Differential impact of glycation on apolipoprotein A-I of high-density lipoprotein: a review

Hyperglycemia is a poorly controlled diabetic condition, affects about 70% of people all round the world. In the year 2015, about 41.5 crore people were diabetic and is expected to reach around 64.3 crore by the year 2040. Cardiovascular diseases (CVDs) are considered as one of the major risk factors that cause more than half of the death of diabetic patients and promote related comorbidities. Atherosclerosis and amyloidosis are the prime factors linked with CVDs. Apolipoprotein A-I (ApoA-I) of HDL have protective action against CVDs, participate in reverse cholesterol transport mechanism and lipid metabolism, but gets easily glycated under prolonged hyperglycemic aura, i.e. glycation. ApoA-I have a potent role in maintenance of glucose level, providing a compelling link between diabetes and CVDs. Increased protein glycation in people with diabetes promote atherosclerosis, which might play possible role in promotion of protein aggregation by altering the protein structure and its confirmation. Here, we intend to investigate the mechanistic behavior of ApoA-I under the menace of glycation and its impact on ApoA-I structure and function that possibly link with aggregation or amyloidosis.

Automated summary

Hyperglycemia, affecting about 70% of the global population, is a poorly controlled diabetic condition. Cardiovascular diseases (CVDs) are major risk factors causing the death of diabetic patients and promoting related comorbidities. Atherosclerosis and amyloidosis are strongly linked with CVDs. Apolipoprotein A-I (ApoA-I) of HDL plays a protective role against CVDs but easily becomes glycated under prolonged hyperglycemic conditions. ApoA-I also has an important role in maintaining glucose levels, providing a compelling link between diabetes and CVDs. Increased protein glycation in people with diabetes promotes atherosclerosis and possibly protein aggregation or amyloidosis.