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Extracellular FABP4 uptake by endothelial cells is dependent on cytokeratin 1 expression

N Martínez-Micaelo1, R Rodríguez-Calvo1, S Guaita-Esteruelas2

  • 1Lipids and Atherosclerosis Research Unit, Hospital Universitari Sant Joan, Institut d'Investigació Sanitària Pere Virgili (IISPV), Spanish Biomedical Research Centre in Diabetes and Associated Metabolic Disorders (CIBERDEM), Universitat Rovira i Virgili, Reus, Spain.

Biochimica Et Biophysica Acta. Molecular and Cell Biology of Lipids
|December 7, 2018
PubMed
Abstract

Insights

Fatty acid-binding protein 4 (FABP4) interacts with cytokeratin 1 (CK1) to increase cellular uptake, promoting inflammation and oxidative stress in endothelial cells. Inhibiting this interaction may offer a therapeutic strategy against these conditions.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Medicine

Background:

  • Fatty acid-binding protein 4 (FABP4) plays a role in cellular lipid metabolism and signaling.
  • Endothelial cells are crucial for vascular health and are susceptible to oxidative stress and inflammation.
  • The interaction between FABP4 and membrane proteins is under investigation for its role in cellular processes.

Purpose of the Study:

  • To elucidate the physical and functional interaction between FABP4 and its candidate receptor, cytokeratin 1 (CK1).
  • To investigate the impact of inhibiting CK1-mediated FABP4 cellular uptake on endothelial cells under normal and stressed conditions.
  • To assess the role of FABP4-CK1 interaction in regulating oxidative stress and inflammation in endothelial cells.

Main Methods:

  • Surface plasmon resonance was used to monitor direct FABP4-CK1 interaction.
  • siRNA was employed to knock down CK1 expression in human umbilical vein endothelial cells (HUVECs).
  • Western blotting analyzed the expression and nuclear translocation of NRF2 and NF-κB (p65) to assess oxidative stress and inflammation.

Main Results:

  • FABP4 and CK1 were confirmed to bind, with a specific binding domain identified on CK1.
  • Exogenous FABP4 (eFABP4) uptake, facilitated by CK1, was shown to regulate endothelial cell responses to oxidative stress.
  • eFABP4 exacerbated palmitate-induced inflammation and oxidative stress, dependent on CK1 expression.

Conclusions:

  • Cytokeratin 1 (CK1) facilitates the cellular uptake of exogenous FABP4 (eFABP4) in endothelial cells.
  • Targeting the CK1-mediated uptake of FABP4 presents a potential therapeutic approach.
  • Inhibition strategies could protect endothelial cells from FABP4-induced inflammation and oxidative stress.
Keywords:
CK1Endothelial dysfunctionFABP4Inflammation

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