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RGS2 is suggested as a novel AD biomarker (alongside other genes) toward early AD detection and future disease modifying therapeutics.
Upregulated RGS2 contributes significantly to the anti-fibrotic effects of pirfenidone in idiopathic pulmonary fibrosis.
study provides functional data for 16 human RGS2 missense variants on their effects on AT1R (show AGTR1 Proteins)-mediated calcium mobilization and provides molecular understanding of those variants with functional loss in vitro.
Our results suggest that RGS2 might be involved in the pathogenesis of preeclampsia particularly in overweight women and contribute to their increased risk for hypertension and other types of cardiovascular disease later in life.
Data suggest that epigenetic changes in histone acetylation and DNA methylation (show HELLS Proteins) may contribute to the repression of RGS2 (regulator of G-protein signaling 2) expression in chemo-resistant ovarian cancer cells; regulation of HDAC1 (histone deacetylase 1 (show HDAC1 Proteins)) and DNMT1 (DNA methyltransferase 1 (show DNMT1 Proteins)) contribute to the suppression of RGS2.
The RGS2 (-391, C>G) genetic polymorphism may serve as a biomarker to predict a patient's response to antihypertensive drug therapy
MIR4717 regulates human RGS2 and contributes to the genetic risk towards anxiety-related traits.
FBXO44-mediated degradation of RGS2 protein uniquely depends on a Cul4B/DDB1 complex.
RGS2 polymorphisms were found to be associated with anxiety disorders and dimensional as well as intermediate phenotypes of anxiety.
RGS2 localizes to the mitotic spindle in a Nek7 (show NEK7 Proteins)-dependent manner, and along with Nek7 (show NEK7 Proteins) contributes to spindle morphology and mitotic spindle pole integrity.
The present results suggest that expression of the eIF2B (show EIF2B4 Proteins)-interacting domain of RGS2, RGS2eb, can protect against pathological cardiac hypertrophy and dysfunction in vivo.
RGS2 has critical roles in maintaining pancreatic beta-cell mass via modulating beta-cell function and apoptosis.
Results show that RGS2 negatively modulates D2R-mediated Galphai/o protein signaling in neuroblastoma N2A cells. Moreover, RGS2 critically regulates agonist-stimulated dopamine D2R internalization. RGS2 knockdown abolished quinpirole-stimulated D2R internalization and impaired beta-arrestin dissociation from the membrane.
Modest anti-inflammatory and anti-remodelling roles for RGS2 are also suggested. If translatable to humans, therapies that maximize RGS2 expression may prove advantageous
RGS2 might play a critical role in mouse oocyte meiotic maturation by affecting beta-tubulin (show TUBB Proteins) polymerization and chromosome segregation.
Knockdown of endogenous Rgs2 expression led to abnormal embryonic development in vitro, with a considerable number of early embryos arrested at the 2- or 4-cell stage. Moreover, mRNA expression of three zygotic gene activation-related genes (i.e. Zscan4 (show ZSCAN4 Proteins), Tcstv1 and MuERV-L) was decreased significantly in 2-cell arrested embryos. These results suggest that Rgs2 plays a critical role in early embryo development.
RGS2 deficiency decreases uterine artery blood flow by increasing myogenic tone at least partly through prolonged G protein activation
Rgs12 (show RGS12 Proteins) has a crucial role in the function of bone-resorbing OCs, particularly in preclinical models of pathological bone loss associated with inflammation-induced bone loss and postmenopausal osteoporosis.
RGS2 deficiency impairs renal function and autoregulation by increasing renal vascular resistance and reducing renal blood flow.
This study reveals a unique regulatory mechanism, the Rgs2-Ppard (show PPARD Proteins)-Sox10 (show SOX10 Proteins) signaling cascade, and defines a key molecular regulator, Rgs2, in neural crest development.
Gonadotropin-dependent up-regulation of RGS2 in equine and bovine preovulatory follicles and regulatory controls involved in RGS2 gene expression in granulosa cells.
We identified a significant RGS2 upregulation and collagen type I downregulation in the sclera of form deprivation myopic eyes.
Regulator of G protein signaling (RGS) family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. Regulator of G protein signaling 2 belongs to this family. The protein acts as a mediator of myeloid differentiation and may play a role in leukemogenesis.
G0 to G1 switch regulatory 8, 24kD
, G0/G1 switch regulatory protein 8
, cell growth-inhibiting gene 31 protein
, cell growth-inhibiting protein 31
, regulator of G-protein signaling 2
, regulator of G-protein signaling protein 2
, regulator of G-protein signalling 2, 24kDa
, regulator of G-protein signalling 2
, regulator of G-protein signaling 2, 24kDa