English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Endosomes: another extra-mitochondrial location of type-1 porin/voltage-dependent anion-selective channels (VDAC)

MPS-Authors

Reymann,  Susanne
Max Planck Institute of Experimental Medicine, Max Planck Society;

/persons/resource/persons137691

Haase,  Winfried
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons182449

Thinnes,  Friedrich P.
Max Planck Institute of Experimental Medicine, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Reymann, S., Haase, W., Krick, W., Burckhardt, G., & Thinnes, F. P. (1998). Endosomes: another extra-mitochondrial location of type-1 porin/voltage-dependent anion-selective channels (VDAC). Pflügers Archiv: European Journal of Physiology, 436, 478-480. doi:10.1007/s004240050659.


Cite as: https://hdl.handle.net/21.11116/0000-0007-A277-C
Abstract
Endocytotic vesicles (EV) isolated from rat renal cortex were subjected to SDS-polyacrylamide gel electrophoresis and Western blotting. A monoclonal antibody against human type-1 porin (31 kDa) detected a strong band of 31 kDa. The same antibody has been used as the primary antibody in indirect immunocytochemistry. Light microscopy of cryostat sections of rat renal cortex showed a heavy staining of EV underneath the brush-border membrane. Electron microscopy was performed by ”preembedding immunogold staining” of rat renal cortex, the sections of which showed an extensive labelling of EV with gold particles. These results demonstrate that the expression of type-1 porin is not restricted to outer mitochondrial membranes. The biological function of endosomal type-1 porin has as yet to be ascertained.