Atherosclerosis in aged mice over-expressing the reverse cholesterol transport genes

We determined whether over-expression of one of the three genes involved in reverse cholesterol transport, apolipoprotein (apo) AI, lecithin-cholesterol acyl transferase (LCAT) and cholesteryl ester transfer protein (CETP), or of their combinations influenced the development of diet-induced atherosclerosis. Eight genotypic groups of mice were studied (AI, LCAT, CETP, LCAT/AI, CETP/AI, LCAT/CETP, LCAT/AI/CETP, and non-transgenic) after four months on an atherogenic diet. The extent of atherosclerosis was assessed by morphometric analysis of lipid-stained areas in the aortic roots. The relative influence (R²) of genotype, sex, total cholesterol, and its main sub-fraction levels on atherosclerotic lesion size was determined by multiple linear regression analysis. Whereas apo AI (R² = 0.22, P < 0.001) and CETP (R² = 0.13, P < 0.01) expression reduced lesion size, the LCAT (R² = 0.16, P < 0.005) and LCAT/AI (R² = 0.13, P < 0.003) genotypes had the opposite effect. Logistic regression analysis revealed that the risk of developing atherosclerotic lesions greater than the 50th percentile was 4.3-fold lower for the apo AI transgenic mice than for non-transgenic mice, and was 3.0-fold lower for male than for female mice. These results show that apo AI overexpression decreased the risk of developing large atherosclerotic lesions but was not sufficient to reduce the atherogenic effect of LCAT when both transgenes were co-expressed. On the other hand, CETP expression was sufficient to eliminate the deleterious effect of LCAT and LCAT/AI overexpression. Therefore, increasing each step of the reverse cholesterol transport per se does not necessarily imply protection against atherosclerosis while CETP expression can change specific athero genic scenarios.39139

The Determination Of Total Calcium In Urine: A Comparison Between The Atomic Absorption And The Ortho-cresolphtalein Complexone Methods [análise Do Cálcio Na Urina: Uma Comparação Entre Os Métodos De Absorção Atômica E Ortocresolftaleína Complexona]

Atomic absorption spectrometry has been recommended as the reference method for the analysis of total calcium in body fluids and the ortho-cresolphtalein complexone (o-CPC) method has been widely used as the field method. We evaluated the performance of the Mega-Bayer, a fully automatic selective analyser, in determining total calcium in urine utilizing the o-CPC method. We assayed native urines with low, normal and high calcium concentrations. The two methods agreed well, according to least-squares analysis and the F-test, with Mega-Bayer having the upper limit of linearity two times higher (10 mmol/L) than that of the atomic absorption. The present method achieved excellent analytical goals and sistematic errors bellow half of the allowed limit goals recommended by the Clinical Laboratory Improvements Amendments. Final Rule. Laboratory Requirements (CLIA). We concluded that o-CPC in the Mega-Bayer equipment can confidently perform the total calcium urinary analysis with the advantage of being a fully automatized biochemical procedure and of allowing a wider linear analytical range.374235238Baginski, E.S., Direct microdetermination of serum calcium (1973) Clin. Chim. Acta, 46, pp. 46-54Ashood, E.R., Final Rule. Laboratory Requirements (1999) Tietz Textbook of Clinical Chemistry. 