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Identification of multiple post-translational modifications in the porcine brain specific p25α

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

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Identification of multiple post-translational modifications in the porcine brain specific p25α. / Kjeinnijenhuis, Anne J.; Hedegaard, Claus; Lundvig, Ditte et al.
I: Journal of Neurochemistry, Bind 106, Nr. 2, 07.2008, s. 925-933.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Kjeinnijenhuis, AJ, Hedegaard, C, Lundvig, D, Sundbye, S, Issinger, OG, Jensen, ON & Jensen, PH 2008, 'Identification of multiple post-translational modifications in the porcine brain specific p25α', Journal of Neurochemistry, bind 106, nr. 2, s. 925-933. https://doi.org/10.1111/j.1471-4159.2008.05437.x

APA

Kjeinnijenhuis, A. J., Hedegaard, C., Lundvig, D., Sundbye, S., Issinger, O. G., Jensen, O. N., & Jensen, P. H. (2008). Identification of multiple post-translational modifications in the porcine brain specific p25α. Journal of Neurochemistry, 106(2), 925-933. https://doi.org/10.1111/j.1471-4159.2008.05437.x

CBE

Kjeinnijenhuis AJ, Hedegaard C, Lundvig D, Sundbye S, Issinger OG, Jensen ON, Jensen PH. 2008. Identification of multiple post-translational modifications in the porcine brain specific p25α. Journal of Neurochemistry. 106(2):925-933. https://doi.org/10.1111/j.1471-4159.2008.05437.x

MLA

Kjeinnijenhuis, Anne J. et al. "Identification of multiple post-translational modifications in the porcine brain specific p25α". Journal of Neurochemistry. 2008, 106(2). 925-933. https://doi.org/10.1111/j.1471-4159.2008.05437.x

Vancouver

Kjeinnijenhuis AJ, Hedegaard C, Lundvig D, Sundbye S, Issinger OG, Jensen ON et al. Identification of multiple post-translational modifications in the porcine brain specific p25α. Journal of Neurochemistry. 2008 jul.;106(2):925-933. doi: 10.1111/j.1471-4159.2008.05437.x

Author

Kjeinnijenhuis, Anne J. ; Hedegaard, Claus ; Lundvig, Ditte et al. / Identification of multiple post-translational modifications in the porcine brain specific p25α. I: Journal of Neurochemistry. 2008 ; Bind 106, Nr. 2. s. 925-933.

Bibtex

@article{ee13cd71880b461b91d430112122e834,
title = "Identification of multiple post-translational modifications in the porcine brain specific p25α",
abstract = "P25α is a protein normally expressed in oligodendrocytes and subcellular relocalization of p25α occurs in multiple system atrophy, Parkinson's disease and Lewy body dementia along with ectopic expression in neurons. Moreover, it accumulates in Lewy body inclusions with aggregated α-synuclein and is a potent stimulator of α-synuclein aggregation. P25α is a phosphoprotein and post-transla- tional modifications (PTMs) may play a role in its disease- related abnormalities. To investigate the spectrum of PTMs on p25α we cloned porcine p25α and isolated the protein from porcine brain. Using several complementary tandem mass spectrometry techniques for peptide mass analysis and amino acid sequencing, a comprehensive analysis of the PTMs on porcine p25α was performed. It was found that porcine p25α is heavily modified with a variety of modifications: phosphorylation, di- and trimethylation, citrullination and a HexNAc group. The modifications are localized within p25α's unfolded terminal domains and suggest that their functional states are regulated. This comprehensive mapping of p25α's PTMs will form the basis for future functional studies and investigations of p25α's potential role as a biomarker.",
keywords = "Citrullination, Methylation, O-glycosylation, Oligodendrocyte, P25α, Phosphorylation",
author = "Kjeinnijenhuis, {Anne J.} and Claus Hedegaard and Ditte Lundvig and Sabrina Sundbye and Issinger, {Olaf Georg} and Jensen, {Ole N{\o}rregaard} and Jensen, {Poul Henning}",
year = "2008",
month = jul,
doi = "10.1111/j.1471-4159.2008.05437.x",
language = "English",
volume = "106",
pages = "925--933",
journal = "Journal of Neurochemistry",
issn = "0022-3042",
publisher = "Wiley-Blackwell Publishing Ltd.",
number = "2",

}

RIS

TY - JOUR

T1 - Identification of multiple post-translational modifications in the porcine brain specific p25α

AU - Kjeinnijenhuis, Anne J.

AU - Hedegaard, Claus

AU - Lundvig, Ditte

AU - Sundbye, Sabrina

AU - Issinger, Olaf Georg

AU - Jensen, Ole Nørregaard

AU - Jensen, Poul Henning

PY - 2008/7

Y1 - 2008/7

N2 - P25α is a protein normally expressed in oligodendrocytes and subcellular relocalization of p25α occurs in multiple system atrophy, Parkinson's disease and Lewy body dementia along with ectopic expression in neurons. Moreover, it accumulates in Lewy body inclusions with aggregated α-synuclein and is a potent stimulator of α-synuclein aggregation. P25α is a phosphoprotein and post-transla- tional modifications (PTMs) may play a role in its disease- related abnormalities. To investigate the spectrum of PTMs on p25α we cloned porcine p25α and isolated the protein from porcine brain. Using several complementary tandem mass spectrometry techniques for peptide mass analysis and amino acid sequencing, a comprehensive analysis of the PTMs on porcine p25α was performed. It was found that porcine p25α is heavily modified with a variety of modifications: phosphorylation, di- and trimethylation, citrullination and a HexNAc group. The modifications are localized within p25α's unfolded terminal domains and suggest that their functional states are regulated. This comprehensive mapping of p25α's PTMs will form the basis for future functional studies and investigations of p25α's potential role as a biomarker.

AB - P25α is a protein normally expressed in oligodendrocytes and subcellular relocalization of p25α occurs in multiple system atrophy, Parkinson's disease and Lewy body dementia along with ectopic expression in neurons. Moreover, it accumulates in Lewy body inclusions with aggregated α-synuclein and is a potent stimulator of α-synuclein aggregation. P25α is a phosphoprotein and post-transla- tional modifications (PTMs) may play a role in its disease- related abnormalities. To investigate the spectrum of PTMs on p25α we cloned porcine p25α and isolated the protein from porcine brain. Using several complementary tandem mass spectrometry techniques for peptide mass analysis and amino acid sequencing, a comprehensive analysis of the PTMs on porcine p25α was performed. It was found that porcine p25α is heavily modified with a variety of modifications: phosphorylation, di- and trimethylation, citrullination and a HexNAc group. The modifications are localized within p25α's unfolded terminal domains and suggest that their functional states are regulated. This comprehensive mapping of p25α's PTMs will form the basis for future functional studies and investigations of p25α's potential role as a biomarker.

KW - Citrullination

KW - Methylation

KW - O-glycosylation

KW - Oligodendrocyte

KW - P25α

KW - Phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=51649129138&partnerID=8YFLogxK

U2 - 10.1111/j.1471-4159.2008.05437.x

DO - 10.1111/j.1471-4159.2008.05437.x

M3 - Journal article

C2 - 18435830

AN - SCOPUS:51649129138

VL - 106

SP - 925

EP - 933

JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

SN - 0022-3042

IS - 2

ER -