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Proteomic comparison between different tissue preservation methods for identification of promising biomarkers of urothelial bladder cancer

Valdés, Alberto (författare)
Uppsala universitet,Analytisk kemi,CSIC, Lab Food, Inst Food Sci Res, CIAL, Nicolas Cabrera 9, Madrid 28049, Spain
Bitzios, Athanasios (författare)
Uppsala universitet,Analytisk kemi
Kassa, Eszter (författare)
Uppsala universitet,Analytisk kemi
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Shevchenko, Ganna (författare)
Uppsala universitet,Analytisk kemi
Falk, Alexander, Research engineer, 1986- (författare)
Uppsala universitet,Analytisk kemi
Malmström, Per-Uno (författare)
Uppsala universitet,Urologkirurgi
Dragomir, Anca (författare)
Uppsala universitet,Klinisk och experimentell patologi
Segersten, Ulrika (författare)
Uppsala universitet,Urologkirurgi
Bergström Lind, Sara, 1977- (författare)
Uppsala universitet,Analytisk kemi
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 (creator_code:org_t)
2021-04-07
2021
Engelska.
Ingår i: Scientific Reports. - : Springer Nature. - 2045-2322. ; 11:1
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • Samples in biobanks are generally preserved by formalin-fixation and paraffin-embedding (FFPE) and/or optimal cutting temperature compound (OCT)-embedding and subsequently frozen. Mass spectrometry (MS)-based analysis of these samples is now available via developed protocols, however, the differences in results with respect to preservation methods needs further investigation. Here we use bladder urothelial carcinoma tissue of two different tumor stages (Ta/T1-non-muscle invasive bladder cancer (NMIBC), and T2/T3-muscle invasive bladder cancer (MIBC)) which, upon sampling, were divided and preserved by FFPE and OCT. Samples were parallel processed from the two methods and proteins were analyzed with label-free quantitative MS. Over 700 and 1200 proteins were quantified in FFPE and OCT samples, respectively. Multivariate analysis indicates that the preservation method is the main source of variation, but also tumors of different stages could be differentiated. Proteins involved in mitochondrial function were overrepresented in OCT data but missing in the FFPE data, indicating that these proteins are not well preserved by FFPE. Concordant results for proteins such as HMGCS2 (uniquely quantified in Ta/T1 tumors), and LGALS1, ANXA5 and plastin (upregulated in T2/T3 tumors) were observed in both FFPE and OCT data, which supports the use of MS technology for biobank samples and encourages the further evaluation of these proteins as biomarkers.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin -- Cancer och onkologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine -- Cancer and Oncology (hsv//eng)

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