3. Ed., pp. 322-323. , Clinical Laboratory Improvements Amendments of 1988 Burtis, C.A. SaundersConnerty, H.V., Briggs, A.R., Determination of serum calcium by means of ortho-cresolphthalein complexone (1966) Am. J. Clin. Pathol., 45, pp. 290-296Cowley, D.M., Improved linearity of calcium - Cresolphthalein complexone reaction with sodium acetate (1986) Clin. Chem., 32, pp. 894-895Dito, W.R., Microdetermination of serum calcium by parallel fast analyzer (1976) Am. J. Clin. Pathol., 65, pp. 1016-1021Endres, D.B., Rude, R.K., Mineral and bone metabolism (1999) Tietz Textbook of Clinical Chemistry. 3. Ed., pp. 1397-1400. , Burtis, C.A. & Ashood, E.R. SaundersFirst, M.R., Renal Function (1991) Clinical Chemistry: Theory, Analysis, and Correlation. 3. Ed., pp. 549-550. , Kaplan, L. & Pesce, A.JGitelman, H.J., An improved automatic procedure for the determination of calcium in biologic specimens (1967) Anal. Biochem., 18, pp. 521-531Gowans, E.M.S., Fraser, C.G., Biological variation in analyte concentrations in urine of apparently healthy men and women (1987) Clin. Chem., 33, pp. 847-850Lorentz, K., Improved determination of serum calcium with 2-cresolphthalein complexone (1982) Clin. Chim. Acta, 126, pp. 327-334Minerals and trace elements (1995) Clinical Chemistry Interpretation and Techniques. 3. Ed., p. 353. , Kaplan, A. Williams and WilkinsMoorehead, W.R., Biggs, H.G., 2-amino-2 methyl-1 propanol as the alkalizing agent in an improved continuous flow cresolphthalein complexone procedure for calcium in serum (1974) Clin. Chem., 20, pp. 1458-1460Morin, L.G., Direct colorimetric determination of serum calcium with o-cresolphthalein complexone (1974) Am. J. Clin. Pathol., 61, pp. 114-117Sarkar, B.C.R., Chauhan, U.S.P., A new method for determining micro quantities of calcium in biological materials (1967) Anal. Biochem., 20, pp. 155-166Shephard, M.D.S., Analytical goals for quantitative urine analysis: A clinical view (1981) Clin. Chem., 27, pp. 1939-1940Tietz, N.W., A model for a comprehensive measurement system in clinical chemistry (1979) Clin. Chem., 25, pp. 833-83

Production Of Xylooligosaccharides From Enzymatic Hydrolysis Of Xylan By White-rot Fungi Pieurotus

Hemicellulose consists of non-cellulosic polysaccharides, with xylans and mannans as their main examples. In nature, xylan can be first degraded to xylooligosaccharides and finally to xylose by certain microorganisms. White-rot fungi basidiomycetes Pieurotus sp. BCCB068 and Pieurotus tailandia were used to degrade oat-spelts xylan under submerged fermentation for a period of 40 days. The study obtained activities of endo-1,4-β-xylanase and β-xylosidase and determination of xylan products by degradation. The fungi reached significant levels of xylan degradation by Pieurotus sp. BCCB068 (75.1%) and P. taiiandia (73.4%), following formations of xylooligosaccharides and sugar monomers. These Pieurotus strains proved to be a feasible alternative for biotechnological processes related to degradation of hemicellulose sources.3213742Adsul, M.G., Ghule, J.E., Shaikh, H., Singh, R., Bastawde, K.B., Gokhale, D.V., Varma, A.J., Enzymatic hydrolysis of delignified bagasse polysaccharides (2005) Carbohydrate Polymers, 62 (1), pp. 6-10Bajpai, P., Microbial xylanolytic enzyme system: Properties and applications (1997) Advances in Applied Microbiology, 43 (1), pp. 141-194Burla, G., Garzillo, A.M., Luna, M., Cardelli, L., Schiesser, A., Effects of different growth conditions on enzyme production by Pleurotus ostreatus in submerged culture (1992) Bioresource Technology, 42 (2), pp. 89-94Buswell, J.A., Chang, S.T., Biomass and extracellular hydrolytic enzyme production by six mushroom species grown on soybean