Diabetes is a
metabolic disease characterized by high
blood sugar. Its complications may damage multiple organs, such as eyes, kidneys, heart, blood vessels, and nerves, severely threatening human health.
Transferrin (Tf) is a major
iron transport protein in the body. Recent studies have shown that the degree of non-enzymatic glycated modification of Tf is increased in diabetic patients, and glycated Tf is closely related to the occurrence and development of diabetes and
diabetic complications. However, the molecular mechanisms underlying this glycated modification in diabetes and
diabetic complications are still unclear. It is speculated that the mechanism may be that glycated modification reduces the binding ability of Tf and its receptor TfR, followed by excessive
iron accumulation in the body.
Iron overload in the body may further lead to the death of pancreatic beta cells and
insulin resistance by increasing oxidative stress, inducing
iron death, interfering with the
insulin signaling pathway, and causing autophagy deficiency. In addition, non-enzymatic glycation affects the binding of Tf with
chromium and reduces the ability of Tf to transport
chromium into tissues, resulting in a decrease in the levels of
chromium in tissues and ultimately affecting the sensitivity of tissues to
insulin. In diabetic patients, the concentrations of glycated Tf in serum were significantly correlated with those of
fructosamine.Tf has a shorter half-life, and not affected by
anemia or
hypoalbuminemia and less negative charge under physiological conditions, while glycated modification could not change the isoelectric point of Tf, which easily passes through the negatively charged basement membrane of the glomerulus. Therefore, compared to
glucosamine, HbA1C, etc., glycated Tf may be a future
biomarker for evaluating short-term
glycemic control and early renal damage in diabetic patients.