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In vitro glycation of human apolipoprotein AI reduces its efficiency in lecithincholesterol acyltransferase activation》.pdf
Clinica Chimica Acta, 204 (1991) 3742 37 0 Elsevier Science Publishers B.V. All rights reserved 0009~8981/91/%03.50 CCA05153 In vitro glycation of human apolipoprotein AI reduces its efficiency in 1ecithin:cholesterol acyltransferase activation A. Gugliucci and A.J.C. Stahl Luboratoire de Biochimie. FacultC de Pharmacie. UniversitCLouis Pasteur, Nkirch (France) (Received 2 May 1991;revision received 1July 1991;accepted 25 September 1991) Key words: Lecithincholesterol-acyltransferase; Apolipoprotein A,; Glycation Introduction Non-enzymatic glycation of proteins occurs both in vitro and in vivo [l]. This reaction may produce structural, immunological and functional modifications of proteins which could contribute to the pathogenesis of the chronic complications of diabetes mellitus [l-3]. Glycation of HDL apolipoproteins has been demonstrated using an antiglucitollysine monoclonal antibody [4]. Low HDL-cholesterol levels associated with high VLDL and remnant levels is common in diabetic populations [5]. This is probably a multifactorial phenomenon in which impairment of the func- tion of both lipoprotein lipase [LPL] and 1ecithin:cholesterol acyltransferase (LCAT, EC 2.3.1.4.3) may be implicated. In fact, much of apolipoprotein At (apo-AI) is trans- fered from VLDL to HDL particles. To test the hypothesis that glycation of apo-At could reduce its ability to activate LCAT, we measured LCAT activity wit
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