The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated
(2013) In Journal of Proteome Research 12(4). p.1764-1771- Abstract
- O-Mannosylation is an important protein modification in brain. During the last years, a few mammalian proteins have been identified as targets of the protein-O-mannosyltransferases 1 and 2. However, these still cannot explain the high content of O-mannosyl glycans in brain and the strong brain involvement of congenital muscular dystrophies caused by POMT mutations (Walker-Warburg syndrome, dystroglycanopathies). By fractionating and analyzing the glycoproteome of mouse and calf brain lysates, we could show that proteins of the perineural net, the lecticans, are O-mannosylated, indicating that major components of neuronal extracellular matrix are O-mannosylated in mammalian brain. This finding corresponds with the high content of O-mannosyl... (More)
- O-Mannosylation is an important protein modification in brain. During the last years, a few mammalian proteins have been identified as targets of the protein-O-mannosyltransferases 1 and 2. However, these still cannot explain the high content of O-mannosyl glycans in brain and the strong brain involvement of congenital muscular dystrophies caused by POMT mutations (Walker-Warburg syndrome, dystroglycanopathies). By fractionating and analyzing the glycoproteome of mouse and calf brain lysates, we could show that proteins of the perineural net, the lecticans, are O-mannosylated, indicating that major components of neuronal extracellular matrix are O-mannosylated in mammalian brain. This finding corresponds with the high content of O-mannosyl glycans in brain as well as with the brain involvement of dystroglycanopathies. In contrast, the lectican neurocan is not O-mannosylated when recombinantly expressed in EBNA-293 cells, revealing the possibility of different control mechanisms for the initiation of O-mannosylation in different cell types. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3739175
- author
- Pacharra, Sandra ; Hanisch, Franz-Georg ; Muehlenhoff, Martina ; Faissner, Andreas ; Rauch, Uwe LU and Breloy, Isabelle
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- O-glycans, O-mannosylation, lecticans, ECM, perineural net, O-glycosylation, ESI-MS/MS, MALDI-MS/MS, glycoproteomics, dystroglycanopathies
- in
- Journal of Proteome Research
- volume
- 12
- issue
- 4
- pages
- 1764 - 1771
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000317327500021
- scopus:84875912842
- pmid:23428289
- ISSN
- 1535-3893
- DOI
- 10.1021/pr3011028
- language
- English
- LU publication?
- yes
- id
- 696bda00-8a8c-44e6-a2b8-ebf892c4b9ee (old id 3739175)
- date added to LUP
- 2016-04-01 11:01:25
- date last changed
- 2022-03-20 02:11:20
@article{696bda00-8a8c-44e6-a2b8-ebf892c4b9ee, abstract = {{O-Mannosylation is an important protein modification in brain. During the last years, a few mammalian proteins have been identified as targets of the protein-O-mannosyltransferases 1 and 2. However, these still cannot explain the high content of O-mannosyl glycans in brain and the strong brain involvement of congenital muscular dystrophies caused by POMT mutations (Walker-Warburg syndrome, dystroglycanopathies). By fractionating and analyzing the glycoproteome of mouse and calf brain lysates, we could show that proteins of the perineural net, the lecticans, are O-mannosylated, indicating that major components of neuronal extracellular matrix are O-mannosylated in mammalian brain. This finding corresponds with the high content of O-mannosyl glycans in brain as well as with the brain involvement of dystroglycanopathies. In contrast, the lectican neurocan is not O-mannosylated when recombinantly expressed in EBNA-293 cells, revealing the possibility of different control mechanisms for the initiation of O-mannosylation in different cell types.}}, author = {{Pacharra, Sandra and Hanisch, Franz-Georg and Muehlenhoff, Martina and Faissner, Andreas and Rauch, Uwe and Breloy, Isabelle}}, issn = {{1535-3893}}, keywords = {{O-glycans; O-mannosylation; lecticans; ECM; perineural net; O-glycosylation; ESI-MS/MS; MALDI-MS/MS; glycoproteomics; dystroglycanopathies}}, language = {{eng}}, number = {{4}}, pages = {{1764--1771}}, publisher = {{The American Chemical Society (ACS)}}, series = {{Journal of Proteome Research}}, title = {{The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated}}, url = {{http://dx.doi.org/10.1021/pr3011028}}, doi = {{10.1021/pr3011028}}, volume = {{12}}, year = {{2013}}, }