Hyperglycemia reduces integrin subunits alpha v and alpha 5 on the surface of dermal fibroblasts contributing to

Maira Estanislau S Almeida1, Kelly S Monteiro1, Ellen E Kato2

  • 1Department of Cell and Developmental Biology, Biomedical Sciences Institute, University of São Paulo, Av. Prof. Lineu Prestes 1524, Cidade Universitária, São Paulo, SP, CEP 05508-000, Brazil.

Insights

Diabetes impairs wound healing by affecting fibroblast function. High glucose reduces integrin expression in diabetic fibroblasts, hindering cell adhesion and migration, crucial for tissue repair.

Area of Science:

  • Cell Biology
  • Dermatology
  • Endocrinology

Background:

  • Diabetic patients exhibit impaired wound healing due to multifactorial complications.
  • The cellular and molecular mechanisms underlying delayed wound healing in diabetes are not fully understood.

Purpose of the Study:

  • To investigate the impact of hyperglycemia on integrin expression in rat dermal fibroblasts.
  • To determine the role of altered integrin expression in diabetic fibroblast cell adhesion and migration.

Main Methods:

  • Diabetes Mellitus was induced in rats using streptozotocin.
  • Dermal fibroblasts from control and diabetic rats were cultured under low or high glucose conditions.
  • Cell adhesion, migration, and integrin subunit (αv, α5) expression were analyzed using kymography, transwell assays, time-lapse imaging, immunocytochemistry, and western blotting.

Main Results:

  • Fibroblasts from diabetic rats showed reduced migration speed and delayed spreading.
  • A decrease in integrin subunits α5 and αv was observed in diabetic fibroblasts.
  • A diminished fibronectin matrix surrounding diabetic fibroblasts was noted.
  • Supplementation with exogenous fibronectin partially improved migration velocity and αv expression in diabetic fibroblasts.

Conclusions:

  • Hyperglycemia negatively affects fibroblast function, contributing to impaired wound healing in diabetes.
  • Reduced expression of integrins αv and α5 and altered fibronectin interactions are key mechanisms involved.

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