What kinase is activated by cGMP?

What kinase is activated by cGMP?

Cyclic GMP-dependent protein kinases (cGKs) are serine/threonine kinases which are activated by the second messenger cGMP.

How does cGMP cause vasodilation?

Active PKG is ultimately responsible for many of the effects of Nitric Oxide including its effects on blood vessel relaxation (vasodilation). Activation of PKG by cGMP leads to activation of myosin phosphatase which in turn leads to release of calcium from intracellular stores in smooth muscle cells.

What does protein kinase G do?

In a variety of systemic blood vessels, protein kinase G (PKG) plays a critical role in mediating relaxation induced by agents that elevate cGMP, such as nitric oxide. The role of PKG in nitric oxide- and cGMP-induced relaxation is less certain in the pulmonary circulation.

What does PKG do in smooth muscle?

PKG has been shown to catalyze the phosphorylation of a number of physiologically relevant proteins whose function it is to regulate the contractile activity of the smooth muscle cell.

Is cGMP a protein?

cGMP acts as a second messenger much like cyclic AMP. Its most likely mechanism of action is activation of intracellular protein kinases in response to the binding of membrane-impermeable peptide hormones to the external cell surface.

Why is cGMP a second messenger?

Cyclic guanosine monophosphate (cGMP) is a unique second messenger molecule formed in different cell types and tissues. cGMP targets a variety of downstream effector molecules and, thus, elicits a very broad variety of cellular effects.

Which is a cGMP dependent protein kinase ( PKG )?

cGMP-dependent protein kinase. cGMP-dependent protein kinase or Protein Kinase G (PKG) is a serine/threonine-specific protein kinase that is activated by cGMP. It phosphorylates a number of biologically important targets and is implicated in the regulation of smooth muscle relaxation, platelet function, sperm metabolism, cell division,…

How does cGMP bind to the regulatory domain?

Binding of cGMP to the regulatory domain induces a conformational change which stops the inhibition of the catalytic core by the N-terminus and allows the phosphorylation of substrate proteins. Whereas PKG-I is predominantly localized in the cytoplasm, PKG-II is anchored to the plasma membrane by N-terminal myristoylation .

How is cGMP related to the proapoptotic effect of no?

In addition to its antihypertrophic effect, NO promotes apoptosis in cardiomyocytes in a dose-dependent manner. On the other hand, the role of cGMP in the proapoptotic effects of NO is rather controversial because cGMP analogs may or may not induce cardiomyocyte apoptosis.

Which is the gene coding for PKG type I?

Two PKG genes, coding for PKG type I (PKG-I) and type II (PKG-II), have been identified in mammals. The N-terminus of PKG-I is encoded by two alternatively spliced exons that specify for the PKG-Iα and PKG-Iβ isoforms. PKG-Iβ is activated at ~10-fold higher cGMP concentrations than PKG-Iα.