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Development of Glycated ApoA-I Model to Screen Therapeutic Agents to Treat Diabetes, Atherosclerosis, Metabolic Syndrome, and Aging_Yeongnam Univ.
Korea Health Industry Development Institute (KHIDI) South Korea flag South Korea
Abstract ID:
Development of glycated apoA-I model to screen therapeutic agents to treat diabetes, atherosclerosis, metabolic syndrome, and aging...
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Nonenzymatic glycation of serum apolipoproteins is a main feature of diabetes mellitus under hyperglycemia.  Advanced glycation end products are implicated in the development of aging and metabolic syndrome, including premature atherosclerosis in diabetic subjects. ApoA-I is the principal protein constituent of high-density lipoprotein (HDL).


 In this study, glycated human apoA-I (gA-I) by fructation was characterized on functional and structural correlations in lipid-free and lipid-bound states. The gA-I showed more spontaneous multimeric band formation up to pentamer and exhibited slower elution profile with more degraded fragments from fast protein liquid chromatography.  The gA-I showed modified secondary structure from fluorescence and circular dichroism analysis.  Reconstituted HDL (rHDL) containing the gA-I had less content of phospholipid with a much smaller particle size than those of rHDL containing nA-I (nA-I-rHDL). The rHDL containing gA-I (gA-I-rHDL) consisted of less molecular number of apoA-I than nA-I-rHDL with decreased alpha-helical content.  Treatment of the gA-I-rHDL induced more atherogenic process in macrophage cell and premature senescence in human dermal fibroblast cell.


Conclusively, fructose-mediated apoA-I glycation resulted in severe loss of several beneficial functions of apoA-I and HDL regarding anti-senescence and anti-atherosclerosis activities due to a lack of anti-oxidant activity with increased susceptibility of protein degradation and structural modification.

FEATURED
Last Updated Jun 2016
Technology Type THERAPEUTIC
Phase of Development EARLY STAGE
GOVERNMENT INSTITUTE