Proteomics

Dataset Information

0

2DG-induced protein glycosylation alterations in colorectal cancer cells CX1 using differential glycosite profiling


ABSTRACT: A new strategy to compare cellular glycoproteomes, thereby identifying membrane proteins with altered glycan structures and the concerned glycosites. The workflow consists of membrane proteins digestion followed by lectin-based isolation of glycopeptides and their fractionation. Since alterations in the glycan part of a glycopeptide causes mass alterations, analytical size exclusion chromatography is applied to detect these mass shifts. A combination of N-glycosidase treatment with nanoUPLC coupled Exploris-Orbitrap mass spectrometry identifies the altered glycoproteins and the respective glycosites. The methodology was established using the human colon cancer cell line CX1 which was treated with 2-deoxy-glucose - a modulator of N-glycosylation.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Colon

DISEASE(S): Colon Cancer

SUBMITTER: Malwina Michalak  

LAB HEAD: Jürgen Kopitz

PROVIDER: PXD024770 | Pride | 2021-09-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
C1.mzTab Mztab
C1.raw Raw
C10.mzTab Mztab
C10.raw Raw
C10_MQ_output.zip Other
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Publications

Differential Glycosite Profiling-A Versatile Method to Compare Membrane Glycoproteomes.

Michalak Malwina M   Kalteis Martin Simon MS   Ahadova Aysel A   Kloor Matthias M   Kriegsmann Mark M   Kriegsmann Katharina K   Warnken Uwe U   Helm Dominic D   Kopitz Jürgen J  

Molecules (Basel, Switzerland) 20210610 12


Glycosylation is the most prevalent and varied form of post-translational protein modifications. Protein glycosylation regulates multiple cellular functions, including protein folding, cell adhesion, molecular trafficking and clearance, receptor activation, signal transduction, and endocytosis. In particular, membrane proteins are frequently highly glycosylated, which is both linked to physiological processes and of high relevance in various disease mechanisms. The cellular glycome is increasing  ...[more]

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