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anti-Human GCK Anticorps:
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Human Polyclonal GCK Primary Antibody pour IHC (p), ELISA - ABIN544489
Gloyn, Noordam, Willemsen, Ellard, Lam, Campbell, Midgley, Shiota, Buettger, Magnuson, Matschinsky, Hattersley: Insights into the biochemical and genetic basis of glucokinase activation from naturally occurring hypoglycemia mutations. dans Diabetes 2003
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Human Polyclonal GCK Primary Antibody pour IHC (p), ELISA - ABIN544490
Rizzo, Magnuson, Drain, Piston: A functional link between glucokinase binding to insulin granules and conformational alterations in response to glucose and insulin. dans The Journal of biological chemistry 2002
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Human Monoclonal GCK Primary Antibody pour ELISA, WB - ABIN966192
Barbetti, Cobo-Vuilleumier, Dionisi-Vici, Toni, Ciampalini, Massa, Rodriguez-Bada, Colombo, Lenzi, Garcia-Gimeno, Bermudez-Silva, Rodriguez de Fonseca, Banin, Aledo, Baixeras, Sanz, Cuesta-Muñoz: Opposite clinical phenotypes of glucokinase disease: Description of a novel activating mutation and contiguous inactivating mutations in human glucokinase (GCK) gene. dans Molecular endocrinology (Baltimore, Md.) 2009
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Human Monoclonal GCK Primary Antibody pour ELISA, WB - ABIN969172
Yoshida, Kato, Yokoi, Oguri, Watanabe, Metoki, Yoshida, Satoh, Aoyagi, Nishigaki, Nozawa, Yamada: Association of genetic variants with chronic kidney disease in individuals with different lipid profiles. dans International journal of molecular medicine 2009
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Human Polyclonal GCK Primary Antibody pour FACS, IF - ABIN411493
Huang, Chou, Lee, Chen, Chen, Tao, Shih: MicroRNA-130a can inhibit hepatitis B virus replication via targeting PGC1α and PPARγ. dans RNA (New York, N.Y.) 2015
Cow (Bovine) Polyclonal GCK Primary Antibody pour WB - ABIN2788816
Tian, Liu, Wang, Dong, Su, Ma, Zhang: Anti-diabetes effect of chronic intermittent hypobaric hypoxia through improving liver insulin resistance in diabetic rats. dans Life sciences 2016
Human Polyclonal GCK Primary Antibody pour IF (p), IHC (p) - ABIN734558
Wang, Liu, Chen, Duan, Chen, Xi: Effects of a Novel Glucokinase Activator, HMS5552, on Glucose Metabolism in a Rat Model of Type 2 Diabetes Mellitus. dans Journal of diabetes research 2017
Human Polyclonal GCK Primary Antibody pour IF, WB - ABIN6680620
Zang, Fan, Chen, Huang, Qin: Improvement of Lipid and Glucose Metabolism by Capsiate in Palmitic Acid-Treated HepG2 Cells via Activation of the AMPK/SIRT1 Signaling Pathway. dans Journal of agricultural and food chemistry 2018
The prevalence of glucokinase variant-induced diabetes (GCK-DM)is approximately 1.3% in the Chinese population with diabetes, and the new clinical screening strategy is helpful for identifying GCK-DM.
In 263 Japanese partients with suspected maturity-onset diabetes of the young, mutations were identified in 103 (39.2%) patients: 57 mutations in GCK; 29, HNF1A; 7, HNF4A; and 10, HNF1B.
Possible consequences of GCK-MODY (maturity-onset diabetes of the young caused by mutations CSK) during pregnancy on fetal development are generally less severe and may differ from those characteristic for other types of diabetes.
Glucokinase (GCK) plays a key role in beta cell glucose sensing. As one form of congenital hyperinsulinism, activating mutations of GCK result in a decreased threshold for glucose-stimulated insulin secretion and hypoglycemia. In contrast, inactivating mutations of GCK result in diabetes, including MODY2 (mild) and permanent neonatal diabetes mellitus (severe). Review.
The defects in enzymatic activity and protein stability, together with alteration of GKRP binding on GCK mutants may synergistically contribute to the development of maturity onset diabetes of young type 2 hyperglycemia
Effect of sequence variants on variance in glucose levels predicts type 2 diabetes risk and accounts for heritability.
Maturity Onset Diabetes of the Young due to Glucokinase, HNF1-A, HNF1-B, and HNF4-A Mutations in a Cohort of Turkish Children Diagnosed as Type 1 Diabetes Mellitus.
Our results suggest that the polymorphism of CYP3A4 *18B and GCK G-30A might affect the new-onset diabetes after transplantation (NODAT) development under tacrolimus-based immunotherapy. We suspect that the depression of GCK function may be a crucial pathogenic factor of tacrolimus-induced NODAT in variant carrier with A allele of GCK, but not be simply reflecting of glucose change.
Data suggest that the following genetic modifications are involved in neonatal diabetes mellitus patients in Oman: (1) mutation in KCNJ11 (potassium voltage-gated channel subfamily J member 11; one patient); (2) mutation in GCK (glucokinase); (3) mutation in SLC2A2 (glucose transporter type 2); (4) chromosome 6q24 methylation abnormalities.
GCK gene mutations were detected in Chinese children and their family members with typical clinical features of glucokinase-maturity-onset diabetes of the young. Four novel mutations were detected.
