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Does soluble guanylyl cyclase need a chaperone?

✍ Scribed by Qian Sun; Julio Ortega; Nazish Sayed; Fu-Jung Chang; Annie Beuve

Book ID
104493356
Publisher
BioMed Central
Year
2005
Tongue
English
Weight
187 KB
Volume
5
Category
Article
ISSN
1471-2210

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✦ Synopsis

Two commonly accepted features of soluble guanylyl cyclase (sGC): its lack of "partners" and its exclusive-cytoplasmic localization were recently challenged. Several proteins that bind directly to sGC have now been identified. The molecular chaperone Hsp70 is one of these sGCinteracting proteins. Hsp70 modulates sGC activity, but apparently requires other associated proteins or co-factors for its sGC-activating effect. Other members of the molecular chaperones family appear to interact with sGC as well.

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Soluble guanylyl cyclase (sGC) is a well-known target for the treatment of cardiovascular diseases. Finding activators of this enzyme is an important goal in pharmaceutical research labs. The predominantly used method to determine the activity of soluble sGC biochemically is based on a radioactive