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Protein Cysteinyl-S-Nitrosylation: Analysis and Quantification.

J E Wiktorowicz1, S J Stafford2, N J Garg3

  • 1Sealy Center of Molecular Medicine, University of Texas Medical Branch, Galveston, TX, United States; Institute for Translational Sciences, University of Texas Medical Branch, Galveston, TX, United States; Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, TX, United States.

Methods in Enzymology
|February 1, 2017
PubMed
Summary
This summary is machine-generated.

This study introduces SNOFlo, a new method for quantifying S-nitrosylation, a cysteine modification affecting protein function. This technique aids in understanding S-nitrosylation in health and disease.

Keywords:
BODIPY Fl-maleimideCysteinyl-S-nitrosylationProteome

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Cysteine residues undergo various biological modifications, including S-nitrosylation, which critically regulate protein function.
  • Altered S-nitrosylation is implicated in numerous health and disease states, necessitating accurate analytical methods.
  • Understanding these modifications is key to deciphering cellular signaling pathways.

Purpose of the Study:

  • To present a novel quantitative proteomic approach for analyzing S-nitrosylation.
  • To introduce a sensitive fluorescence-based method (SNOFlo) for detecting cysteinyl-S-nitrosylation.
  • To enable the measurement of S-nitrosylation changes relative to overall protein abundance.

Main Methods:

  • Development of SNOFlo, a quantitative fluorescence modification technique for S-nitrosylation.
  • Ensuring the method does not alter electrophoretic mobility of proteins.
  • Application of the method to investigate endogenous S-nitrosylation in various biological contexts.

Main Results:

  • SNOFlo provides accurate and sensitive quantification of S-nitrosylation.
  • The method effectively measures changes in S-nitrosylation status independent of protein abundance.
  • Suitability of SNOFlo for studying endogenous S-nitrosylation in health and disease models was demonstrated.

Conclusions:

  • SNOFlo is a valuable tool for the proteomic analysis of S-nitrosylation.
  • This approach facilitates a deeper understanding of the role of S-nitrosylation in biological processes and disease.
  • The method offers a robust platform for future research in redox biology and post-translational modifications.