Evidence map›Paper›PMID 28810879›Full record

ArticleJournal of translational medicine2017

Quantification of mutant SPOP proteins in prostate cancer using mass spectrometry-based targeted proteomics.

Hui Wang, Christopher E Barbieri, Jintang He, Yuqian Gao, Tujin Shi, Chaochao Wu, Athena A Schepmoes, Thomas L Fillmore, Sung-Suk Chae, Dennis Huang and 9 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of translational medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
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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

19 authors at 3 institutions in 1 country.

Hui WangBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Christopher E BarbieriInstitute of Precision Medicine of Weill Cornell Medical College and New York Presbyterian Hospital, New York, NY, USA.
Jintang HeBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Yuqian GaoBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Tujin ShiBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Chaochao WuBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Athena A SchepmoesBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Thomas L FillmoreBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Sung-Suk ChaeInstitute of Precision Medicine of Weill Cornell Medical College and New York Presbyterian Hospital, New York, NY, USA.
Dennis HuangInstitute of Precision Medicine of Weill Cornell Medical College and New York Presbyterian Hospital, New York, NY, USA.
Juan Miguel MosqueraInstitute of Precision Medicine of Weill Cornell Medical College and New York Presbyterian Hospital, New York, NY, USA.
Wei-Jun QianBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Richard D SmithBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Sudhir SrivastavaDivision of Cancer Prevention, Cancer Biomarkers Research Group, National Cancer Institute, Bethesda, MD, USA.
Jacob KaganDivision of Cancer Prevention, Cancer Biomarkers Research Group, National Cancer Institute, Bethesda, MD, USA.
David G CampBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Karin D RodlandBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA.
Mark A RubinInstitute of Precision Medicine of Weill Cornell Medical College and New York Presbyterian Hospital, New York, NY, USA.
Tao LiuBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: K8-98, Richland, WA, 99354, USA. tao.liu@pnnl.gov.ORCID 0000-0001-9529-6550
Pacific Northwest National Laboratory · USNewYork–Presbyterian Hospital · USNational Cancer Institute · US

Funding

WORKSHOP AND TRAINING ACTIVITIESP41RR018522 · NCRR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2003 to 2011
$25.1M
NCRR NIH HHS P41 RR018522
6 · The paper itself

Abstract

backgroundSpeckle-type POZ protein (SPOP) is an E3 ubiquitin ligase adaptor protein that functions as a potential tumor suppressor, and SPOP mutations have been identified in ~10% of human prostate cancers. However, it remains unclear if mutant SPOP proteins can be utilized as biomarkers for early detection, diagnosis, prognosis or targeted therapy of prostate cancer. Moreover, the SPOP mutation sites are distributed in a relatively short region with multiple lysine residues, posing significant challenges for bottom-up proteomics analysis of the SPOP mutations.

methodsTo address this issue, PRISM (high-pressure, high-resolution separations coupled with intelligent selection and multiplexing)-SRM (selected reaction monitoring) mass spectrometry assays have been developed for quantifying wild-type SPOP protein and 11 prostate cancer-derived SPOP mutations.

resultsDespite inherent limitations due to amino acid sequence constraints, all the PRISM-SRM assays developed using Arg-C digestion showed a linear dynamic range of at least two orders of magnitude, with limits of quantification ranged from 0.1 to 1 fmol/μg of total protein in the cell lysate. Applying these SRM assays to analyze HEK293T cells with and without expression of the three most frequent SPOP mutations in prostate cancer (Y87N, F102C or F133V) led to confident detection of all three SPOP mutations in corresponding positive cell lines but not in the negative cell lines. Expression of the F133V mutation and wild-type SPOP was at much lower levels compared to that of F102C and Y87N mutations; however, at present, it is unknown if this also affects the biological activity of the SPOP protein.

conclusionsIn summary, PRISM-SRM enables multiplexed, isoform-specific detection of mutant SPOP proteins in cell lysates, providing significant potential in biomarker development for prostate cancer.

Indexed as

Amino Acid SequenceHEK293 CellsHumansLimit of DetectionMaleMass SpectrometryMutationNuclear ProteinsPeptidesProstatic NeoplasmsProteomicsRepressor ProteinsNuclear ProteinsPeptidesRepressor ProteinsSPOP protein, humanBiomarkerMass spectrometryPRISM-SRMProstate cancerSPOP mutationTargeted proteomics

Identifiers

PMID28810879
PMCPMC5557563
OpenAlexW2747833111

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Registered trials

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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.