TY  - JOUR
A1  - Doppler, Kathrin
A1  - Appeltshauser, Luise
A1  - Krämer, Heidrun H.
A1  - King Man Ng, Judy
A1  - Meinl, Edgar
A1  - Villmann, Carmen
A1  - Brophy, Peter
A1  - Dib-Hajj, Sulayman D.
A1  - Waxman, Stephen G.
A1  - Weishaupt, Andreas
A1  - Sommer, Claudia
T1  - Contactin-1 and Neurofascin-155/-186 Are Not Targets of Auto-Antibodies in Multifocal Motor Neuropathy
JF  - PLoS One
N2  - Multifocal motor neuropathy is an immune mediated disease presenting with multifocal muscle weakness and conduction block. IgM auto-antibodies against the ganglioside GM1 are detectable in about 50% of the patients. Auto-antibodies against the paranodal proteins contactin-1 and neurofascin-155 and the nodal protein neurofascin-186 have been detected in subgroups of patients with chronic inflammatory demyelinating polyneuropathy. Recently, auto-antibodies against neurofascin-186 and gliomedin were described in more than 60% of patients with multifocal motor neuropathy. In the current study, we aimed to validate this finding, using a combination of different assays for auto-antibody detection. In addition we intended to detect further auto-antibodies against paranodal proteins, specifically contactin-1 and neurofascin-155 in multifocal motor neuropathy patients’ sera. We analyzed sera of 33 patients with well-characterized multifocal motor neuropathy for IgM or IgG anti-contactin-1, anti-neurofascin-155 or -186 antibodies using enzyme-linked immunosorbent assay, binding assays with transfected human embryonic kidney 293 cells and murine teased fibers. We did not detect any IgM or IgG auto-antibodies against contactin-1, neurofascin-155 or -186 in any of our multifocal motor neuropathy patients. We conclude that auto-antibodies against contactin-1, neurofascin-155 and -186 do not play a relevant role in the pathogenesis in this cohort with multifocal motor neuropathy.
KW  - motor proteins
KW  - enzyme-linked immunoassays
KW  - binding analysis
KW  - neuropathy
KW  - nerve fibers
KW  - cell binding assay
KW  - antibodies
KW  - enzyme assays
Y1  - 2015
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-126156
VL  - 10
IS  - 7
ER  - 
TY  - JOUR
A1  - Ott, Christine
A1  - Dorsch, Eva
A1  - Fraunholz, Martin
A1  - Straub, Sebastian
A1  - Kozjak-Pavlovic, Vera
T1  - Detailed Analysis of the Human Mitochondrial Contact Site Complex Indicate a Hierarchy of Subunits
JF  - PLoS One
N2  - Mitochondrial inner membrane folds into cristae, which significantly increase its surface and are important for mitochondrial function. The stability of cristae depends on the mitochondrial contact site (MICOS) complex. In human mitochondria, the inner membrane MICOS complex interacts with the outer membrane sorting and assembly machinery (SAM) complex, to form the mitochondrial intermembrane space bridging complex (MIB). We have created knockdown cell lines of most of the MICOS and MIB components and have used them to study the importance of the individual subunits for the cristae formation and complex stability. We show that the most important subunits of the MIB complex in human mitochondria are Mic60/Mitofilin, Mic19/CHCHD3 and an outer membrane component Sam50. We provide additional proof that ApoO indeed is a subunit of the MICOS and MIB complexes and propose the name Mic23 for this protein. According to our results, Mic25/CHCHD6, Mic27/ApoOL and Mic23/ApoO appear to be periphery subunits of the MICOS complex, because their depletion does not affect cristae morphology or stability of other components.
KW  - co-immunoprecipitation
KW  - motor proteins
KW  - mitochondria
KW  - membrane potential
KW  - membrane proteins
KW  - protein complexes
KW  - mitochondrial membrane
KW  - outer membrane proteins
Y1  - 2015
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-125347
VL  - 10
IS  - 3
ER  -