waste (1994) Biotechnology Letters, 16 (12), pp. 1317-1322Castanares, A., Hay, A.J., Gordon, H., Mccrae, S.I., Wood, T., D-xylan degrading enzyme system from de fungus Phanerochaete chrysosporium. Isolation and partial characterization of an Q-(4-O-methyl)-D- glucuronidase (1995) Journal of Biotechnology, 43 (3), pp. 183-194Christakopoulos, P., Nerinckx, W., Kekos, D., Macris, B., Claeyssens, M., Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F2 (1996) Journal of Biotechnology, 51 (2), pp. 181-189Collins, T., Meuwis, N.A., Stals, I., Claeyssens, M., Feller, G., Gerday, C., A novel family 8 xylanase, functional and physicochemical characterization (2002) The Journal of Biological Chemistry, 277 (2), pp. 3513-3519Cotta, M.A., Zeltwanger, R.L., Degradation and utilization of xylan by the ruminal bacteria butyrivibrio fibrisolvens and selenomonas ruminantium (1995) Applied and Environmental Microbiology, 61 (12), pp. 4396-4402Den Hann, R., Van Zyl, W.H., Enhanced xylan degradation and utilization by Pichia stipitis overproducing fungal xylanolytic enzyles (2003) Enzyme and Microbial Technology, 33 (5), pp. 620-628El-Nasser, N.H.A., Helmy, S.M., El-Gammal, A.A., Formation of enzymes by biodegradation of agricultural wastes with white rot fungi (1997) Polymer Degradation and Stability, 55 (2), pp. 249-255Furlan, S.A., Virmond, L.J., Miers, D.A., Bonatti, M., Gern, R.M.M., Jonas, R., Mushroom strains able to grow at high temperatures and low pH values (1997) World Journal of Microbiology and Biotechnology, 13 (6), pp. 689-692Garzillo, A.M.V., Di Paolo, S., Ruzzi, M., Buonocore, V., Hydrolytic properties of extracellular cellulases from pleurotus ostreatus (1994) Applied and Environmental Microbiology, 42 (3), pp. 476-481Hespell, R.B., Cotta, M., Degradation and utilization by Butyrivibrio fibrisolvens H17c of xylan with different chemicaql and physical properties (1995) Applied and Environmental Microbiology, 61 (8), pp. 3042-3050Iembo, T., Azevedo, M.O., Block Jr., C., Filho, E.X.F., Purification and partial characterization of a new β-xylosidase from Humicola grisea var (2005) Thermoidea. World Journal of Microbiology and Biotechnology, 20 (9), pp. 949-957Ingram, L.O., Aldrich, H.C., Borges, A.C., Causey, T.B., Martinez, A., Moralez, F., Enteric bacterial catalysts for fuel ethanol production (1999) Biotechnology in Progress, 15 (5), pp. 855-866Jong, S.C., Donovick, R., Antitumoral and antiviral substances from fungi (1989) Advances in Applied Microbiology, 34 (1), pp. 183-262Kall, E.E.J., Field, J.A., Joyce, T.W., Increasing ligninolytic enzyme activities in several white-rot basidiomycetes by nitrogen-sufficient media (1995) Bioresource Technology, 53 (2), pp. 133-139Lee, H., Barbosa, M.F.S., Biely, P., Latta, R.K., Schneider, H., Utilization of xylan by yeasts and its conversion to ethanol by Pichia stipitis strains (1986) Applied and Environmental Microbiology, 82 (2), pp. 324-326Milagres, A.M.F., Magalhaes, P.O., Ferraz, A., Purification and properties of a xylanase from Ceriporiopsis subvermispora cultivated on Pinus taeda (2005) FEMS Microbiology Letters, 253 (2), pp. 267-272Miller, G.L., Use of the dinitrosalicylic acid reagent for fetermination of reducing sugar (1959) Analytical Chemistry, 31 (3), pp. 426-428Pellerin, P., Gosselin, M., Lepoutre, J.P., Samain, E., Debeire, P., Enzymatic production of oligosaccharides from corncob xylan (1991) Enzyme and Microbial Technology, 13 (4), pp. 617-621Pinphanichakarn, P., Tangsakul, T., Thongnumwom, T., Talawanich, Y., Thamchaipenet, A., Purification