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Glycogen synthase 1

GYS1, Gys
The protein encoded by this gene catalyzes the addition of glucose monomers to the growing glycogen molecule through the formation of alpha-1,4-glycoside linkages. Mutations in this gene are associated with muscle glycogen storage disease. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Sep 2009] (from NCBI)
Top mentioned proteins: Insulin, HAD, ACID, CAN, AGE
Papers using GYS1 antibodies
A rapid filter paper assay for UDPglucose-glycogen glucosyltransferase, including an improved biosynthesis of UDP-14C-glucose.
Tora Laszlo, In PLoS ONE, 1967
... - We used the following commercial siRNAs: HIF1alpha siRNA (Santa Cruz, predesigned siRNA#16708), GYS1 siRNA (Qiagen, SI01060843), and All Stars ...
Papers on GYS1
Polyglucosan storage myopathies.
Oldfors et al., Göteborg, Sweden. In Mol Aspects Med, Dec 2015
There is also a common equine polysaccharide storage myopathy belonging to this group of diseases involving the GYS1 gene.
Pathological glycogenesis through glycogen synthase 1 and suppression of excessive AMP kinase activity in myeloid leukemia cells.
Sattler et al., Boston, United States. In Leukemia, Jul 2015
Targeting the rate-limiting glycogen synthase 1 (GYS1) not only decreased glycolytic flux but also increased activation of the glycogen-responsive AMP kinase (AMPK), leading to significant growth suppression.
Overexpression of GYS1, MIF, and MYC is associated with adverse outcome and poor response to azacitidine in myelodysplastic syndromes and acute myeloid leukemia.
Pérez-Simón et al., Sevilla, Spain. In Clin Lymphoma Myeloma Leuk, Apr 2015
RESULTS: Overexpression of glycogen synthase 1 and macrophage migration inhibitory factor genes had an adverse outcome in multivariate analysis (P = .003
Expression and purification of functional human glycogen synthase-1:glycogenin-1 complex in insect cells.
Sakamoto et al., Lausanne, Switzerland. In Protein Expr Purif, Apr 2015
We report the successful expression and purification of functional human muscle glycogen synthase (GYS1) in complex with human glycogenin-1 (GN1).
Short-term high-fat diet increases macrophage markers in skeletal muscle accompanied by impaired insulin signalling in healthy male subjects.
Rensen et al., Leiden, Netherlands. In Clin Sci (lond), 2015
This was accompanied by down-regulation of SLC2A4 and GYS1 mRNA expression, and elevated plasma glucose (+4%, P<0.001) and insulin (+55%, P<0.001) levels together with homoeostasis model assessment of insulin resistance (HOMA-IR) (+48%, P<0.001), suggesting development of insulin resistance (IR).
Role of brain glycogen in the response to hypoxia and in susceptibility to epilepsy.
Delgado-García et al., Sevilla, Spain. In Front Cell Neurosci, 2014
To address these issues, we used our brain-specific Glycogen Synthase knockout (GYS1(Nestin-KO)) mouse to study the functional consequences of glycogen depletion in the brain under hypoxic conditions and susceptibility to epilepsy.
Neuron-astrocyte interaction enhance GABAergic synaptic transmission in a manner dependent on key metabolic enzymes.
Mozrzymas et al., Wrocław, Poland. In Front Cell Neurosci, 2014
Moreover, treatment of ANCC with inhibitor of glycogen phosphorylase (Gys) (BAYU6751) or with selective inhibitor of astrocytic Krebs cycle, fluoroacetate, resulted in a marked reduction of mIPSC frequency in ANCC having no effect in NC.
Glucose-6-phosphatase is a key metabolic regulator of glioblastoma invasion.
Quinones-Hinojosa et al., Baltimore, United States. In Mol Cancer Res, 2014
Downregulation of G6PC renders the majority of these cells unable to survive glycolytic inhibition, and promotes glycogen accumulation through the activation of glycogen synthase (GYS1) and inhibition of glycogen phosphorylase (PYGL).
Prospection of genomic regions divergently selected in racing line of Quarter Horses in relation to cutting line.
Mota et al., Jaboticabal, Brazil. In Animal, 2014
Genes involved in muscle growth (n=8), skeletal growth (n=10), muscle energy metabolism (n=15), cardiovascular system (n=14) and nervous system (n=23) were identified, including the FKTN, INSR, GYS1, CLCN1, MYLK, SYK, ANG, CNTFR and HTR2B.
