana Arunthavasothy; Janusz Lipski
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-12-08
Journal Detail:
Title:  Brain research     Volume:  1196     ISSN:  0006-8993     ISO Abbreviation:  Brain Res.     Publication Date:  2008 Feb 
Date Detail:
Created Date:  2008-02-18     Completed Date:  2008-05-30     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0045503     Medline TA:  Brain Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  121-30     Citation Subset:  IM    
Affiliation:
Department of Physiology, Faculty of Medical and Health Sciences, University of Auckland, 85 Park Road, Grafton, Auckland 1023, New Zealand. m.grammer@auckland.ac.nz
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MeSH Terms
Descriptor/Qualifier:
Animals
Animals, Newborn
Anoxia / complications*
Brain Injuries / etiology*,  pathology*
Calpain / metabolism*
Cortical Spreading Depression / drug effects,  physiology
Cysteine Proteinase Inhibitors / pharmacology
Dipeptides / pharmacology
Edema / etiology,  pathology
Electric Stimulation / methods
Excitatory Postsynaptic Potentials / drug effects,  physiology,  radiation effects
Glucose / deficiency*
Hippocampus / drug effects,  metabolism*
Membrane Potential, Mitochondrial / drug effects,  physiology,  radiation effects
Rats
Rats, Wistar
Tissue Culture Techniques
Chemical
Reg. No./Substance:
0/Cysteine Proteinase Inhibitors; 0/Dipeptides; 50-99-7/Glucose; 88191-84-8/calpain inhibitor III; EC 3.4.22.-/Calpain

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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