PTP1B Modulates Carotid Plaque Vulnerability in Atherosclerosis Through Rab5-PDGFRβ-Mediated Endocytosis Disruption

Xiao Zhang1,2, Ran Xu1,2, Tao Wang1,2

  • 1Department of Neurosurgery, Xuanwu Hospital, Capital Medical University, Beijing, China.

PubMed
Abstract

Insights

Protein tyrosine phosphatase 1B (PTP1B) disrupts endocytosis and promotes apoptosis in vascular smooth muscle cells (VSMCs) via the Rab5-PDGFRβ pathway. This finding offers a potential therapeutic target for stabilizing vulnerable carotid plaques.

Area of Science:

  • Vascular Biology
  • Cellular Signaling
  • Atherosclerosis Research

Background:

  • Protein tyrosine phosphatase 1B (PTP1B) modulates platelet-derived growth factor receptor (PDGFR) signaling in vascular smooth muscle cells (VSMCs) through endocytosis.
  • The precise molecular mechanisms governing PDGFR trafficking and its interaction with the endo-lysosomal system in atherosclerosis remain largely undefined.

Purpose of the Study:

  • To elucidate the subcellular regulatory role of PTP1B in the endo-lysosomal degradation of PDGFR within atherosclerotic carotid plaques.
  • To identify PTP1B as a potential therapeutic target for stabilizing carotid plaques.

Main Methods:

  • Immunohistochemical staining for PDGFR-β and Caspase 3 in carotid plaques.
  • TUNEL and Propidium Iodide staining for apoptosis quantification.
  • Live-cell imaging to observe endocytic motility.
  • In vivo studies using ApoE-/- mice treated with a PTP1B inhibitor.

Main Results:

  • Elevated PDGFR-β expression correlates with increased apoptosis in vulnerable carotid plaques.
  • PTP1B modulates PDGFR-β signaling via Rab5-mediated endocytosis, impacting endosomal-lysosomal trafficking.
  • Inhibition of PTP1B reduced atherosclerosis in ApoE-/- mice, while elevated PTP1B induced VSMC apoptosis and impaired function.

Conclusions:

  • PTP1B disrupts VSMC endocytosis and promotes apoptosis through the Rab5-PDGFRβ pathway.
  • This pathway is implicated in the increased vulnerability of carotid plaques, suggesting PTP1B as a therapeutic target.