Diabetes is a chronic disease that affects millions of people worldwide, causing a range of complications and health problems. One of the major challenges in managing diabetes is controlling blood sugar levels, especially during episodes of hypoglycemia or insulin shock. However, a recent breakthrough in enzyme discovery offers new hope for diabetes treatment. Scientists have identified a novel enzyme that can block the effects of insulin shock and prevent dangerous glucose drops in people with diabetes. This promising development could revolutionize diabetes management and help millions of patients lead healthier, more productive lives. In this article, we’ll explore the science behind the insulin shock blocker and what it means for the future of diabetes care.
Researchers at the University of California San Diego School of Medicine have discovered an enzyme, fructose-1,6-bisphosphate phosphatase (FBP1), which acts as a natural defence against insulin shock. FBP1 controls gluconeogenesis, a process where the liver synthesises glucose and maintains a steady supply in the bloodstream. The researchers discovered that FBP1 inhibits the protein kinase AKT, preventing insulin hyper-responsiveness and related complications. A peptide derived from FBP1, called E7, was then developed and was shown to reverse insulin resistance and restore normal glycemic control in mice. Insulin is a crucial treatment for type 1 diabetes and, often, for type 2 diabetes. Approximately 8.4 million Americans use insulin, according to the American Diabetes Association.
Hypoglycemia or low blood sugar is a significant cause of death among people with diabetes. Insulin hyper-responsiveness is prevented by FBP1, which curtails AKT activation, an essential conduit of insulin activity. Patients who are treated with insulin or drugs that stimulate insulin secretion often experience hypoglycemia, a condition that, if unnoticed and untreated, can lead to seizures, coma and even death. This discovery may lead to an alternative therapeutic option for millions of people with diabetes.
FBP1 also has a second non-enzymatic but critical function, inhibiting AKT, and acting as a safety valve against insulin hyper-responsiveness, hypoglycemic shock and acute fatty liver disease. This valve reduces the risk of insulin shock caused by excessive insulin in the body, which can be fatal.
In collaboration with scientists from Chongqing University in China, researchers created a peptide derived from FBP1, which disrupted the association of FBP1 with AKT and another protein that inactivates AKT. The peptide works like an insulin mimetic, activating AKT. The peptide injected into mice, which had been rendered insulin resistant due to prolonged consumption of a high-fat diet, reversed insulin resistance and restored normal glycemic control. The researchers claim that the results from the study suggest that it is unlikely that E7 will cause insulin shock, and so they may continue to further develop it as a clinically useful alternative to insulin.
Funding for this research came, in part, from the National Institutes of Health (NIH), whose grants played a crucial role in supporting this research. Further working to decipher the roles of FBP1 may offer new possibilities for improving the efficacy of insulin replacement therapy in diabetic patients.
In conclusion, the discovery of Insulin Shock Blocker, an enzyme that can help prevent dangerous drops in blood sugar levels in people with diabetes, is a groundbreaking development in the field of diabetes treatment. With further research and clinical trials, this enzyme could potentially become a new and effective therapy for individuals with type 1 and type 2 diabetes. By providing a way to avoid the potentially life-threatening complications of hypoglycemia, the Insulin Shock Blocker could greatly improve the quality of life for millions of people living with this chronic disease. As we look to the future of diabetes management and care, this exciting discovery offers hope for better outcomes and brighter prospects for those affected by diabetes.
