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Submitted on August 31, 2004
Revised on February 10, 2005
Accepted on April 25, 2005

Subcellular proteomics of neuromelanin granules isolated from the human brain

Florian Tribl, Manfred Gerlach, Katrin Marcus, Esther Asan, Thomas Tatschner, Thomas Arzberger, Helmut E. Meyer, Gerhard Bringmann, and Peter Riederer

Department of Clinical Neurochemistry, University of Wurzburg, Wuerzburg, Germany D-97080

Corresponding Author: florian.tribl{at}web.de

‘Subcellular proteomics’ is currently the most effective approach to characterize subcellular compartments. Based on the powerful combination of subcellular fractionation and protein identification by liquid chromatography coupled to electrospray tandem mass spectrometry (LC-MS/MS) we were able for the first time to (1) isolate intact neuromelanin granules from the human brain and (2) to establish the first protein profile of these granules. This compartment containing neuromelanin (NM) is primarily located in the primate’s substantia nigra (SN), one of the main brain regions degenerating in Parkinson’s disease. We employed mechanic tissue disaggregation, discontinuous sucrose gradient centrifugation, cell disruption, and organelle separation to isolate NM granules from human SN. Using transmission electron microscopy we demonstrated that the morphological characteristics of the isolated NM granules are similar to those described in human brain tissue. Fundamentally, we found numerous proteins definitely demonstrating a close relationship of NM-containing granules with lysosomes or lysosome-related organelles originating from the endosome-lysosome lineage. Intriguingly, we further revealed the presence of endoplasmatic reticulum derived chaperones, especially the transmembrane protein calnexin, which has recently been located in lysosome-related melanosomes and has been suggested to be a melanogenic chaperone.


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