and characterization of b-xylosidase from Streptomyces sp. CH7 and its gene sequence analysis (2004) World Journal of Microbiology & Biotechnology, 20 (5), pp. 727-733Puls, J., Orneman, A., Gottschalk, D., Wiegel, J., Xylobiose and xylooligomers Methods in Enzimology, 160 (528), p. 1998Qinnghe, C., Xiaoyu, Y., Tiangui, N., Cheng, J., Qiugang, M., The screening of culture condition and properties of xylanase by White-rot fungus Pleurotus ostreatus (2004) Process Biochemistry, 39 (11), pp. 1561-1566Reddy, G.V., Babu, R., Komaraiah, P., Roy, K.R.R.M., Kothari, I.L., Utilization of banana waste for the production of lignolytic and cellulolytic enzymes by solid substrate fermentation using two pleurotus species (2003) Process Biochemistry, 38 (10), pp. 1457-1462. , P. ostreatus and P. sajor-cajuSermanni, G.G., Annibale, A., Lena, D., Vitale, G., Di, N.S., Mattia, E., The production of exo-enzymes by Lentinus edodes and Pieurotus ostreatus and their use for upgrading corn straw (1994) Bioresource Technology, 48 (2), pp. 173-178Sethuraman, A., Akin, D.E., Eriksson, K.E.L., Plantcell-wall-degrading enzymes produced by the white- rot fungus ceriporiopsis subvermispora (1998) Biotechnology and Applied Biochemistry, 27 (1), pp. 37-47Souza-Cruz, P.B., Freer, J., Siika-Aho, M., Ferraz, A., Extraction and determination of enzymes produced by ceriporiopsis subvermispora during biopulping of Pinus taeda wood chips (2004) Enzyme and Microbial Technology, 34 (3), pp. 228-234Sun, R.C., Tomkison, J., Liang, S.F., Comparative study of hemicelluloses from rice straw by alkali and hydrogen peroxide treatments (2000) Carbohydrate Polymers, 42 (2), pp. 111-122Tan, S.S., Li, D.Y., Jiang, Z.Q., Zhu, Y.P., Shi, B., Li, L.T., Production of xylobiose from the autohydrolysis explosion liquor of corncob using Thermotoga maritima xylanase B (XynB) immobilized on nickel-chelated Eupergit C (2008) Bioresource Technology, 99 (1), pp. 200-204Techapun, C., Charoenrat, T., Watanabe, M., Sasaki, K., Poosaran, N., Optimization of thermostable and alkaline-tolerant cellulose-free xylanase production from agricultural waste by tehrmotolerant Streptomyces sp. Ab106, using the central composite experimental design (2002) Biochemical Engineering Journal, 12 (1), pp. 99-105Tenkanen, M., Siika-Aho, M., Hausalo, T., Puls, J., Viikari, L., Synergism of xylanolytic enzymes of trichoderma reesei in the degradation of acetyl-4-O- methylglucuronoxylan (1996) Biotechnology in the pulp and paper industry. Vienna: Facultas-Universitatsverlog, p. 156. , SREBOTNIK, E.MESSNER, K. (Ed.)Valaskovã, V., Baldrian, P., Estimation of bound and free fractions of lignocellulose-degrading enzymes of wood-rotting fungi Pieurotus ostreatus, trametes versicoior and pictoporus betuiinus (2006) Research in Microbiology, 157 (2), pp. 119-12

Plasma Lipases And Lipid Transfer Proteins Increase Phospholipid But Not Free Cholesterol Transfer From Lipid Emulsion To High Density Lipoproteins

Background: Plasma lipases and lipid transfer proteins are involved in the generation and speciation of high density lipoproteins. In this study we have examined the influence of plasma lipases and lipid transfer protein activities on the transfer of free cholesterol (FC) and phospholipids (PL) from lipid emulsion to human, rat and mouse lipoproteins. The effect of the lipases was verified by incubation of labeled (3H-FC, 14C-PL) triglyceride rich emulsion with human plasma (control, post-heparin and post-heparin plus lipase inhibitor), rat plasma (control and post-heparin) and by the