The studies screening criteria allowed for the identification of glucokinase (GCK)-deficient patients who were diagnosed with gestational diabetes, and these mutations in the GCK gene were not common in Chinese women with gestational diabetes.
Functional characterization of MODY2 mutations in the nuclear export signal of glucokinase.
44 different mutations affecting the GCK and co-segregating with the clinical phenotype of MODY were identified.
Twenty-five different variants were identified in GCK gene (30 probands-61% of positivity), and 7 variants in HNF1A (10 probands-17% of positivity). Fourteen of them were novel (12- GCK /2- HNF1A ). ACMG guidelines were able to classify a large portion of variants as pathogenic (36%- GCK /86%- HNF1A ) and likely pathogenic (44%- GCK /14%- HNF1A ), with 16% (5/32) as uncertain significance.
a nuclear import of glucokinase mediated by a redundant mechanism, involving a nuclear localization signal, and which is modulated by its SUMOylation, is reported.
La variante confirmada of the glucokinase gene para esta familia es c.148C>T, p.His50Tyr. Tiene caracter patogenico, dado que produce una disminucion de la actividad enzimatica de GCK y ha sido reportada en la literatura
described the clinical and genetic presentation of four families with activating GCK mutations The clinical phenotype of the GCK activating mutation carriers was heterogeneous, the severity of symptoms and age at presentation varied markedly between affected individuals, even within the same family.
the contribution of the Maturity Onset Diabetes of the Young gene GCK in the etiology of 23 unrelated Tunisian families
GCK-dependent glycolysis regulates Treg cell migration.
Mutations in the GCK gene were identified in 79 out of 177.
These data also imply an etiological role of GCK in diet-induced diabetes.
Long-term treatment with octanoic acid increased cellular glucose uptake in MIN6 cells by up-regulating the expression of glucokinase (GK).
Glucokinase governs an alpha-cell metabolic pathway that suppresses secretion at or above normoglycemic levels; abnormal suppression of glucagon secretion deregulates hepatic glucose metabolism and, over time, induces a pre-diabetic phenotype.
GCK expression is regulated by nutrient-sensing O-linked beta-N-acetylglucosaminylation cycling in liver.
Absence of Gck expression did not prevent the glucose responsiveness of glucose-excited or glucose-inhibited Sf1 neurons in either sex. Thus Gck in the VMN plays a sex-specific role in the glucose-dependent control of autonomic nervous activity; this is, however, unrelated to the control of the firing activity of classical glucose-responsive neurons.
Using a mutant GCK gene (GCK 262) with a knocked out cytosine at position 2643 results in lower protein expression and more ubiquitination-led protein degradation compared with wild-type GCK (GCK 261)
lncLGR facilitates the recruitment of hnRNPL to the GCK promoter and suppresses GCK transcription.
Given that acetylated GKRP may affiliate with type-2 diabetes mellitus (T2DM), understanding the mechanism of GKRP acetylation in the liver could reveal novel targets within the GK-GKRP pathway, for treating T2DM and other metabolic pathologies.
These results suggest a mechanism for integrative control over GCK activation and, therefore, glucose metabolism and insulin secretion through regulation of cytoplasmic Ca(2+) levels.
GHR knockdown caused increased glucokinase mRNA and protein levels.
results suggest that chronic suppression of hepatic glucokinase has a small influence on intertissue (liver-to-BAT as well as liver-to-beta-cell) metabolic communication
Atf3-silencing reversed ethanol-mediated Gck down-regulation and beta-cell dysfunction, followed by the amelioration of impaired glucose tolerance and insulin resistance.
Suggest heterozygous glucokinase knockout mouse as a translatable model of human type 2 diabetes.
Chronic treatment with glucose kinase activators in animal models of diabetes provided sustained lowering of blood glucose.
In the liver-specific glucokinase knockout mouse reduced expression of glucokinase in the liver induces diabetic cardiomyopathy.
Glucokinase is regulated by the ubiquitin-proteasome system to avoid misfolding and reduced activity of the enzyme.
IRS-2 signalling is important for maintaining the activity of liver glucokinase.
Hepatic GK overexpression in obesity-resistant mice promoted weight gain, while hepatic GK knockdown in obesity-prone mice attenuated weight gain with increased adaptive thermogenesis.
In this study, the level of GK mRNA was significantly higher in fish fed the low-carbohydrate (20%)/high protein diet (50%).
This study using immunoreactive techniques, we have demonstrated in those specific areas of the rainbow trout brain previously described as glucosensor the presence of glucokinase in different cell types.
GKRP binds to a super-open conformation of GK mainly through hydrophobic interaction, inhibiting the GK activity by locking a small domain of GK.
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, the first step in most glucose metabolism pathways. Alternative splicing of this gene results in three tissue-specific forms of glucokinase, one found in pancreatic islet beta cells and two found in liver. The protein localizes to the outer membrane of mitochondria. In contrast to other forms of hexokinase, this enzyme is not inhibited by its product glucose-6-phosphate but remains active while glucose is abundant. Mutations in this gene have been associated with non-insulin dependent diabetes mellitus (NIDDM), maturity onset diabetes of the young, type 2 (MODY2) and persistent hyperinsulinemic hypoglycemia of infancy (PHHI).
, HK IV
, hexokinase D, pancreatic isozyme
, hexokinase type IV
, hexokinase 4
, glucokinase (hexokinase 4, maturity onset diabetes of the young 2)