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Nonselective ion pathways in human endothelial cells

B Nilius1, G Droogmans, M Gericke

  • 1KU Leuven, Department of Physiology, Belgium.

EXS
|January 1, 1993
PubMed
Summary
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Human endothelial cells possess four distinct cation channels for calcium (Ca2+) entry, activated by agonists, shear stress, thapsigargin, or present as a leak. These pathways are crucial for cell signaling and function.

Area of Science:

  • Cell Biology
  • Physiology
  • Biochemistry

Background:

  • Endothelial cells (EN) play a vital role in regulating vascular function.
  • Calcium (Ca2+) signaling is critical for various cellular processes in endothelial cells.
  • Understanding transmembrane ion transport is essential for comprehending endothelial cell physiology.

Purpose of the Study:

  • To identify and characterize distinct transmembrane pathways for cation entry in human endothelial cells.
  • To investigate the gating mechanisms and properties of these identified pathways.
  • To elucidate the role of these pathways in calcium (Ca2+) homeostasis and signaling.

Main Methods:

  • Electrophysiological recordings to characterize ion channel activity.
  • Pharmacological manipulation using agonists (histamine) and blockers (thapsigargin, nickel).

Related Experiment Videos

  • Application of mechanical stimuli (shear stress) to assess pathway activation.

    • Main Results:

    • Four nonselective cation pathways were identified in human endothelial cells.
    • Agonist-gated channel permeable to Na+, K+, and Ca2+.
    • Mechanically activated channel permeable to divalent cations.
    • Thapsigargin-activated pathway linked to Ca2+ release from endoplasmic reticulum stores.
    • A nickel-blockable, Ca2+-permeable leak pathway was also observed.

    Conclusions:

    • Human endothelial cells utilize multiple, distinct transmembrane pathways for cation and Ca2+ entry.
    • These pathways exhibit varied activation mechanisms, including agonist-gating, mechanical activation, and store depletion.
    • The identified pathways contribute to cellular Ca2+ signaling and mechano-sensing properties of endothelial cells.