This product is a CRISPR/Cas9-edited polyclonal knockout cell population derived from the Jurkat human T-lymphocyte cell line, featuring targeted disruption of the GYS1 gene. GYS1 encodes glycogen synthase, the rate-limiting enzyme in glycogen synthesis, and its loss provides a loss-of-function model for investigating glycogen metabolism, insulin signaling, and energy homeostasis.
Jurkat cells are an immortalized T-lymphocyte line established from the peripheral blood of a 14-year-old male with acute T-cell leukemia. They are widely used for studying T-cell receptor signaling, apoptosis, and cancer biology. Jurkat cells display high glycolytic activity typical of the Warburg effect and harbor functional glycogen metabolism pathways, making them an ideal host for exploring the role of GYS1 in immune cell energetics and leukemic growth.
Glycogen synthase (GYS1) catalyzes the transfer of glucose from UDP-glucose to a growing glycogen chain, functioning as a key regulatory node. Insulin signaling, through INSR?CIRS1?CPI3K?CAKT, inhibits GSK3??, reducing inhibitory phosphorylation of GYS1 and promoting glycogen synthesis. Conversely, glucagon, epinephrine, and AMPK promote GYS1 phosphorylation via GSK3??, suppressing its activity. GYS1 interacts with glycogenin and protein phosphatase 1 regulatory subunits, including PPP1R3C (PTG), PPP1R3B, and PPP1R3D, which mediate its activation. Downstream, GYS1 activity generates glycogen and consumes UDP-glucose, linking nutrient-sensing pathways to carbohydrate storage.
In Jurkat T cells, GYS1 knockout enables dissection of the intersection between immune signaling and metabolic reprogramming. T lymphocytes rely on glycolysis during activation, yet glycogen turnover contributes to memory T-cell function and survival. Loss of GYS1 in this leukemic context permits analysis of how impaired glycogen synthesis affects proliferation, stress resistance, and metabolic inhibitor sensitivity, offering insights into T-cell biology and potential vulnerabilities in leukemia.
Researchers can employ these GYS1 knockout polyclonal cells in diverse experimental workflows. Glycogen synthesis defects are detectable via glycogen content assays or periodic acid?CSchiff (PAS) staining. Western blotting for GYS1 and phospho-GSK3?? confirms gene disruption and monitors insulin pathway activity. Functional metabolic studies, including glucose uptake assays and Seahorse metabolic flux analysis, reveal shifts in glycolytic and oxidative metabolism. This model supports research into the Warburg effect, mTOR signaling, glycogen storage diseases, and diabetes mellitus. For further details or custom cell engineering inquiries, please contact Ascent Research.
