Hypoxia suppresses KV1.5 channel expression through endogenous 15-HETE in rat pulmonary artery

Prostaglandins Other Lipid Mediat. 2009 Jan;88(1-2):42-50. doi: 10.1016/j.prostaglandins.2008.09.005. Epub 2008 Oct 15.

Abstract

Hypoxia initiated pulmonary vasoconstriction is due to the inhibition of voltage-gated K(+) (K(V)) channels. But the mechanism is unclear. We have evidence that hypoxia activates 15-lipoxygenase (15-LOX) in distal pulmonary arteries and increases the formation of 15-hydroxyeicosatetraenoate (15-HETE). 15-HETE-induced pulmonary artery constriction to be through the inhibition of K(V) channels (K(V)1.5, K(V)2.1 and K(V)3.4). However, no direct link among hypoxia, 15-HETE and inhibition of K(V) subtypes is established. Therefore, we investigated whether 15-LOX/15-HETE pathway contributes to the hypoxia-induced down-regulation of K(V) channels. As K(V)1.5 channel is O(2)-sensitive, it was chosen in the initial study. We found that inhibition of 15-LOX suppressed the response of hypoxic pulmonary artery rings to phenylephrine. The expressions of K(V)1.5 channel mRNA and protein was robustly up-regulated in cultured PASMC and pulmonary artery after blocking of 15-LOX by lipoxygenase inhibitors in hypoxia. The 15-LOX blockade also partly rescued the voltage-gated K(+) current (I(K(V))). 15-HETE contributes to the down-regulation of K(V)1.5 channel, inhibition of I(K(V)) and increase of native pulmonary artery tension after hypoxia. Hypoxia inhibits K(V)1.5 channel through 15-LOX/15-HETE pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arachidonate 15-Lipoxygenase / metabolism
  • Cell Hypoxia
  • Gene Expression
  • Hydroxyeicosatetraenoic Acids / metabolism*
  • Kv1.5 Potassium Channel / genetics*
  • Kv1.5 Potassium Channel / metabolism
  • Male
  • Pulmonary Artery / metabolism*
  • RNA, Messenger / metabolism
  • Rats
  • Rats, Wistar

Substances

  • Hydroxyeicosatetraenoic Acids
  • Kv1.5 Potassium Channel
  • RNA, Messenger
  • 15-hydroxy-5,8,11,13-eicosatetraenoic acid
  • Arachidonate 15-Lipoxygenase