Soluble guanylyl cyclase activation promotes angiogenesis
نویسندگان
چکیده
منابع مشابه
Soluble guanylyl cyclase activation promotes angiogenesis.
Soluble guanylyl cyclase (sGC) is a cGMP-generating enzyme carrying a heme prosthetic group that functions as a nitric oxide (NO) sensor. sGC is present in most cells types, including the vascular endothelium, where its biological functions remain largely unexplored. Herein, we have investigated the role of sGC in angiogenesis and angiogenesis-related properties of endothelial cells (EC). Initi...
متن کاملMechanism of YC-1-induced activation of soluble guanylyl cyclase.
The signaling molecule nitric oxide (NO) mediates many of its effects by the stimulation of soluble guanylyl cyclase (sGC). The activation process is initiated by high-affinity binding of NO to the enzyme's prosthetic heme group. Despite its poor sGC-activating properties, carbon monoxide (CO) has also been suggested as a physiological activator of sGC. Recently, we have shown that the substanc...
متن کاملBiphasic roles for soluble guanylyl cyclase (sGC) in platelet activation.
Nitric oxide (NO) stimulates cGMP synthesis by activating its intracellular receptor, soluble guanylyl cyclase (sGC). It is a currently prevailing concept that No and cGMP inhibits platelet function. However, the data supporting the inhibitory role of NO/sGC/cGMP in platelets have been obtained either in vitro or using whole body gene deletion that affects vessel wall function. Here we have gen...
متن کاملNO activation of guanylyl cyclase.
Nitric oxide (NO)-sensitive guanylyl-cyclase (GC) is the most important receptor for the signaling molecule NO. Activation of the enzyme is brought about by binding of NO to the prosthetic heme group. By monitoring NO-binding and catalytic activity simultaneously, we show that NO activates GC only if the reaction products of the enzyme are present. NO-binding in the absence of the products did ...
متن کاملNucleotidyl cyclase activity of soluble guanylyl cyclase in intact cells.
Soluble guanylyl cyclase (sGC) is activated by nitric oxide (NO) and generates the second messenger cyclic GMP (cGMP). Recently, purified sGC α1β1 has been shown to additionally generate the cyclic pyrimidine nucleotides cCMP and cUMP. However, since cyclic pyrimidine nucleotide formation occurred only the presence of Mn(2+) but not Mg(2+), the physiological relevance of these in vitro findings...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: BMC Pharmacology
سال: 2005
ISSN: 1471-2210
DOI: 10.1186/1471-2210-5-s1-p46