Molecular basis of morphological changes in mitochondrial membrane accompanying induction of permeability transition, as revealed by immuno-electron microscopy.
The mitochondrial inner membrane typically shows a condensed structure when examined by electron microscopy. However, this typical structure is known to disappear upon induction of the mitochondrial permeability transition (PT). This change in the appearance of the mitochondrial membrane structure that accompanies the induction of PT is thought to reflect changes in the permeability of inner mitochondrial membrane; however, its molecular basis has remained uncertain. In the present study, changes in membrane status were examined by immuno-electron microscopy using antibodies against the voltage-dependent anion channel (VDAC), beta-subunit of F1-ATPase (F1beta), and cytochrome c (cyt. c). In control mitochondria, antibody against VDAC was observed at the rim of the mitochondria, whereas antibodies against F1beta and cytochrome c bound these molecules inside of the mitochondria. However, in PT-induced mitochondria, all three antibodies were observed at the mitochondrial rim. These results strongly suggest that the inner mitochondrial membrane is shoved to the rim region of mitochondria upon induction of mitochondrial PT.
Terauchi
Satsuki
S
Institute for Genome Research, University of Tokushima, Kuramotocho-3, Tokushima 770-8503, Japan.
Yamamoto
Takenori
T
Yamashita
Kikuji
K
Kataoka
Masatoshi
M
Terada
Hiroshi
H
Shinohara
Yasuo
Y
D000818:Animals; D000918:Antibody Specificity; D045304:Cytochromes c / Q000032:analysis / Q000276:immunology; D007425:Intracellular Membranes / Q000276:immunology / Q000648:ultrastructure*; D008297:Male; D016253:Microscopy, Immunoelectron; D008930:Mitochondria, Liver / Q000502:physiology / Q000648:ultrastructure*; D010539:Permeability / Q000187:drug effects; D018272:Porins / Q000032:analysis / Q000276:immunology; D006180:Proton-Translocating ATPases / Q000032:analysis / Q000276:immunology; D011817:Rabbits; D051381:Rats; D017208:Rats, Wistar; D050994:Voltage-Dependent Anion Channels
D018272:Porins; D050994:Voltage-Dependent Anion Channels; D045304:Cytochromes c; D006180:Proton-Translocating ATPases