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Related Concept Videos

Proteomics01:33

Proteomics

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 proteomics...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
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Phosphoproteomics: searching for a needle in a haystack.

Ales Tichy1, Barbora Salovska, Pavel Rehulka

  • 1Department of Radiobiology, Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic. tichy@pmfhk.cz

Journal of Proteomics
|August 16, 2011
PubMed
Summary
This summary is machine-generated.

Phosphorylation regulates key cellular processes, and mass spectrometry is vital for studying it. This review details phosphoproteomics enrichment techniques to enhance the detection of low-abundance phosphopeptides.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Proteomics
  • Cellular Signaling

Background:

  • Reversible protein phosphorylation is a fundamental regulatory mechanism controlling crucial cellular processes like gene expression, cell division, signal transduction, metabolism, differentiation, and apoptosis.
  • Mass spectrometry (MS) of phosphopeptides from tryptic protein digests is a powerful technique for identifying and characterizing phosphoproteins involved in these cellular functions.
  • A significant challenge in phosphoproteomics is the low abundance of phosphopeptides, their insufficient ionization, and suppression by non-phosphorylated peptides, necessitating effective enrichment strategies.

Purpose of the Study:

  • To provide a comprehensive overview of contemporary phosphoproteomics methods.
  • To describe and compare various phosphopeptide enrichment techniques.
  • To highlight different approaches for characterizing the phosphoproteome using mass spectrometry.

Main Methods:

  • Review of current literature on phosphoproteomics.
  • Description of various phosphopeptide enrichment strategies (e.g., affinity chromatography, metal ion immobilization, strong cation exchange chromatography).
  • Comparison of different mass spectrometry-based approaches for phosphoproteome characterization.

Main Results:

  • Detailed overview of state-of-the-art phosphopeptide enrichment methods.
  • Comparative analysis of the strengths and weaknesses of different enrichment techniques.
  • Discussion of mass spectrometry workflows for phosphoproteome analysis.

Conclusions:

  • Effective enrichment of phosphopeptides is crucial for successful phosphoproteomics studies.
  • A variety of enrichment techniques are available, each with specific advantages for different experimental needs.
  • Mass spectrometry-based phosphoproteomics continues to advance, offering powerful tools for understanding cellular regulation.