PD-L1 Triggered by Binding eIF3I Contributes to the Amelioration of Diabetes-Associated Wound Healing Defects by Regulating IRS4

J Invest Dermatol. 2022 Jan;142(1):220-231.e8. doi: 10.1016/j.jid.2021.06.028. Epub 2021 Jul 20.

Abstract

Persistent chronic inflammation and delayed epithelialization lead to stalled healing in diabetic ulcers (DUs). PD-L1 shows anti-inflammatory and proliferative activities in healing defects, whereas its function in DU pathogenesis remains unknown. Lower levels of PD-L1 were found in DU tissues, and exogenous PD-L1 has therapeutic effects in the healing process by accelerating re-epithelialization and attenuating prolonged inflammation, which contributed to the delayed wound closure. We detected the downstream effectors of PD-L1 using transcriptional profiles and screened the interacting proteins using immunoprecipitation in combination with mass spectrometry and coimmunoprecipitation assays. The biological functions of eIF3I‒PD-L1‒IRS4 axis were tested both in vivo and in vitro. Finally, we validated the expression levels of eIF3I, PD-L1, and IRS4 in DU tissues from human clinical samples by immunohistochemistry staining. Mechanistically, PD-L1 binds to eIF3I and promotes cutaneous diabetic wound healing by downregulating IRS4. These findings identify that the eIF3I‒PD-L1‒IRS4 axis contributes to wound healing defects, which can serve as a potential therapeutic target in DUs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • B7-H1 Antigen / genetics
  • B7-H1 Antigen / metabolism*
  • Cell Line
  • Diabetes Mellitus, Type 1 / metabolism*
  • Disease Models, Animal
  • Eukaryotic Initiation Factors / metabolism*
  • Gene Expression Regulation
  • Humans
  • Insulin Receptor Substrate Proteins / genetics
  • Insulin Receptor Substrate Proteins / metabolism*
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Keratinocytes / physiology*
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Molecular Targeted Therapy
  • Protein Binding
  • Re-Epithelialization
  • Signal Transduction
  • Ulcer / metabolism*
  • Wound Healing

Substances

  • B7-H1 Antigen
  • Eukaryotic Initiation Factors
  • Insulin Receptor Substrate Proteins
  • Intracellular Signaling Peptides and Proteins
  • Irs4 protein, mouse
  • TRIP-1 protein, mouse