Parallel evolution of the glycogen synthase 1 (muscle) gene Gys1 between Old World and New World fruit bats (Order: Chiroptera).
Zhang et al., Shanghai, China. In Biochem Genet, 2014
Glycogen synthase 1, encoded by the Gys1 gene, is the glycogen synthase isozyme that functions in muscles.
Transcriptional expression changes of glucose metabolism genes after exercise in thoroughbred horses.
Kim et al., Pusan, South Korea. In Gene, 2014
In the present study, we monitored the expression levels of LDHA (lactate dehydrogenase) and GYS1 (glycogen synthase 1) in the blood, to confirm the roles of these genes in exercise physiology.
Evaluation of Protein Expression in Housekeeping Genes across Multiple Tissues in Rats.
Park et al., Kwangju, South Korea. In Korean J Pathol, 2014
METHODS: The protein expression profiles of seven housekeeping genes (HPRT1, PPIA, GYS1, TBP, YWHAZ, GAPDH and ACTB) in various rat tissues (cerebrum, cerebellum, cardiac ventricle and atrium, psoas muscle, femoral muscle, liver, spleen, kidney, and aorta) were analyzed by Western blot and compared by coefficient of variation (CV).
Antisense Oligonucleotide-mediated Suppression of Muscle Glycogen Synthase 1 Synthesis as an Approach for Substrate Reduction Therapy of Pompe Disease.
Wentworth et al., Framingham, United States. In Mol Ther Nucleic Acids, 2013
A phosphorodiamidate morpholino oligonucleotide (PMO) designed to invoke exon skipping and premature stop codon usage in the transcript for muscle specific glycogen synthase (Gys1) was identified and conjugated to a cell penetrating peptide (GS-PPMO) to facilitate PMO delivery to muscle.
Glucose utilization via glycogen phosphorylase sustains proliferation and prevents premature senescence in cancer cells.
Harris et al., Radcliffe, United Kingdom. In Cell Metab, 2013
Concordantly, glycogen synthase (GYS1) showed a rapid induction, followed by a later increase of glycogen phosphorylase (PYGL).
GLUT4 and glycogen synthase are key players in bed rest-induced insulin resistance.
Wojtaszewski et al., Copenhagen, Denmark. In Diabetes, 2012
The present findings demonstrate that physical inactivity-induced insulin resistance in muscle is associated with lower content/activity of key proteins in glucose transport/phosphorylation and storage.
Neurodegeneration and functional impairments associated with glycogen synthase accumulation in a mouse model of Lafora disease.
Guinovart et al., Barcelona, Spain. In Embo Mol Med, 2011
Neurodegeneration and functional impairments are associated with glycogen synthase accumulation in the mouse model of Lafora disease.
Insulin-stimulated glycogen synthesis and glycogen synthase activation after electrical stimulation of epitrochlearis muscles with different initial glycogen contents.
Jensen et al., Oslo, Norway. In Arch Physiol Biochem, 2010
After contraction insulin-stimulated glycogen synthesis was increased by rather similar magnitude at all glycogen contents in concert with increased glycogen synthase activation.
Hypoxia promotes glycogen accumulation through hypoxia inducible factor (HIF)-mediated induction of glycogen synthase 1.
del Peso et al., Madrid, Spain. In Plos One, 2009
GYS1 regulation by HIF plays a central role in the hypoxic accumulation of glycogen, and hypoxia also upregulates the expression of UTP:glucose-1-phosphate urydylyltransferase (UGP2) and 1,4-alpha glucan branching enzyme (GBE1)
[The regulation of glucose-6-phosphate dehydrogenase and glycogen synthase activities by insulin superfamily peptides in myometrium of pregnant women and its impairments under different types of diabetes mellitus].
Chistiakova et al., In Biomed Khim, 2009
The regulation of glucose-6-phosphate dehydrogenase and glycogen synthase activities by insulin superfamily peptides in myometrium of pregnant women and its impairments under different types of diabetes mellitus
Trace elements in regulation of NF-kappaB activity.
Kudrin, Moscow, Russia. In J Trace Elem Med Biol, 2000
DNA-binding activity of NF-kappaB is regulated by the redox state of the cysteine residue (Gys-62) in the DNA binding domain of the p50 subunit and impaired by different metals (Go, Cr, Ni, Cd, Pb).
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