Dataset Information

Glycoprotein 2(GP2) glycosylation

ABSTRACT: The GP2 was extracted from surgically excised pancreas and its N-glycans were identified using mass gel-based proteomics.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Pancreas

SUBMITTER: Jianting Han

LAB HEAD: Qin Cao

PROVIDER: PXD055045 | Pride | 2025-05-23

REPOSITORIES: Pride

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Project description:Primary myelofibrosis (PMF) is a myeloproliferative neoplasm prone to leukemic transformation, for which limited treatment is available. Amongst individuals diagnosed with PMF, the most prevalent mutation is the JAK2V617F somatic point mutation that activates the Janus kinase 2 (JAK2) enzyme. Our earlier reports on hyperactivity of β1 integrin and enhanced adhesion activity of the α2β1 complex in JAK2V617F megakaryocytes (MKs) led us to examine the new hypothesis that this mutation leads to post-translational modification via changes in glycosylation. Samples were derived from immunoprecipitation of MKs obtained from Vav1-hJAK2V617F and wild type mice. Immunoprecipitated fractions were separated by SDS-PAGE and analyzed using LC-MS/MS techniques in a bottom-up glycoproteomics workflow. In the immunoprecipitate, glycopeptiforms corresponding to 11 out of the 12 potential N-glycosylation sites of integrin β1, and to all nine potential glycosylation sites of integrin α2, were observed. Glycopeptiforms were compared across WT and JAK2V617F phenotypes for both integrins. The overall trend observed is that JAK2V617F mutation in PMF MKs leads to changes in β1 glycosylation; in most cases, it results in an increase in the integrated area of glycopeptiforms. We also observed that, in mutated MKs, changes in integrin α2 glycosylation were more substantial than those observed for integrin β1 glycosylation, a finding that suggests that altered integrin α2 glycosylation may also affect activation. Additionally, the identification of proteins associated to the cytoskeleton that were co-immunoprecipitated with integrins α2 and β1 demonstrated the potential of the methodology employed in this study to provide some insight, at the peptide level, into the consequences of integrin activation in MKs. The extensive and detailed glycosylation patterns we uncovered provide a basis for future functional studies of each site in control cells as compared to JAK2V617F mutated cells.

			Action	DRS
	GP2-Chymo.zip	Other
	GP2-Elastase.zip	Other
	GP2-Pepsin.zip	Other
	GP2-Trypsin.zip	Other
	W_G316_human-review-20386-No_target.fasta	Fasta

Dataset Information

Glycoprotein 2(GP2) glycosylation

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