Department of Biotechnology, School of Applied and Life Science (SALS), Uttaranchal University, Dehradun, 248007, Uttarakhand, India.
Department of Biosciences, Integral University, Lucknow, 226026, India.
Appl Biochem Biotechnol. 2023 Jul;195(7):4653-4672. doi: 10.1007/s12010-023-04330-2. Epub 2023 Jan 23.
For several strategies formulated to prevent atherosclerosis, Apolipoprotein A1 Milano (ApoA1M) remains a prime target. ApoA1M has been reported to have greater efficiency in reducing the incidence of coronary artery diseases. Furthermore, recombinant ApoA1M based mimetic peptide exhibits comparatively greater atheroprotective potential, offers a hope in reducing the burden of atherosclerosis in in vivo model system. The aim of this review is to emphasize on some of the observed ApoA1M structural and functional effects that are clinically and therapeutically meaningful that might converge on the basic role of ApoA1M in reducing the chances of glycation assisted ailments in diabetes. We also hypothesize that the nonenzymatic glycation prone arginine amino acid of ApoA1 gets replaced with cysteine residue and the rate of ApoA1 glycation may decrease due to change substitution of amino acid. Therefore, to circumvent the effect of ApoA1M glycation, the related mechanism should be explored at the cellular and functional levels, especially in respective experimental disease model in vivo.
针对几种预防动脉粥样硬化的策略，载脂蛋白 A1 米兰（ApoA1M）仍然是主要目标。据报道，ApoA1M 在降低冠心病发病率方面更有效。此外，基于重组 ApoA1M 的模拟肽表现出相对更大的抗动脉粥样硬化潜力，为减轻体内模型系统中动脉粥样硬化的负担带来了希望。本综述的目的是强调一些观察到的 ApoA1M 结构和功能效应，这些效应在临床上和治疗上具有意义，可能与 ApoA1M 在降低糖尿病中糖化辅助疾病风险的基本作用有关。我们还假设 ApoA1 中易发生非酶糖化的精氨酸氨基酸被半胱氨酸残基取代，并且由于氨基酸取代，ApoA1 的糖化速率可能降低。因此，为了避免 ApoA1M 糖化的影响，应在细胞和功能水平上探索相关机制，特别是在相应的体内实验疾病模型中。
