Nitric Oxide Regulates Cyclic GMP‐Dependent Protein Kinase Phosphorylation in Rat Brain

Abstract: Nitric oxide (NO) acts via soluble guanylyl cyclase to increase cyclic GMP (cGMP), which can regulate various targets including protein kinases. Western blotting showed that type II cGMP‐dependent protein kinase (cGK II) is widely expressed in various brain regions, especially in the thalamus. In thalamic extracts, the phosphorylation of several proteins, including cGK II, was increased by exogenous NO or cGMP. In vivo pretreatment with a NO synthase inhibitor reduced the phosphorylation of cGK II, and this could be reversed by exogenous NO or cGMP. Conversely, brainstem electrical stimulation, which enhances thalamic NO release, caused a NO synthase‐dependent increase in the phosphorylation of thalamic cGK II. These results indicate that endogenous NO regulates cGMP‐dependent protein phosphorylation in the thalamus. The activation of cGKII by NO may play a role in thalamic mechanisms underlying arousal.

• Publication year

  1998

• Venue

  Journal of Neurochemistry

• Publication date

  1998-08-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1046/j.1471-4159.1998.71020676.xPMID 9681458
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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