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Seeing citrulline: Development of a phenylglyoxal-based probe to visualize protein citrullination

Academic Article
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Overview

authors

  • Bicker, K. L.
  • Subramanian, V.
  • Chumanevich, A. A.
  • Hofseth, L. J.
  • Thompson, Paul

publication date

  • October 2012

journal

  • Journal of the American Chemical Society  Journal

abstract

  • Protein arginine deiminases (PADs) catalyze the hydrolysis of peptidyl arginine to form peptidyl citrulline. Abnormally high PAD activity is observed in a host of human diseases, but the exact role of protein citrullination in these diseases and the identities of specific citrullinated disease biomarkers remain unknown, largely because of the lack of readily available chemical probes to detect protein citrullination. For this reason, we developed a citrulline-specific chemical probe, rhodamine-phenylglyoxal (Rh-PG), which we show can be used to investigate protein citrullination. This methodology is superior to existing techniques because it possesses higher throughput and excellent sensitivity. Additionally, we demonstrate that this probe can be used to determine the kinetic parameters for a number of protein substrates, monitor drug efficacy, and identify disease biomarkers in an animal model of ulcerative colitis that displays aberrantly increased PAD activity.

subject areas

  • Animals
  • Biomarkers
  • Citrulline
  • Hydrolases
  • Kinetics
  • Mice
  • Molecular Probes
  • Molecular Structure
  • Phenylglyoxal
  • Rhodamines
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Identity

PubMed Central ID

  • PMC3572846

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja308871v

PubMed ID

  • 23030787
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Additional Document Info

start page

  • 17015

end page

  • 17018

volume

  • 134

issue

  • 41

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