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The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated

Pacharra, Sandra ; Hanisch, Franz-Georg ; Muehlenhoff, Martina ; Faissner, Andreas ; Rauch, Uwe LU and Breloy, Isabelle (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)
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author
; ; ; ; and
organization
publishing date
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}},
}