Heme-dependent activation of guanylate cyclase by nitric oxide: a novel signal transduction mechanism

Blood Vessels. 1991;28(1-3):67-73. doi: 10.1159/000158845.


The interaction between nitric oxide (NO) synthesized in one cell and cytosolic guanylate-cyclase-bound heme located in adjacent target cells to generate the NO-heme adduct of guanylate cyclase represents a novel and widespread signal transduction mechanism that links extracellular stimuli to the biosynthesis of cyclic GMP in target cells. A variety of chemical factors interact with selective extracellular receptors and trigger the biosynthesis of NO from L-arginine. The unique chemistry of NO endows this molecule with the capacity to diffuse rapidly into nearby cells and stimulate cyclic GMP formation. Cyclic GMP acts as a messenger in each cell type to trigger different but complementary cellular responses within a localized environment. This transcellular signaling is a form of rapid intercellular communication allowing the simultaneous local initiation of increased blood flow, inhibition of platelet-induced thrombosis and other cellular functions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Arginine / analogs & derivatives
  • Arginine / pharmacology
  • Enzyme Activation / drug effects
  • Guanylate Cyclase / metabolism*
  • Heme / physiology*
  • Humans
  • Nitric Oxide / pharmacology*
  • Signal Transduction*


  • Nitric Oxide
  • Heme
  • Arginine
  • Guanylate Cyclase