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La variante confirmada of the glucokinase gene para esta (show RPL11 Proteins) familia es c.148C>T, p.His50Tyr. Tiene caracter patogenico, dado que (show DBT Proteins) 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.
GCK GCK GCK GCK
GCK gene mutations (pathogenic or likely pathogenic variants) and a novel intronic variant of uncertain significance (c.208 + 3A>T) were identified in 13/54 probands (24%).
Data suggest that hepatic glucokinase activity is regulated by reversible binding to specific inhibitor protein glucokinase regulatory protein (GKRP (show GCKR Proteins)) and by binding to activator proteins such as 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase (PFK2 (show PFKFB3 Proteins)/FBP2 (show KHSRP Proteins)); changes in glucokinase expression and activity are associated with poorly controlled type 2 diabetes and nonalcoholic fatty liver disease. [REVIEW]
GCK expression is regulated by nutrient-sensing O-linked beta-N-acetylglucosaminylation cycling in liver.
GCK mutations are associated with MODY2.
Glucokinase governs an alpha-cell metabolic pathway that suppresses secretion at or above normoglycemic levels; abnormal suppression of glucagon (show GCG Proteins) secretion deregulates hepatic glucose metabolism and, over time, induces a pre-diabetic phenotype.
Absence of Gck expression did not prevent the glucose responsiveness of glucose-excited or glucose-inhibited Sf1 (show SF1 Proteins) 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 (show HNRNPL Proteins) to the GCK promoter and suppresses GCK transcription.
Given that acetylated GKRP (show GCKR Proteins) may affiliate with type-2 diabetes mellitus (T2DM), understanding the mechanism of GKRP (show GCKR Proteins) acetylation in the liver could reveal novel targets within the GK-GKRP (show GCKR Proteins) 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 (show INS Proteins) secretion through regulation of cytoplasmic Ca(2 (show CA2 Proteins)+) levels.
GHR (show GHR Proteins) 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 (show BAAT Proteins) as well as liver-to-beta-cell) metabolic communication
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 (show GCKR Proteins) 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)