injection of the labeled lipid emulsion into control and heparinized functionally hepatectomized rats. Results: In vitro, the lipase enriched plasma stimulated significantly the transfer of 14C-PL from emulsion to high density lipoprotein (p&lt;0.001) but did not modify the transfer of 3H-FC. In hepatectomized rats, heparin stimulation of intravascular lipolysis increased the plasma removal of 14C-PL and the amount of 14C-PL found in the low density lipoprotein density fraction but not in the high density lipoprotein density fraction. The in vitro and in vivo experiments showed that free cholesterol and phospholipids were transferred from lipid emulsion to plasma lipoproteins independently from each other. The incubation of human plasma, control and control plus monoclonal antibody anti-cholesteryl ester transfer protein (CETP), with 14C-PL emulsion showed that CETP increases 14C-PL transfer to human HDL, since its partial inhibition by the anti-CETP antibody reduced significantly the 14C-PL transfer (p&lt;0.05). However, comparing the nontransgenic (no CETP activity) with the CETP transgenic mouse plasma, no effect of CETP on the 14C-PL distribution in mice lipoproteins was observed. Conclusions: It is concluded that: 1-intravascular lipases stimulate phospholipid transfer protein mediated phospholipid transfer, but not free cholesterol, from triglyceride rich particles to human high density lipoproteins and rat low density lipoproteins and high density lipoproteins; 2-free cholesterol and phospholipids are transferred from triglyceride rich particles to plasma lipoproteins by distinct mechanisms, and 3 - CETP also contributes to phospholipid transfer activity in human plasma but not in transgenic mice plasma, a species which has high levels of the specific phospholipid transfer protein activity.219Backer, G., Bacquer, D., Konitzer, M., Epidemiological aspects of high density lipoprotein cholesterol (1998) Atherosclerosis, 137, pp. S1-S6Stein, O., Stein, Y., Atheroprotective mechanisms of HDL (1999) Atherosclerosis, 144, pp. 285-301Tall, A.R., Plasma lipid transfer proteins (1995) Annu Rev Biochem, 64, pp. 235-257Hesler, B., Tall, A.R., Swenson, T.L., Weech, P.K., Marcel, Y.L., Milne, R.W., Monoclonal antibody to the Mr 74000 cholesterol ester transfer protein neutralize all of the cholesterol ester and triglyceride transfer activities in human plasma (1988) J Biol Chem, 263, pp. 5020-5023Swenson, T.L., Brocia, R.W., Tall, A.R., Plasma cholesteryl ester transfer protein has binding sites for neutral lipids and phospholipids (1988) J Biol Chem, 263, pp. 5150-5157Lagrost, L., Athias, A., Gambert, P., Lallemant, C., Comparative study of phospholipid transfer activities mediated by cholesteryl ester transfer protein and phospholipid transfer protein (1994) J Lipid Res, 35, pp. 825-835Tato, F., Vega, G.L., Grundy, S.M., Determinants of plasma HDL-cholesterol in hypertriglyceridemic patients (1997) Arterioscler Thromb Vasc Biol, 17, pp. 56-63Tall, A.R., Forester, L.R., Bongiovanni, G.L., Facilitation of phosphatidylcholine transfer into HDL lipoproteins by an apolipoprotein in the density 1.20-1.26 g/ml fraction of plasma (1983) J Lipid Res, 24, pp. 277-289Albers, J.J., Tollefson, J.H., Chen, C.H., Steinmetz, A., Isolation and characterization of human plasma lipid transfer proteins (1984) Arteriosclerosis, 4, pp. 49-58Guyard-Dangremont, V., Desrumaux, C., Gambert, P., Lallemant, C., Lagrost, L., Phospholipid and cholesteryl ester transfer activities in plasma from 14 vertebrate species. Relation to atherogenesis