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PMID: 9003762 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Sensitizing soluble guanylyl cyclase to become a highly CO-sensitive enzyme.

The EMBO journal ·Vol. 15 ·No. 24 ·1996-12-16 ·Pages 6863-8

Friebe A, Schultz G, Koesling D

Abstract

It took at least a decade to realize that the toxic gas NO is the physiological activator of soluble guanylyl cyclase (sGC), thereby acting as a signaling molecule in the nervous and cardiovascular systems. Despite its rather poor sGC-activating property, CO has also been implicated as a physiological stimulator of sGC in neurotransmission and vasorelaxation. Here, we establish YC-1 as a novel NO-independent sGC activator that potentiates both CO- and NO-induced sGC stimulation. As this potentiating effect is also observed with protoporphyrin IX which activates sGC independently of a gaseous ligand, we conclude that stabilization of the enzyme's active configuration is the underlying mechanism of YC-1's action. Moreover, the results obtained with YC-1 reveal that CO is capable of stimulating sGC to a degree similar to NO, and thus provide the molecular basis for CO functioning as a signaling molecule.

MeSH Terms
Animals Carbon Monoxide/metabolism Cattle Enzyme Activation Guanylate Cyclase/metabolism Recombinant Proteins/metabolism
Chemicals
Recombinant Proteins Carbon Monoxide Guanylate Cyclase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Friebe A
Institut für Pharmakologie, Freie Universität Berlin, Germany.
Schultz G
Koesling D
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1996-12-16
Pages
6863-8
Language
English
Region
England
NLM ID
8208664
PMCID
PMC452512
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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