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anti-Rat (Rattus) PRKAG2 Antibodies:
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Human Polyclonal PRKAG2 Primary Antibody for ICC, IF - ABIN4347313
Martiáñez, Francès, López: Generation of digital responses in stress sensors. in The Journal of biological chemistry 2009
Show all 3 Pubmed References
the PRKAG2 gene can be used for marker-assisted selection to improve the body measurement and meat quality traits in the Qinchuan cattle population.
No differences in PRKAG2 transcript abundance were detected in small intestine, liver or muscle. Correlation between gene expression level of PRKAG2 in rumen and average daily feed intake was detected in both seasons but the direction differed by season.
Alleles of 2 equine AMPK gamma subunit genes had no causative role in polysaccharide storage myopathy in horses
eQTL analysis found that rs10224002 was associated with PRKAG2 gene expression in peripheral blood (P = 0.0016). PRKAG2 was differentially expressed between hypertension cases and controls (P = 0.0133), coronary artery disease cases and controls (P = 0.02112) and stroke cases and controls (P = 0.0059).
the PRKAG2-R302Q mutation led to increased AMPK activities, resulting in extensive glycogen deposition and cardiomyocyte hypertrophy.
PRKAG2 mutations are associated with dominant hereditary heart defects that include left ventricular hypertrophy, ventricular pre-excitation, atrial tachyarrhythmia, cardiac conduction disease, and myocardial glycogen storage.
Targeted analysis of DNA methylation array revealed the mesenchymal stem cells in infants born to obese mothers had hypermethylation in genes regulating Fatty Acid Oxidation (PRKAG2, ACC2, CPT1A, SDHC) and corresponding lower mRNA content of these genes. Moreover, mesenchymal stem cells methylation was positively correlated with infant adiposity.
molecular screening for PRKAG2 mutations should be considered in patients who exhibit cardiac hypertrophy coexisting with ventricular pre-excitation. CMR offers promising advantages for evaluation of PRKAG2 cardiomyopathy.
PRKAG2-mutated iPSC-CMs displayed functional and structural abnormalities, which were abolished by correcting the mutation in the patient's iPSCs using CRISPR technology.
gamma2 AMPK activation downregulates fundamental sinoatrial cell pacemaker mechanisms to lower heart rate, including sarcolemmal hyperpolarization-activated current (I f) and ryanodine receptor-derived diastolic local subsarcolemmal Ca(2+) release. In contrast, loss of gamma2 AMPK induces a reciprocal phenotype of increased heart rate, and prevents the adaptive intrinsic bradycardia of endurance training.
Case Report: PRKAG2 missense mutation causing glycogen storage disease and severe biventricular hypertrophy and high-grade atrio-ventricular block.
We highlight the potential for patients with PRKAG2 mutations.
This study of patients with PRKAG2 mutations provides a more comprehensive view of the natural history of this disease and demonstrates a high risk of cardiac complications. Early recognition of this disease appears important to allow an appropriate management.
A novel missense genetic variant of unknown significance (GVUS) was detected in the PRKAG2 gene (c.869A>T, p.K290I). This novel GVUS has not been identified in any global population databases.
As in patients with PRKAG2 cardiomyopathy, iPS cell and mouse models are protected from cardiac fibrosis, and we define a crosstalk between AMPK and post-transcriptional regulation of TGFbeta isoform signaling that has implications in fibrotic forms of cardiomyopathy.
Identify a novel, de novo PRKAG2 mutation (K475E) in the cystathionine beta-synthase 3 repeat, a region critical for AMP binding, which affects AMP-activated protein kinase activity, activates cell growth pathways, and results in cardiac hypertrophy, which can be reversed with rapamycin.
PRKAG2 polymorphism maybe important factor treating hypertensive patients with hydrochlorothiazide.
Data suggest different gamma-isoforms in AMPK can have different effects on enzyme activation; here, activation of AMPK by compound 991 is greater if AMPK contains PRKAG2 versus PRKAG1 or PRKAG3.
mice with chronic AMPK activation, resulting from mutation of the AMPK gamma2 subunit, exhibit ghrelin signaling-dependent hyperphagia, obesity, and impaired pancreatic islet insulin secretion. Humans bearing the homologous mutation manifest a congruent phenotype.
PRKAG2 cardiac syndrome may present with eccentric distribution of LVH, involving focal mid-infero-lateral pattern in the early disease stage, and more diffuse pattern but focusing on interventricular septum in advanced cases.
Overexpression of G100S mutation in PRKAG2 causes Wolff-Parkinson-White syndrome in transgenic zebrafish.
Its mutation causes AMPK signaling abnormality which leads to cardiac syndrome.
The PRKAG2 autosomal dominant cardiac syndrome may be commonly characterized by Left Ventricular Hypertrophy, an accessory pathway, and progression to conduction disease requiring implantation of a pacemaker.
gamma2-specific AMPK activity was elevated in neonatal FNIP1-deficient myocardium, supporting a role for FNIP1 as a negative regulator of AMPK.
Increased AMPK-gamma2 activation is required to protect against myocardial ischemia/reperfusion injury.
These results demonstrate that expression of AMPK subunit gamma-2(NI) and AMPK subunit gamma-2(RG) mutations at physiological levels can induce beneficial metabolic effects but that this is accompanied by Wolff-Parkinson-White Syndrome syndrome.
Prkag2 point mutation causes glycogen storage via enhanced insulin sensitivity and AKT activation. It stimulates postnatal cardiomyocyte proliferation by downregulating FoxO. It promotes cardiac hypertrophy via mTOR activation in developed hearts.
We have demonstrated that a third AMPK gamma2 variant, gamma2-3B, is increasingly expressed in the developing heart.
important for cigarette smoking-induced IL-8 production by lung epithelial cells
CNTF(Ax15) bypasses diet-induced leptin resistance to reduce hypothalamic AMPK activity
CR resulted in incerasd AMPK phosphorylation and, hence, activation. GHR knockout animals also exhibited invrease p-AMPK levels. P-AMPK levels were not altered by disruption of the GHR gene.
Despite high glycogen content, the TGT400N heart is not protected against ischemia-reperfusion injury.
Ceramide- and AMPK-mediated signaling pathways augment the expression and activity of 11beta-HSD1 in preadipocytes by way of C/EBPbeta.
AMP-activated protein kinase (AMPK) is a heterotrimeric protein composed of a catalytic alpha subunit, a noncatalytic beta subunit, and a noncatalytic regulatory gamma subunit. Various forms of each of these subunits exist, encoded by different genes. AMPK is an important energy-sensing enzyme that monitors cellular energy status and functions by inactivating key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This gene is a member of the AMPK gamma subunit family and encodes a protein with four cystathionine beta-synthase domains. Mutations in this gene have been associated with ventricular pre-excitation (Wolff-Parkinson-White syndrome), progressive conduction system disease and cardiac hypertrophy. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
5'-AMP-activated protein kinase subunit gamma-2
, AMP-activated protein kinase gamma2 subunit
, AMPK gamma 2
, adenosine monophosphate-activated protein kinase gamma 2-subunit
, 5'-AMP-activated protein kinase gamma-2 non-catalytic subunit
, protein kinase, AMP-activated, gamma 2 non-catalytic subunit
, AMPK-activated protein kinase gamma-2 subunit
, AMPK subunit gamma-2
, 5-AMP-activated protein kinase, gamma-2 subunit
, AMPK gamma-2 chain
, AMPK gamma2