A comparison of cathepsin B processing and distribution during neuronal death in rats following global ischemia or decapitation necrosis.
The objective of this study was to examine the possible role of the cysteine protease cathepsin B (E.C. 3.4.22.1) in the delayed neuronal death in rats subjected to the two-vessel occlusion model of global ischemia. Immunohistochemistry of the hippocampus showed an alteration in the distribution of cathepsin B in CA1 neurons from a lysosomal pattern to a more intense label redistributed into the cytoplasm. This change was not detected until the neurons had become morphologically altered with obvious shrinkage of the cytoplasmic region. Western blotting and enzyme activity measurements of subcellular fractions, including lysosomes and a cell soluble fraction, demonstrated that there was an overall decrease in cathepsin B activity at this time but an increase in the proenzyme form, particularly in the soluble fraction. This was found to be completely different from the marked loss of all forms of cathepsin B in necrotic neurons following decapitation.
Hill
I E
IE
Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ont. irene.hill@nrc.ca
Preston
E
E
Monette
R
R
MacManus
J P
JP
D000818:Animals; D015153:Blotting, Western; D002545:Brain Ischemia / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology*; D002401:Cathepsin B / Q000378:metabolism*; D016923:Cell Death; D003655:Decerebrate State / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology*; D007150:Immunohistochemistry; D008297:Male; D009336:Necrosis; D009474:Neurons / Q000502:physiology*; D011499:Protein Processing, Post-Translational; D051381:Rats; D017207:Rats, Sprague-Dawley; D013997:Time Factors; D014018:Tissue Distribution
D002401:Cathepsin B