Fructated apolipoprotein A-I showed severe structural modification and loss of beneficial functions in lipid-free and lipid-bound state with acceleration of atherosclerosis and senescence》.pdfVIP

Biochemical and Biophysical Research Communications 392 (2010) 295–300 Contents lists available at ScienceDirect Biochemical and Biophysical Research Communications journal homepage: www.else /locate/ybbrc Fructated apolipoprotein A-I showed severe structural modification and loss of beneficial functions in lipid-free and lipid-bound state with acceleration of atherosclerosis and senescence Ki-Hoon Park a,1, Wookju Jang a,1, Ki-Yong Kim b, Jae-Ryong Kim c, Kyung-Hyun Cho a,* a School of Biotechnology, Aging-associated Vascular Disease Research Center, Yeungnam University, Gyeongsan 712-749, Republic of Korea b Central Research Center, Green Cross Corp., Yongin 449-903, Republic of Korea c Department of Biochemistry and Molecular Biology, Aging-associated Vascular Disease Research Center, Yeungnam University, Daegu 705-717, Republic of Korea a r t i c l e i n f o a b s t r a c t Article history: Non-enzymatic glycation of serum apolipoproteins is a main feature of diabetes mellitus under hypergly- Received 19 December 2009 cemia. Advanced glycation end products are implicated in the development of aging and metabolic syn- Available online 7 January 2010 drome, including premature atherosclerosis in diabetic subjects. ApoA-I is the principal protein constituent of HDL. In this study, glycated human apoA-I (gA-I) by fructation was characterized on func- Keywords: tional and structural correlations in lipid-free and lipid-bound states. Glycation The gA-I showed more spontaneous multimeric band