Understanding Alzheimer's disease by global quantification of protein phosphorylation and sialylated N-linked glycosylation profiles: A chance for new biomarkers in neuroproteomics?

Pernille S. Lassen, Camilla Thygesen, Martin R. Larsen, Stefan J. Kempf*

*Kontaktforfatter for dette arbejde

Publikation: Bidrag til tidsskriftReviewForskningpeer review

Resumé

Phosphorylation and glycosylation are important protein modifications in the mammalian brain acting as drivers of neural development, neurotransmission signalling and neurite elongation as well as synaptic morphology. Despite their important functional roles in the brain, only a few studies have elucidated them in neurodegenerative diseases such as Alzheimer's disease. Here, we comprehensively review Alzheimer's pathology in relation to protein phosphorylation and glycosylation on synaptic plasticity from neuroproteomics data. Moreover, we highlight several mass spectrometry-based sample processing technologies including an in-house developed TiO2-SIMAC-TiO2-based enrichment protocol to isolate and enrich phosphorylated and glycosylated peptides enabling to elucidate hopefully new early disease biomarkers.

OriginalsprogEngelsk
TidsskriftJournal of Proteomics
Vol/bind161
Udgave nummerMay
Sider (fra-til)11-25
ISSN1874-3919
DOI
StatusUdgivet - 2017

Fingeraftryk

Glycosylation
Phosphorylation
Biomarkers
Brain
Alzheimer Disease
Neurodegenerative diseases
Pathology
Neurodegenerative Diseases
Mass spectrometry
Plasticity
Elongation
Proteins
Peptides
Processing

Citer dette

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title = "Understanding Alzheimer's disease by global quantification of protein phosphorylation and sialylated N-linked glycosylation profiles: A chance for new biomarkers in neuroproteomics?",
abstract = "Phosphorylation and glycosylation are important protein modifications in the mammalian brain acting as drivers of neural development, neurotransmission signalling and neurite elongation as well as synaptic morphology. Despite their important functional roles in the brain, only a few studies have elucidated them in neurodegenerative diseases such as Alzheimer's disease. Here, we comprehensively review Alzheimer's pathology in relation to protein phosphorylation and glycosylation on synaptic plasticity from neuroproteomics data. Moreover, we highlight several mass spectrometry-based sample processing technologies including an in-house developed TiO2-SIMAC-TiO2-based enrichment protocol to isolate and enrich phosphorylated and glycosylated peptides enabling to elucidate hopefully new early disease biomarkers.",
keywords = "LTP, Neurodegeneration, Neuron, Phosphoproteomics, Synapse, Synaptic plasticity, Phosphorylation, Humans, Glycosylation, Animals, Neuronal Plasticity, Proteomics/methods, Protein Processing, Post-Translational, Alzheimer Disease/metabolism",
author = "Lassen, {Pernille S.} and Camilla Thygesen and Larsen, {Martin R.} and Kempf, {Stefan J.}",
year = "2017",
doi = "10.1016/j.jprot.2017.04.003",
language = "English",
volume = "161",
pages = "11--25",
journal = "Journal of Proteomics",
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Understanding Alzheimer's disease by global quantification of protein phosphorylation and sialylated N-linked glycosylation profiles : A chance for new biomarkers in neuroproteomics? / Lassen, Pernille S.; Thygesen, Camilla; Larsen, Martin R.; Kempf, Stefan J.

I: Journal of Proteomics, Bind 161, Nr. May, 2017, s. 11-25.

Publikation: Bidrag til tidsskriftReviewForskningpeer review

TY - JOUR

T1 - Understanding Alzheimer's disease by global quantification of protein phosphorylation and sialylated N-linked glycosylation profiles

T2 - A chance for new biomarkers in neuroproteomics?

AU - Lassen, Pernille S.

AU - Thygesen, Camilla

AU - Larsen, Martin R.

AU - Kempf, Stefan J.

PY - 2017

Y1 - 2017

N2 - Phosphorylation and glycosylation are important protein modifications in the mammalian brain acting as drivers of neural development, neurotransmission signalling and neurite elongation as well as synaptic morphology. Despite their important functional roles in the brain, only a few studies have elucidated them in neurodegenerative diseases such as Alzheimer's disease. Here, we comprehensively review Alzheimer's pathology in relation to protein phosphorylation and glycosylation on synaptic plasticity from neuroproteomics data. Moreover, we highlight several mass spectrometry-based sample processing technologies including an in-house developed TiO2-SIMAC-TiO2-based enrichment protocol to isolate and enrich phosphorylated and glycosylated peptides enabling to elucidate hopefully new early disease biomarkers.

AB - Phosphorylation and glycosylation are important protein modifications in the mammalian brain acting as drivers of neural development, neurotransmission signalling and neurite elongation as well as synaptic morphology. Despite their important functional roles in the brain, only a few studies have elucidated them in neurodegenerative diseases such as Alzheimer's disease. Here, we comprehensively review Alzheimer's pathology in relation to protein phosphorylation and glycosylation on synaptic plasticity from neuroproteomics data. Moreover, we highlight several mass spectrometry-based sample processing technologies including an in-house developed TiO2-SIMAC-TiO2-based enrichment protocol to isolate and enrich phosphorylated and glycosylated peptides enabling to elucidate hopefully new early disease biomarkers.

KW - LTP

KW - Neurodegeneration

KW - Neuron

KW - Phosphoproteomics

KW - Synapse

KW - Synaptic plasticity

KW - Phosphorylation

KW - Humans

KW - Glycosylation

KW - Animals

KW - Neuronal Plasticity

KW - Proteomics/methods

KW - Protein Processing, Post-Translational

KW - Alzheimer Disease/metabolism

U2 - 10.1016/j.jprot.2017.04.003

DO - 10.1016/j.jprot.2017.04.003

M3 - Review

C2 - 28396268

AN - SCOPUS:85017474127

VL - 161

SP - 11

EP - 25

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

IS - May

ER -