Proteomics

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Global protein analysis of pediatric acute leukemia patients and matched xenografts

ABSTRACT: Proteomics reveal protein stability after xenotransplantation in murine models. Tryptic peptide digests from patient mononuclear cells were analyzed by Data Independent Acquisition (DIA) mass spectrometry. High-pH fractionation was performed on a pool of samples, followed by data dependent acquisition (DDA) mass spectrometry analysis. Spectral information from DDA and DIA data were used to generate a sample-specific library for targeted analysis to identify and quantify proteins. We present a global landscape of protein stability in paired patients and patient-derived xenografts, pediatric leukemic cell lines, and normal individuals.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Dr. Philipp Lange  

PROVIDER: MSV000084646 | MassIVE | Mon Dec 02 16:25:00 GMT 2019

SECONDARY ACCESSION(S): PXD016548

REPOSITORIES: MassIVE

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PDX models reflect the proteome landscape of pediatric acute lymphoblastic leukemia but divert in select pathways.

Uzozie Anuli C AC   Ergin Enes K EK   Rolf Nina N   Tsui Janice J   Lorentzian Amanda A   Weng Samuel S H SSH   Nierves Lorenz L   Smith Theodore G TG   Lim C James CJ   Maxwell Christopher A CA   Reid Gregor S D GSD   Lange Philipp F PF  

Journal of experimental & clinical cancer research : CR 20210315 1

<h4>Background</h4>Murine xenografts of pediatric leukemia accurately recapitulate genomic aberrations. How this translates to the functional capacity of cells remains unclear. Here, we studied global protein abundance, phosphorylation, and protein maturation by proteolytic processing in 11 pediatric B- and T- cell ALL patients and 19 corresponding xenografts.<h4>Methods</h4>Xenograft models were generated for each pediatric patient leukemia. Mass spectrometry-based methods were used to investig  ...[more]

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