susceptibility (1998) Comp Biochem Physiol Biochem Mol Biol, 120, pp. 517-525Tall, A.R., Krumholz, S., Olivecrona, T., Deckelbaum, R.J., Plasma phospholipid transfer protein enhances transfer and exchange of phospholipids between VLDL and HDL lipoproteins during lipolysis (1985) J Lipid Res, 26, pp. 842-851Nishida, H.I., Nishida, T., Phospholipid transfer protein mediates transfer of not only phosphatidylcholine but also cholesterol from phosphatidylcholine-cholesterol vesicles to high density lipoproteins (1997) J Biol Chem, 272, pp. 6959-6964Lagrost, L., Desrumaux, C., Masson, D., Deckert, V., Gambert, P., Structure and function of the plasma phospholipid transfer protein (1998) Curr Opin Lipidol, 9, pp. 203-209Albers, J.J., Tu, A.Y., Paigen, B., Chen, H., Cheung, M.C., Marcovina, S.M., Transgenic mice expressing human phospholipid transfer protein have increased HDL/non-HDL cholesterol ratio (1996) Int J Clin Lab Res, 26, pp. 262-267Foger, B., Santamarina-Fojo, S., Shamburek, R.D., Parrot, C.L., Talley, G.D., Brewer Jr., H.B., Plasma phospholipid transfer protein. Adenovirus-mediated overexpression in mice leads to decreased plasma high density lipoprotein (HDL) and enhanced hepatic uptake of phospholipids and cholesteryl esters from HDL (1997) J Biol Chem, 272, pp. 27393-27400Redgrave, T.G., Small, D.M., Quantitation of the transfer of surface phospholipid of chylomicrons to the HDL lipoprotein fraction during the catabolism of chylomicrons in the rat (1979) J Clin Invest, 64, pp. 162-171Tall, A.R., Green, P.H., Glickman, R.M., Riley, J.W., Metabolic fate of chylomicron phospholipids and apoproteins in the rat (1979) J Clin Invest, 64, pp. 977-989Tall, A.R., Blum, C.B., Forester, G.P., Nelson, C.A., Changes in the distribution and composition of plasma HDL liproteins after ingestion of fat (1982) J Biol Chem, 257, pp. 198-207Groot, H., Scheek, L.M., Effects of fat ingestion on HDL profiles in human sera (1984) J Lipid Res, 25, pp. 684-692Brunzell, J.D., Familial lipoprotein lipase deficiency and other causes of the chylomicronemia syndrome (1995) Metabolic & Molecular Bases of Inherited Disease, pp. 1913-1932. , Scriver, CR, Beaudet, AL, Sly, WS, ed, McGraw-Hill Inc, New York, 7th edBijvoet, S., Gagne, S.E., Moorjani, S., Gagne, C., Henderson, H.E., Fruchart, J.C., Dallongeville, J., Hayden, M.R., Alterations in plasma lipoproteins and apolipoproteins before the age of 40 in heterozygotes for lipoprotein lipase deficiency (1996) J Lipid Res, 37, pp. 640-650Kuusi, T., Ehnholm, C., Viikari, J., Harkonen, R., Vartiainen, E., Puska, P., Taskinen, M.-R., Postheparin plasma lipoprotein and hepatic lipase are determinants of hypo- and hyperalphalipoproteinemia (1989) J Lipid Res, 30, pp. 1117-1126Liu, S., Jirik, F.R., LeBoeuf, R.C., Henderson, H., Castellani, L.W., Lusis, A.J., Ma, Y., Kirk, E., Alteration of lipid profiles in plasma of transgenic mice expressing human lipoprotein lipase (1994) J Biol Chem, 269, pp. 11417-11424Weinstock, P.H., Bisgaier, C.L., Aalto-Setala, K., Radner, H., Ramakrishnan, R., Levak-Frank, S., Essenburg, A.D., Breslow, J.L., Severe hypertriglyceridemia, reduced high density lipoprotein, and neonatal death in lipoprotein lipase knockout mice. Mild hypertriglyceridemia with impaired very low density lipoprotein clearance in heterozygotes (1995) J Clin Invest, 96, pp. 2555-2568Applebaum-Bowden, D., Kobayashi, J., Kashyap, V.S., Brown, D.R., Berard, A., Meyn, S., Parrott, C., Santamarina-Fojo, S., Hepatic lipase gene therapy in hepatic lipase-deficient mice. Adenovirus-mediated