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NADPH oxidase does not account fully for O2-sensing in model airway chemoreceptor cells

I O'Kelly1, C Peers, P J Kemp

  • 1School of Biomedical Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom.

Biochemical and Biophysical Research Communications
|May 18, 2001
PubMed

Insights

Hypoxic inhibition of K+ channels in H146 cells involves NADPH oxidase, but not exclusively. This study suggests multiple mechanisms contribute to oxygen sensing in these cells.

Area of Science:

  • Cellular physiology
  • Respiratory system biology

Background:

  • Oxygen sensing is crucial for chemoreceptor tissues, involving hypoxic inhibition of potassium (K+) channels.
  • Mechanisms for O2 sensing vary; in neuroepithelial bodies and H146 cells, it involves reactive oxygen species from NADPH oxidase, unlike the carotid body.

Purpose of the Study:

  • To provide pharmacological evidence for NADPH oxidase's role in hypoxic K+ current inhibition in H146 cells.
  • To investigate the contribution of NADPH oxidase to oxygen sensing mechanisms in H146 cells.

Main Methods:

  • Patch-clamp electrophysiology was used to record K+ currents.
  • Pharmacological inhibition of NADPH oxidase using diphenylene iodonium and phenylarsine oxide.

Main Results:

  • NADPH oxidase inhibitors partially suppressed the hypoxic inhibition of K+ currents in H146 cells.
  • The suppression was not complete, indicating other mechanisms are involved.

Conclusions:

  • NADPH oxidase plays a role in the hypoxic suppression of K+ channel activity in H146 cells.
  • Multiple mechanisms likely coexist within H146 cells to mediate hypoxic K+ channel inhibition, highlighting cellular complexity in oxygen sensing.

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