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The Parkinsonism-associated protein DJ-1/Park7 prevents glycation damage in human keratinocyte

Tamara Advedissian1, Frédérique Deshayes1, Françoise Poirier1

  • 1Team Morphogénèse, Homéostasie et Pathologies, Univ Paris Diderot, Sorbonne Paris Cité, CNRS UMR 7592, Institut Jacques Monod, 15 Rue Hélène Brion, 75013, Paris, France.

Biochemical and Biophysical Research Communications
|March 21, 2016
PubMed

Insights

DJ-1 (also known as Park7) is a protein deglycase that prevents protein glycation, a process linked to diabetic complications. This study shows DJ-1 protects skin cells from glycation, suggesting its importance in preventing skin aging and damage.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Dermatology

Background:

  • Protein glycation, caused by reducing sugars and dicarbonyls, inactivates proteins and is linked to diabetic complications.
  • DJ-1 (Park7) is a recently identified protein deglycase that repairs proteins damaged by glycation.
  • Glycation contributes to various diabetic complications, including skin defects.

Purpose of the Study:

  • To investigate the role of DJ-1 in preventing protein glycation in keratinocytes.
  • To determine if DJ-1 expression levels affect protein glycation in skin cells.
  • To explore DJ-1's potential in preventing skin glycation.

Main Methods:

  • Assessed collagen and keratinocyte protein glycation using ultraviolet absorption and fluorescence emission.
  • Utilized immunodetection with anti-advanced glycation endproduct antibodies in HaCaT keratinocytes.
  • Manipulated DJ-1 levels via small interfering RNAs (siRNAs) for depletion and plasmid transfection for overexpression.
  • Investigated the effect of Nrf2 inducer sulforaphane on DJ-1-mediated glycation prevention.

Main Results:

  • In vitro, DJ-1 demonstrated the ability to prevent the glycation of collagen and keratinocyte protein extracts.
  • Depletion of DJ-1 using siRNAs led to a threefold increase in protein glycation levels in HaCaT keratinocytes.
  • Overexpression of DJ-1, induced by sulforaphane or plasmid transfection, resulted in a significant, several-fold decrease in protein glycation.
  • DJ-1 was confirmed to play a crucial role in preventing protein glycation within eukaryotic cells.

Conclusions:

  • DJ-1 acts as a key deglycase, actively preventing protein glycation in skin cells.
  • DJ-1's protective function against glycation suggests its therapeutic potential for skin aging and diabetic skin complications.
  • DJ-1 is essential for maintaining protein integrity against glycation damage in eukaryotic cells.
Keywords:
Carbonyl stressDiabetesGlycationMaillard reactionProtein repairSkin

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