Evidence map›Paper›PMID 19471015›Full record

ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2009

Protein extraction of formalin-fixed, paraffin-embedded tissue enables robust proteomic profiles by mass spectrometry.

Marshall S Scicchitano, Deidre A Dalmas, Rogely W Boyce, Heath C Thomas, Kendall S Frazier

Open access · bronzeAbstract read
In one paragraph

Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.0field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 101 citations in OpenAlex.

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  14. Proteogenomic Analysis of Surgically Resected Lung Adenocarcinoma.Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer · 2018
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Marshall S ScicchitanoDepartment of Safety Assessment, 709 Swedeland Road, Mail Stop UE0364, King of Prussia, PA 19406, USA. Marshall.2.Scicchitano@gsk.com
Deidre A Dalmas
Rogely W Boyce
Heath C Thomas
Kendall S Frazier
GlaxoSmithKline (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Global mass spectrometry (MS) profiling and spectral count quantitation are used to identify unique or differentially expressed proteins and can help identify potential biomarkers. MS has rarely been conducted in retrospective studies, because historically, available samples for protein analyses were limited to formalin-fixed, paraffin-embedded (FFPE) archived tissue specimens. Reliable methods for obtaining proteomic profiles from FFPE samples are needed. Proteomic analysis of these samples has been confounded by formalin-induced protein cross-linking. The performance of extracted proteins in a liquid chromatography tandem MS format from FFPE samples and extracts from whole and laser capture microdissected (LCM) FFPE and frozen/optimal cutting temperature (OCT)-embedded matched control rat liver samples were compared. Extracts from FFPE and frozen/OCT-embedded livers from atorvastatin-treated rats were further compared to assess the performance of FFPE samples in identifying atorvastatin-regulated proteins. Comparable molecular mass representation was found in extracts from FFPE and OCT-frozen tissue sections, whereas protein yields were slightly less for the FFPE sample. The numbers of shared proteins identified indicated that robust proteomic representation from FFPE tissue and LCM did not negatively affect the number of identified proteins from either OCT-frozen or FFPE samples. Subcellular representation in FFPE samples was similar to OCT-frozen, with predominantly cytoplasmic proteins identified. Biologically relevant protein changes were detected in atorvastatin-treated FFPE liver samples, and selected atorvastatin-related proteins identified by MS were confirmed by Western blot analysis. These findings demonstrate that formalin fixation, paraffin processing, and LCM do not negatively impact protein quality and quantity as determined by MS and that FFPE samples are amenable to global proteomic analysis.

Indexed as

FixativesFormaldehydeParaffin EmbeddingAnimalsAtorvastatinBiomarkersCell NucleusChromatography, LiquidCytoplasmHeptanoic AcidsHydroxymethylglutaryl-CoA Reductase InhibitorsIntracellular MembranesLiverMaleProteomePyrrolesAtorvastatinBiomarkersFixativesFormaldehydeHeptanoic AcidsHydroxymethylglutaryl-CoA Reductase InhibitorsProteomePyrroles

Identifiers

PMID19471015
PMCPMC2728129
OpenAlexW1993876820

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.