Model Status

This is the original version of the model imported from the previous CellML model repository. This model still contains the reaction element. We were unable to recode this model to remove the reaction element because the published paper does not contain the full set of equations required to carry out this translation into CellML.

Model Structure

In both pulmonary and vascular smooth muscle, nitric oxide (NO) acts as an activator of the enzyme soluble guanylate cyclase (sGC). sGC catalyses the conversion of guanosine 5'-triphosphate (GTP) to guanosine 3',5'-cyclic monophosphate (cGMP). Previous to this 2001 publication, (the complete original paper reference is cited below) binding rates of NO to sGC had only been measured in vitro under non-physiological conditions. Using their mathematical model (see the figure below) and in vitro data, Condorelli and George provide a mechanism by which NO activates sGC in vivo.

In Vivo Control of Soluble Guanylate Cyclase Activation by Nitric Oxide: A Kinetic Analysis, Peter Condorelli and Steven C. George, 2001, Biophysical Journal , 80, 2110-2119. (A PDF version of the article is available for Journal Members on the Biophysical Journal website.) PubMed ID: 11325714

A schematic diagram of the reactions involved in the binding of free nitric oxide (NO) to soluble guanylate cyclase (sGC). sGC catalyses the conversion of guanosine 5'-triphosphate (GTP) to guanosine 3',5'-cyclic monophosphate (cGMP).

• condorelli_george_2001_version01.cellml