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Home > Protein Information

Adipose(ADP)

Adipose tissue is mainly composed of large amounts of clustered fat cells. Adiponectin/ADP is an endogenous bioactive peptide or protein secreted by adipose cells. Adiponectin is An Insulin- sensitization Hormone, which can improve Insulin resistance and atherosclerosis in mice. Human studies have found that adiponectin levels predict the development of type 2 diabetes and coronary heart disease, and show potential in clinical trials to combat diabetes, atherosclerosis and inflammation. Researchers have discovered a new compound that regulates adiponectin, thus providing a new way to study the function of adiponectin and the mechanism of insulin sensitivity. Insulin is a hormone secreted by the cells of the pancreas, the organ of the pancreas. Its main function is to promote glucose in the blood to the muscles or adipose tissue and provide energy for the body. 
When insulin fails to work, glucose in the blood cannot be converted into the energy needed by the human body, causing blood sugar to rise and diabetes occurs. Insulin resistance refers to the inability of cells to effectively use and even become less sensitive to insulin, which is the main cause of diabetes. 
Scientists believe that molecules released by free fatty acids and certain fats are responsible for insulin resistance. Lily Dong and her collaborators have been looking for cellular proteins associated with adiponectin receptors to find new targets for regulating the function of adiponectin hormones. They identified a multidomain protein that regulates the function of adiponectin in fatty acid oxidation and glucose uptake, and named the new protein APPL1. Their study further showed that APPL1 regulates adiponectin's insulin sensitivity through kinase channels in muscle cells.
Adiponectin is one of the protein products with the most abundant gene expression in adipose tissue, which is abundant in blood circulation. In the human body, a concentration of 3-30ug/ml appears in circulating plasma. Also known as Acrp30, apM1, AdipoQ, and GBP28, adiponectin was originally found in adipocytes in subcutaneous adipose tissue, plasma, and mouse fat cells. Adiponectin in human body is composed of 244 amino acids with a molecular weight of 30KD. It is composed of secretory signal sequences of the amino terminal (aa 1-18), a specific sequence (aa19-41), a collagen repeat sequence (aa 42-107) consisting of 22 amino acids, and a spherical sequence (aa108-244). The spherical area is the key part of adiponectin biological activity, and the structure of TNF alpha, adiponectin and glue the original Ⅷ, X and complement C1q highly homologous. The monomers and trimers of adiponectin are their biologically active forms or receptor affinity ligands that specifically bind to the g-protein-coupled receptors type 1 or type 2 on skeletal muscle or liver cell membranes, thus regulating the oxidation of fatty acids and glucose metabolism.
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