Oxidative stress causes reversible changes in mitochondrial permeability and structure.
Mitochondria are a primary source as well a principal target of reactive oxygen species within cells. Using immunofluorescence microscopy, we have found that a number of mitochondrial matrix proteins are normally undetectable in formaldehyde-fixed cells permeabilized with the cholesterol-binding detergent saponin. However, exogenous or endogenous oxidative stress applied prior to fixation altered the permeability of mitochondria, rendering these matrix proteins accessible to antibodies. Electron microscopy revealed a loss of matrix density and disorganization of inner membrane cristae upon oxidative stress. Notably, the changes in permeability and in structure were rapidly reversed when the oxidative stress was relieved. The ability of reactive oxygen species to reversibly alter the permeability of the mitochondrial membrane provides a potential mechanism for communication within the cell such as between nucleus and mitochondria.
Cole
Nelson B
NB
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892-8012, USA. ncole@nhlbi.nih.gov
Daniels
Mathew P
MP
Levine
Rodney L
RL
Kim
Geumsoo
G
D000818:Animals; D001693:Biological Transport, Active; D002460:Cell Line; D005949:Glucose Oxidase / Q000378:metabolism / Q000494:pharmacology; D051150:Methionine Sulfoxide Reductases / Q000235:genetics / Q000378:metabolism; D051379:Mice; D046529:Microscopy, Electron, Transmission; D008856:Microscopy, Fluorescence; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure*; D051336:Mitochondrial Membranes / Q000378:metabolism; D018384:Oxidative Stress; D010539:Permeability; D017382:Reactive Oxygen Species / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D017382:Reactive Oxygen Species; D011994:Recombinant Proteins; D005949:Glucose Oxidase; D051150:Methionine Sulfoxide Reductases; C027219:methionine sulfoxide reductase