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Peptic ulcer disease, commonly called PUD, represents a multifaceted condition characterized by disruptions in the lining of the gastrointestinal (GI)  tract. Central to the protection of the gastrointestinal lining is the mucosal-bicarbonate barrier. This physiological defense mechanism is a formidable shield against the corrosive effects of gastric acid and pepsin secretion in the stomach. Its role is pivotal in maintaining the structural integrity of the stomach's inner lining.
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Related Experiment Video

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Small molecule activates citrullination through targeting PAD2.

Xue Zhang1,2, Mengzhen Shen1,2, Huimin Zhu1,2

  • 1Shanghai Frontiers Science Center of TCM Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai 201203, People's Republic of China.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|October 1, 2023
PubMed
Summary

Researchers discovered demethoxycurcumin (DMC) activates protein citrullination by targeting peptidyl arginine deiminase 2 (PAD2). This finding offers a new chemical approach for activating citrullination, a process implicated in various diseases.

Keywords:
PAD2activatorcitrullinationdemethoxycurcumin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Protein citrullination, a post-translational modification catalyzed by peptidyl arginine deiminase (PAD) enzymes, is implicated in numerous pathological conditions.
  • While numerous citrullination inhibitors exist, activators remain scarce, limiting research into PAD enzyme function and therapeutic potential.

Purpose of the Study:

  • To screen for small molecules that activate protein citrullination.
  • To identify the specific PAD enzyme involved in the activation.
  • To characterize the mechanism of action of the identified activator.

Main Methods:

  • Screening for citrullination activators using an antibody against citrullinated histone H3 (cit-H3).
  • Loss-of-function assays to determine PAD enzyme requirement.
  • Direct binding assays and point mutation analysis to identify the interaction site.
  • Phenotypic analysis of DMC-induced cellular changes.

Main Results:

  • Demethoxycurcumin (DMC) was identified as a potent activator of protein citrullination.
  • PAD2 was confirmed as the essential enzyme for DMC-mediated citrullination.
  • DMC directly binds to PAD2, with residue E352 being critical for this interaction.
  • DMC treatment induced cellular apoptosis and DNA damage, consistent with PAD2 dysregulation.

Conclusions:

  • This study presents a novel strategy for screening citrullination activators.
  • Demethoxycurcumin provides a chemical tool for activating protein citrullination and studying PAD2 function.
  • The findings open new avenues for exploring the therapeutic potential of modulating protein citrullination.