Apolipoprotein A-I is a 28 kDa glycoprotein that is predominantly produced by hepatocytes (about 75%) and epithelial cells of the small intestine (about 25%) . In mice, some ApoA-I is also produced by the most proximal part of the colon . The protein is composed of 243 amino acids and has a high affinity for phospholipids, which allows it to form HDL particles.
The primary function of ApoA-I is to promote cholesterol efflux from tissues by acting as a cofactor for the enzyme lecithin-cholesterol acyltransferase (LCAT). This enzyme is responsible for the esterification of cholesterol, which is a critical step in the formation of mature HDL particles . Additionally, ApoA-I has been shown to have anti-inflammatory and antioxidant properties, which contribute to its protective effects against cardiovascular diseases .
Recombinant ApoA-I is produced using various expression systems, with Escherichia coli being one of the most common hosts . The recombinant protein is typically purified to a high degree of purity (>90%) and is suitable for various applications, including SDS-PAGE and mass spectrometry . The recombinant form retains the functional properties of the native protein, making it a valuable tool for research and therapeutic purposes.
Recombinant ApoA-I is widely used in research to study its role in lipid metabolism, cardiovascular diseases, and other related fields. It is also used in the development of synthetic HDL (sHDL) particles, which have shown promise in reducing atherosclerosis in animal models . These synthetic particles are designed to mimic the structure and function of natural HDL, providing a potential therapeutic approach for cardiovascular diseases.