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- Table of Contents
Facts about Glycogen [starch] synthase, muscle.
Human | |
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Gene Name: | GYS1 |
Uniprot: | P13807 |
Entrez: | 2997 |
Belongs to: |
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glycosyltransferase 3 family |
EC 2.4.1.11; glycogen [starch] synthase, muscle; glycogen synthase 1 (muscle); GYSGSY
Mass (kDA):
83.786 kDA
Human | |
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Location: | 19q13.33 |
Sequence: | 19; NC_000019.10 (48968130..48993309, complement) |
This article discusses the Anti-Glycogen Systase 1/GYS1 Antibody. It also discusses the Specificity and Validation of the antibodies. Boster is the only company to validate its antibodies using known positive and negative samples. This ensures high affinity and specificity. Boster recognizes that product reviews are important and rewards early reviewers by giving them a product credit. This incentive is offered to all scientists in the world.
GYS1 was shown to inhibit excessive AMPK activation in RA. This has allowed synovial inflammation to be controlled. GYS1 might be suppressed as a novel strategy to combat chronic inflammatory disease. This research is based in part on the findings from other researchers. They found that GYS1 knockdown reduced inflammation markers and inhibited invasion and chemotactic chemotactic movements.
This antibody reacts to Glycogen synthase-1, (GYS1) from mouse or rat. It is part of the Picoband(tm) catalog and has been tested in ELISA and Flow Cytometry. Boster Bio validated the antibody in ELISA and immunofluorescence.
This antibody recognizes GYS1 (pS641) and is monoclonal. This monoclonal antibody was affinity purified using antiserum raised against the phosphorylated immunizing protein. This antibody recognizes phosphorylated GYS1 but has cross-reactivity with muscle glycogen synthase in mouse tissues.
GYS1 has been found in many cells, and even in cancer cells. GYS1 expression is found in many types tumor cell lines. A poor prognosis has been linked with some cancers. It is not clear if glycogen metabolism can be disrupted by chronic inflammation diseases. However, RA patients' ST and FLSs had increased levels of glycogen. GYS1 is therefore not understood in RA.
AICAR can decrease the effects of collagen-induced joint disease. It is effective in reducing the symptoms of collagen-induced arthritis in rats. However, it is not recommended for clinical use. Until now, a better candidate for anti-Glycogen synthase psuedo-glycogen synthase antibodies is needed.
Insulin resistance is linked to Gys1, which encodes the muscle glycogen synase gene. It is not known how the gene functions, nor how specific deficiencies in muscle glucose storage might contribute to insulin resistance. We used a Cre/loxP system to create muscle-specific GYS1 mice. This was done in order to better understand the role of this gene for diabetes. We then tested the mice with glucose tolerance, euglycemic clamps.
GYS1 is highly expressed within beta cells. Previous studies have shown that glycogen is more prevalent in beta cells due to their higher glycogenic ability. We created a Pdx1-1-cre transgenic line to delete Gys1 from the Pancreas in early embryonic stages. We observed that beta-cell-specific Gys1KO mice were born at the Mendelian ratio. This result eliminated embryonic lethality and we now have evidence of the GYS1 gene’s role in glucose homeostasis.
Glycogen storage diseases can be caused by the GYS1 gene. These are inborn errors of glycogen synthesis and catabolism that can often lead to life-threatening complications. Since the GYS1 gene is highly heterogeneous, diagnosing glycogen storage diseases has been challenging. However, a massively parallel sequencing (MPS) test has been developed for the rapid analysis of 16 genes. The 16 genes were enriched for nucleotides within the coding region.
Ozgene offers a genetic construct that targets Gys1 gene expression in mice. It includes an MLC promoter to drive expression of mercremer and a HS4 boostr to enhance tissue-specific expression. We crossed gys1lox/lox-mercremer mice with gys1lox/lox mouse lines. We obtained 4 genotypes each from each cross and then selected 2 to represent the experimental or control groups.
GYS1 is a marker that can be used to assess muscle glucose metabolism. Although the gene is involved in the metabolism of glucose, previous studies have not been able to identify the mechanism. In this study, we have investigated how a conditional deletion of the GYS1 gene affects muscle glucose and exercise metabolism. This will allow us to test whether gys1 mutations are able to predict diabetes, obesity, or other metabolic disorders.
The GYS1 marker can be used by scientists and clinicians to identify patients most at-risk for Pompe disease. It is a rare, inherited disease caused in part by mutations in acid alpha-glucosidase. Deficiency in this enzyme causes abnormal accumulations of glycogen and eventually leads to respiratory compromise, progressive weakness, and respiratory compromise. GYS1 inhibits, which are drugs that have been shown to be effective in this condition, were well-tolerated by both patients (and their caregivers).
The GYS1 marker was validated using a mouse model of APBD. Mice with this mouse model showed a reduction of the GYS1 protein by 85% compared to controls. GYS1 gene expression was also found in the heart as well as the WAT. GYS1KO mice showed a decreased activity in glycogen synthase. However, there were no significant differences between the experimental group and the control group in WAT or heart.
In mice with APBD, the GYS1 genes is missing in a model. The mice with this mutation show gait difficulty, a hallmark of the disease. This phenotypic result can be rescued using the APBD mouse model. The results support the predictive validity of the GYS1 gene marker for the GSD IV variant in human patients. The GYS1 Gene is an important biomarker to APBD.
Further studies have shown that GYS1 is expressed in all three major organs. GYS1 is expressed in muscle and brain while glucose is stored in the liver. Gbe1ys/ys mice had a significantly lower level of total glycogen. The research is ongoing. Once validated, GYS1 will be used for research purposes. It is still not clear if Gbe1ys/ys-mutant mice have a lower liver glycogen level than gbe1ys/ys.
GYS1 codes for muscle glycogen synthesise. This protein is present in all cells but is particularly abundant within the heart and skeletal. Glycogen (the body's major energy source) is stored in muscle cells. Glycogen is broken down to provide energy during exercise. Although the function of GYS1 in the body is not clear, it is thought to be involved in energy production and metabolism.
The GYS1 marker can be used in many ways in horses. It can detect positive selection in horses. In addition, it can detect low allele frequencies and paucity of haplotype diversity. The GYS1 Haplotype is closely related to the Arg309His Allele of the derived GYS1 Marker. Moreover, extended LD near the "A" allele supports the hypothesis of positive selection in the equine population.
The mutation has been shown to be linked to insulin action in Pima Indians, NIDDM, and other forms of insulin resistance. It has also been associated to insulin resistance. GYS1 PSSM mutation can be found at position 309, and the surrounding amino acids are highly preserved in both GS isoforms. These results suggest GYS1 might be a useful marker in the detection of insulin resistance in horses. This mutation has also been associated with decreased insulin resistance in horses.
Another example of how this mutation could be used in horses is in diagnosing PSSM. Horses with the GYS1 Her309 allele are more susceptible to developing muscle pain due to PSSM than horses who have the non-H allele. GYS1 mutations may increase skeletal muscle glycogen. It could be a mechanism for the higher polysaccharide level in PSSM in horses.
PMID: 2493642 by Browner M.F., et al. Human muscle glycogen synthase cDNA sequence: a negatively charged protein with an asymmetric charge distribution.
PMID: 7657035 by Orho M., et al. Isolation and characterization of the human muscle glycogen synthase gene.