replacement of a lipolytic enzyme to the vascular endothelium (1996) J Clin Invest, 97, pp. 799-805Gillett, M.P., Vieira, E.M., Dimenstein, R., The phospholipase activities present in preheparin mouse plasma are inhibited by antiserum to hepatic lipase (1993) Int J Biochem, 25, pp. 449-453Ha, Y.C., Barter, P.J., Differences in plasma cholesteryl ester transfer activity in sixteen vertebrate species (1982) Comp Biochem Physiol B, 71, pp. 265-269Clee, S.M., Zhang, H., Bissada, N., Miao, L., Ehrenborg, E., Benlian, P., Shen, G.X., Hayden, M.R., Relationship between lipoprotein lipase and HDL lipoprotein cholesterol in mice: Modulation by cholesteryl ester transfer protein and dietary status (1997) J Lipid Res, 38, pp. 2079-2089Oliveira, H.C.F., Hirata, M.H., Redgrave, T.G., Maranhão, R.C., Competition between chylomicrons and their remnants for plasma removal: A study with artificial emulsion models of chylomicrons (1988) Biochim Biophys Acta, 958, pp. 211-217Nakandakare, E.R., Lottenberg, S.A., Oliveira, H.C.F., Bertolami, M.C., Vasconcelos, K.S., Sperotto, G., Quintão, E.C., Simultaneous measurements of chylomicron lipolysis and remnant removal using a doubly labeled artificial lipid emulsion: Studies in normolipidemic and hyperlipidemic subjects (1994) J Lipid Res, 35, pp. 143-152Jiao, S., Cole, T.G., Kitchens, R.T., Pfleger, B., Schonfeld, G., Genetic heterogeneity of lipoproteins in inbred strains of mice: Analysis by gel-permeation chromatography (1990) Metabolism, 39, pp. 155-160Ehnholm, C., Kuusi, T., Preparation, characterization and measurement of hepatic lipase (1986) Methods Enzymol, 129, pp. 716-738Oliveira, H.C.F., Quintão, E.C., 'In vitro' cholesteryl ester bidirectional flow between high-density lipoproteins and triglyceride-rich emulsions: Effects of particle concentration and composition, cholesteryl ester transfer activity and oleic acid (1996) J Biochem Biophys Methods, 32, pp. 45-57Huff, M.W., Miller, D.B., Wolf, B.M., Connelly, P.W., Sawyez, C.G., Uptake of hypertriglyceridemic VLDL and their remnants by HepG2 cells: The role of lipoprotein lipase, hepatic triglyceride lipase, and cell surface proteoglycans (1997) J Lipid Res, 38, pp. 1318-1333Marques-Vidal, P., Jauhiainen, M., Metso, J., Ehnholm, C., Transformation of HDL2 particles by hepatic lipase and phospholipid transfer protein (1997) Atherosclerosis, 133, pp. 87-96Murdoch, S.J., Breckenridge, W.C., Effect of lipid transfer proteins on lipoprotein lipase induced transformation of VLDL and HDL (1996) Biochim Biophys Acta, 1303, pp. 222-232Murdoch, S.J., Breckenridge, W.C., Influence of lipoprotein lipase and hepatic lipase on the transformation of VLDL and HDL during lipolysis of VLDL (1995) Atherosclerosis, 118, pp. 193-212Patsch, J.R., Gotto Jr., A.M., Olivercrona, T., Eisenberg, S., Formation of HDL2-like particles during lipolysis of VLDL in vitro (1978) Proc Natl Acad Sci USA, 75, pp. 4519-4523Gillett, M.P., Costa, E.M., Owen, J.S., The phospholipase activities present in preheparin mouse plasma are inhibited by antiserum to hepatic lipase (1980) Biochim Biophys Acta, 617, pp. 237-244Peterson, J., Bengtsson-Olivecrona, G., Olivecrona, T., Mouse preheparin plasma contains high levels of hepatic lipase with low affinity for heparin (1986) Biochim Biophys Acta, 87, pp. 865-870O'Meara, N.M., Cabana, V.G., Lukens, J.R., Loharikar, B., Forte, T.M., Polonsky, K.S., Getz, G.S., Heparin-induced lipolysis in hypertriglyceridemic subjects results in the formation of atypical HDL particle (1994) J Lipid Res, 35, pp. 2178-219