Protein disulfide-isomerase interacts with soluble guanylyl cyclase via a redox-based mechanism and modulates its activity.
- Resource Type
- Article
- Authors
- HECKLER, Erin J.; CRASSOUS, Pierre-Antoine; BASKARAN, Padmamalini; BEUVE, Annie
- Source
- Biochemical Journal. 5/15/2013, Vol. 452 Issue 1, p161-169. 11p.
- Subject
- *HOMEOSTASIS
*VASODILATION
*GUANYLATE cyclase
*PROTEIN disulfide isomerase
*NITRIC oxide
*CARDIOVASCULAR system
- Language
- ISSN
- 0264-6021
The article offers information on a research study related to the role of pathway of nitric oxide (NO), soluble guanylyl cylase (sGC) and cyclic guonosine monophosphate (cGMP) in cardiovascular system. It mentions that protein disulphide isomerase (PDI) binds with sGC through a redox reaction forming a PDI-sGC complex that helps sGC in modulating vasodilation and inhibiting platelet aggregation. It also discusses the role of redox reaction of PDI with sGC in controlling homeostasis.