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• W2184439949 abstract "Human HDL are heterogeneous in their metabo- lism and comprise small, nascent pre-PHDL and more ma- ture a-HDL. Evidence exists that pre-P,-HDL is the initial ac- ceptor of cellular free cholesterol, which then transfers sequentially to other pre-P species and then, after esterifica- tion, into a-HDL. As HDL particles are themselves trans- formed during this process, we postulated that in disorders in which HDLcholesterol is low, such as obesity, the distribution of HDL particles may be disturbed. In this study, we analyzed the HDL profile in 23 obese and 18 lean subjects, and further investigated the effects of dietary change in 15 obese subjects. HDL were separated by two-dimensional nondenaturing elec- trophoresis and the apoA-I content in each fraction was quan- tified. a,-HDL in obese subjects was significantly lower (P < 0.001) and ax-, as-, and pre-P1-HDL were significantly higher (P < 0.05 for a,HDL, P < 0.001 for a%- and pre-P,-HDL) than in lean subjects. On stepwise regression analysis, body mass index accounted for 52% (negatively) of the variance in a,- HDL and for 16% and 33% (positively) for the variances in a, and pre-P,-HDL, respectively. a,- and pre-p3-HDL in- creased significantly after low-fat, oleic acid-rich, or a-lino- lenic acid-rich diets.l The profile of a-HDL particles and also of pre-P-HDL particles therefore shifted to smaller spe- cies in obese subjects, and this was influenced by dietary fat. Increased pre-P1-HDLapoA-I in obese subjects is likely to de- rive from increased HDL catabolism but may also reflect di- minished transformation of pre-PI- to pre-P,-HDL which might reduce capacity for reverse cholesterol transport and partly explain lower HDLcholesterol levels.-Sasahara, T., T. Yamashita, D. Sviridov, N. Fidge, and P. Nestel. Altered prop- erties of high density lipoprotein subfractions in obese sub- jects. J. Zipid &. 1997. 38: 600-61 I. high density lipoprotein subfractions bolically interrelated species, the pre-(3- and a-HDL. The identification of the specific HDL subclass that might be the primary cholesterol acceptor, and the mechanism (s) responsible for regulating cellular cho- lesterol release, have been only partially answered Several studies have postulated a specific metabolic role for the pre-FHDL subfractions. Hara and Yoko- yama (7) have proposed that free apolipoproteins (A-I, A-11, and E) react with cellular cholesterol and phos- pholipid to generate small, disc-shaped pre-FHDL-like particles. These lipoprotein species had previously been demonstrated to be the initial recipients of effluxed cholesterol in short-term incubations of donor cells with human plasma (2, 4). Kawano et al. (8) demon- strated the presence of two distinct pathways of choles- terol efflux: one is directly proportional to plasma pre- 0-HDL concentration and may involve a cell-surface protein and the other is a nonspecific efflux process which is protease insensitive. Kinetic and pulse-chase in- vestigations from the laboratories of Castro and Fiel- ding (2), Francone, Gurakar, and Fielding (3), and Huang, von Eckardstein, and Assmann (5), using fibroblasts radiolabeled with cholesterol and fresh hu- man plasma, suggested that cell-derived cholesterol moved along a pathway involving three different pre-(3- HDL subclasses. The initial cholesterol acceptor, pre- P,-HDL, transferred its cholesterol, either by a transfer process or particle fusion, to a larger pre-P2-HDL, then sequentially to pre-PS-HDL, and finally to the a-HDL" @default.
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• W2184439949 date "1997-03-01" @default.
• W2184439949 modified "2023-10-15" @default.
• W2184439949 title "Altered properties of high density lipoprotein subfractions in obese subjects" @default.
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• W2184439949 doi "https://doi.org/10.1016/s0022-2275(20)37268-0" @default.
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