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Parallel Proteomic Workflow for Mass Spectrometric Analysis of Tissue Samples Preserved by Different Methods
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Kemiska sektionen, Institutionen för kemi - BMC, Analytisk kemi.
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Kemiska sektionen, Institutionen för kemi - BMC, Analytisk kemi.
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för kirurgiska vetenskaper, Urologkirurgi.ORCID-id: 0000-0001-8572-9957
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för kirurgiska vetenskaper, Urologkirurgi.
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2018 (engelsk)Inngår i: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 90, nr 9, s. 5841-5849Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Formalin-fixed and paraffin-embedded (FFPE) and optimal cutting temperature (OCT)-embedded and frozen tissue specimens in biobanks are highly valuable in clinical studies but proteomic and post-translational modification (PTM) studies using mass spectrometry (MS) have been limited due to structural arrangement of proteins and contaminations from embedding material. This study aims to develop a parallel proteomic workflow for FFPE and OCT/frozen samples that allows for large-scale, quick, reproducible, qualitative, and quantitative high-resolution MS analysis. The optimized protocol gives details on removal of embedding material, protein extraction, and multienzyme digestion using filter-aided sample preparation method. The method was evaluated by investigating the protein expression levels in nonmuscle-invasive and muscle-invasive bladder cancer samples in two cohorts and MS spectra were carefully reviewed for contaminations. More than 2000 and 3000 proteins in FFPE and OCT/frozen samples, respectively, were identified, and samples could be clustered in different tumor stages based on their protein expression. Furthermore, more than 250 and 400 phosphopeptides could be identified from specific patient samples of FFPE and OCT/frozen, respectively, using titanium dioxide enrichment. The paper presents unique data describing the similarities and differences observed in FFPE and OCT/frozen samples and shows the feasibility to detect proteins and site-specific phosphorylation even after long-term storage of clinical samples.

sted, utgiver, år, opplag, sider
2018. Vol. 90, nr 9, s. 5841-5849
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Identifikatorer
URN: urn:nbn:se:uu:diva-356506DOI: 10.1021/acs.analchem.8b00379ISI: 000431464400045PubMedID: 29624047OAI: oai:DiVA.org:uu-356506DiVA, id: diva2:1237864
Forskningsfinansiär
Åke Wiberg Foundation, M14-0127Magnus Bergvall Foundation, 2015-01200; 2016-01675Carl Tryggers foundation , CST 15:57Tilgjengelig fra: 2018-08-10 Laget: 2018-08-10 Sist oppdatert: 2018-08-10bibliografisk kontrollert

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Valdés, AlbertoMalmström, Per-UnoSegersten, UlrikaBergström Lind, Sara

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