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Related Concept Videos

Proteomics01:33

Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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Peptide Identification Using Tandem Mass Spectrometry01:33

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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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Proteomics equipped with multiplexing toward ultra high throughput.

Min-Sik Kim1

  • 1McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Proteomics
|December 19, 2014
PubMed
Summary
This summary is machine-generated.

Multiplexing in mass spectrometry (MS) quantitative proteomics enables higher throughput analysis. This study found minimal protein changes but widespread phosphorylation alterations in mice treated with small molecule inhibitors.

Keywords:
Mass spectrometryPhosphoproteomicsQuantitative proteomicsTagging

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Area of Science:

  • Biochemistry
  • Proteomics
  • Pharmacology

Background:

  • Mass spectrometry (MS)-based quantitative proteomics is a high-throughput technology for biological and clinical sample analysis.
  • Analyzing a large number of samples using MS remains practically and economically challenging.
  • Multiplexing strategies can enhance the efficiency of quantitative proteomic analyses.

Purpose of the Study:

  • To demonstrate the utility of a multiplexing strategy for quantitative proteome and phosphoproteome analysis.
  • To investigate the in vivo effects of two small molecule inhibitors on a mouse model.
  • To assess protein and phosphorylation level alterations following short-term drug treatment.

Main Methods:

  • Quantitative proteomics using mass spectrometry (MS).
  • Application of a multiplexing strategy for sample analysis.
  • In vivo drug treatment of a mouse model.
  • Analysis of proteome and phosphoproteome changes in mouse tissues.

Main Results:

  • Protein alterations were minimal in three tested tissues after short-term drug treatment.
  • Phosphorylation levels were widely altered in response to the drug treatment.
  • The multiplexing strategy proved effective for quantitative proteome and phosphoproteome analysis.

Conclusions:

  • Multiplexing strategies improve the feasibility of high-throughput MS-based quantitative proteomics.
  • Short-term treatment with small molecule inhibitors primarily impacts phosphorylation rather than overall protein levels.
  • This approach aids in understanding drug effects in vivo.