Rabbit Anti-PRKG1 Polyclonal Antibody#abs133056

abs133056-50ug

1-2 Weeks

201.0

abs133056-100ug

1-2 Weeks

301.0

catalog

Description

PRKG1 is a serine/threonine protein kinase that plays a crucial role in the nitric oxide (NO)/cGMP signaling pathway. When GMP binds to PRKG1, it becomes activated and phosphorylates serines and threonines on various cellular proteins. These phosphorylated proteins are involved in regulating cellular calcium levels, but their specific contributions may differ between different cell types.
The targets of PRKG1 phosphorylation are diverse and have important functions in platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback regulation of the NO-signaling pathway, and various processes within the central nervous system (CNS) such as axon guidance, learning in the hippocampus and cerebellum, circadian rhythm, and nociception.
One of the key roles of PRKG1 is to induce smooth muscle relaxation. It achieves this by reducing intracellular free calcium levels, desensitizing contractile proteins to calcium, and decreasing the contractile state of smooth muscle or platelet activation. PRKG1 influences intracellular calcium levels through multiple pathways, including phosphorylation of MRVI1/IRAG to inhibit IP3-induced Ca(2+) release from intracellular stores and phosphorylation of KCNMA1 (BKCa) channels, which decreases intracellular Ca(2+) levels and leads to increased channel opening. Additionally, PRKG1 phosphorylates members of the transient receptor potential channel (TRPC) family, causing inactivation of the associated inward calcium current.
Another important mechanism of NO/cGMP/PRKG1 signaling involves the inactivation of the protein RhoA by PRKG1 phosphorylation. This has widespread effects on various processes, such as regulating RhoA translocation, reducing contraction, controlling vesicle trafficking, and decreasing myosin light chain phosphorylation, ultimately resulting in vasorelaxation.
The activation of PRKG1 by NO signaling also influences gene expression in different tissues. For example, in smooth muscle cells, increased cGMP and PRKG1 activity affect the expression of smooth muscle-specific contractile proteins and proteins involved in the NO/cGMP signaling pathway. Furthermore, PRKG1 helps down-regulate matrix proteins like osteopontin and thrombospondin-1, which limits smooth muscle cell migration and phenotypic changes.
PRKG1 also plays a role in regulating the functions of vasodilator-stimulated phosphoprotein (VASP) in platelets and smooth muscle cells.
In summary, PRKG1 is a crucial protein kinase in the NO/cGMP signaling pathway with broad-ranging effects on cellular processes, including the modulation of calcium levels, smooth muscle relaxation, gene expression, and platelet and smooth muscle cell functions. Its activity and phosphorylation of various targets contribute to the fine-tuning of these processes in different cell types.

Concentration

1mg/ml

Target

Background

Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca2+ release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca2+ levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle.