The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated

Research output: Contribution to journalArticle

Standard

The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated. / Pacharra, Sandra; Hanisch, Franz-Georg; Muehlenhoff, Martina; Faissner, Andreas; Rauch, Uwe; Breloy, Isabelle.

In: Journal of Proteome Research, Vol. 12, No. 4, 2013, p. 1764-1771.

Research output: Contribution to journalArticle

Harvard

Pacharra, S, Hanisch, F-G, Muehlenhoff, M, Faissner, A, Rauch, U & Breloy, I 2013, 'The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated', Journal of Proteome Research, vol. 12, no. 4, pp. 1764-1771. https://doi.org/10.1021/pr3011028

APA

Pacharra, S., Hanisch, F-G., Muehlenhoff, M., Faissner, A., Rauch, U., & Breloy, I. (2013). The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated. Journal of Proteome Research, 12(4), 1764-1771. https://doi.org/10.1021/pr3011028

CBE

MLA

Vancouver

Author

Pacharra, Sandra ; Hanisch, Franz-Georg ; Muehlenhoff, Martina ; Faissner, Andreas ; Rauch, Uwe ; Breloy, Isabelle. / The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated. In: Journal of Proteome Research. 2013 ; Vol. 12, No. 4. pp. 1764-1771.

RIS

TY - JOUR

T1 - The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated

AU - Pacharra, Sandra

AU - Hanisch, Franz-Georg

AU - Muehlenhoff, Martina

AU - Faissner, Andreas

AU - Rauch, Uwe

AU - Breloy, Isabelle

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - O-glycans

KW - O-mannosylation

KW - lecticans

KW - ECM

KW - perineural net

KW - O-glycosylation

KW - ESI-MS/MS

KW - MALDI-MS/MS

KW - glycoproteomics

KW - dystroglycanopathies

U2 - 10.1021/pr3011028

DO - 10.1021/pr3011028

M3 - Article

VL - 12

SP - 1764

EP - 1771

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 4

ER -