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E Reaven

Publications and source records attributed to E Reaven.

18 recordsLinked to original sources
PubMed1992

Reconstitution of the lipoprotein cholesteryl ester transfer process using isolated rat ovary plasma membranes.

Steroidogenic cells are able to utilize lipoprotein-derived cholesteryl esters for steroidogenesis without internalizing intact lipoproteins. In the current report, we provide evidence that an early step in this process may be the selective extraction of cholesteryl esters at the cell (plasma membrane) surface. We have used a highly purified plasma membrane preparation from rat luteinized ovaries for incubation with rat- and human-derived high density (HDL) and low density (LDL) lipoproteins. The lipoproteins were modified with residualizing [125I]apoprotein or [3H]cholesteryl ester markers. Following trypsin treatment to remove intact surface-bound apoprotein particles, the membranes were analyzed for transferred radioactive labels. The results show that all the lipoproteins tested could serve as cholesteryl ester donors. Although far more [3H]cholesteryl ester than [125I]apoprotein radioactivity was transferred to plasma membranes in each case, and varied with the ligand used, the total (net) mass of cholesteryl ester transferred was comparable with the different lipoproteins. These data were confirmed using direct chemical methodology. Transfer was found to be specific for cholesteryl esters or ethers and did not involve other lipoprotein core lipids tested. Endomembranes from the same tissue could not substitute for plasma membranes as the primary cholesteryl ester acceptor. These results provide evidence that a reconstituted lipoprotein-plasma membrane system can simulate the cholesteryl ester extraction process described in situ and suggest uses for this methodology in future experiments designed to understand the transfer process.

Animals↗
PubMed1991

Okadaic acid interferes with lipoprotein-supported corticosterone production in adrenal cells.

Rat adrenocortical cells in culture respond to stimulation by ACTH alone (15 fold over basal) and to ACTH + added lipoproteins (as an exogeneous source of cholesterol), with an additional 25-30 fold rise in steroidogenesis. With the addition of okadaic acid (OKA, 100 nM), a potent protein phosphatase inhibitor, the lipoprotein-induced rise in steroidogenesis is blocked. If 20 alpha-hydroxycholesterol is provided instead of lipoprotein-cholesterol, OKA has no effect suggesting that OKA affects only actively transported cholesterol. Since the OKA block is preceded by specific morphological changes in the cell (i.e., the loss of Golgi-associated microtubules followed by the disruption of the Golgi apparatus itself), it is hypothesized that some OKA-sensitive phosphoprotein associated with the microtubule/Golgi network of adrenocortical cells is critical for lipoprotein-derived cholesterol uptake and/or transport during steroidogenesis.

Adrenal Cortex↗
PubMed1990

Uptake and utilization of lipoprotein cholesteryl esters by rat granulosa cells.

Earlier studies have shown that rat granulosa cells grown in serum-free medium are exquisitely responsive to exogenously provided lipoprotein cholesterol. In this study we compare the amount of cholesterol (cholesteryl ester) actually delivered from various homologous and heterologous cholesterol-rich lipoproteins and examine the intracellular pathways used in the delivery system. Granulosa cells were incubated for 5 or 24 h with 125I-labeled human (h) HDL3, rat (r) HDL or hLDL equipped with non-releasable apoprotein and cholesteryl ether tags which accumulate within cells, even after degradation. We show that all the tested lipoproteins were similarly efficient in cholesteryl ester delivery; i.e., based on cholesterol: protein ratios of the starting ligands, each delivered approximately the same cholesteryl ester mass and evoked a similar progestin response. However, each lipoprotein was processed quite differently by the granulosa cells: hHDL3-cholesteryl ester was taken up almost exclusively by an non-endocytic pathway, hLDL-cholesteryl ester almost exclusively by an endocytic pathway and rHDL-cholesteryl ester by both pathways. In general, there was no correlation between the total amount of lipoprotein bound or apoprotein internalized and/or degraded by the cells with the amount of cholesteryl ester received or the level of the progestin response. Hormone stimulation upregulated the preferred pathway for each lipoprotein.

Animals↗
PubMed1990

Interaction of lipoproteins with isolated ovary plasma membranes.

Plasma membranes of ovarian luteal and adrenal cortical cells from "microvillar channels," a unique extracellular compartment formed by the close apposition of flattened microvillar surfaces. Microvillar channels have unusual affinity for cholesterol-rich lipoproteins, and, in vivo, may provide an increased surface area for these particles. In this research, we have isolated a plasma membrane-enriched fraction from rat luteinized ovaries, in which closely apposed membrane (i.e. microvillar channels) comprise about 30% of the preparation. Following in vitro incubations (approximately 1 h) of this plasma membrane fraction with different plasma lipoproteins, the closely apposed plasma membrane surfaces widen and become filled with lipoprotein particles (up to about 30 nm), whereas other membranes of the fraction show little binding. Competition experiments show that rat high density lipoproteins have the highest affinity for binding to the plasma membrane fraction. Radiolabeled plasma lipoprotein and the tissue-specific hormone, human chorionic gonadotropin, showed specific and saturable binding to the plasma membrane fraction, whereas other macromolecules used as controls did not. Radioautographic analyses of 125I-labeled lipoproteins and human chorionic gonadotropin indicate that binding occurs predominantly to the closely apposed plasma membranes (i.e. microvillar channels of the fraction). These studies show that microvillar channels of steroid-secreting cells entrap large numbers of plasma lipoproteins, particularly high density lipoproteins particles, presumably functioning in the delivery of cholesterol to these cells.

Animals↗
PubMed1989

Differences in uptake of high-density lipoproteins by rat adrenals using in vivo vs. in situ perfusion techniques.

This study describes the effect of the delivery route of high-density lipoproteins (HDL) on the ultimate fate of the lipoprotein in the intact rat adrenal. Equal amounts of human (h)-derived affinity-purified apoE-free 125I-labeled HDL3 was given to ethinyl estradiol-treated (i.e., lipoprotein-deficient) rats either intravenously (in vivo route) or by non-recycling perfusion (in situ perfusion route). After 60-90 min, the adrenals were either excised and assessed for uptake of radioactivity, or perfusion-fixed with glutaraldehyde and prepared for autoradiograms at the electron microscope level. The results show that hHDL3 circulated in vivo binds 9-times more readily to adrenal tissues than the same quantity of ligand delivered by perfusion. Also, when the lipoprotein is administered in vivo, it is 5-times more likely to be interiorized as an intact particle by zona fasciculata (corticosterone-secreting) cells via an endocytic pathway than when delivered by perfusion. Similar differences between the in vivo and in situ routes were not seen when 125I-labeled rat HDL was the ligand delivered. Whereas the starting hHDL3 ligand was free of apoE, there was a substantial (7-fold) conversion of the HDL3 to apoE-containing HDL3 following in vivo circulation of the ligand, as shown by sodium phosphotungstate-MgCl2 precipitation or heparin-Sepharose column chromatography. These results show that the route of lipoprotein delivery to specific tissues can play a major role in determining both the binding and the processing of the ligand by the tissue in question. With hHDL3, acquisition of apoE during only 1 h of recirculation in lipoprotein-deficient rats was sufficient to totally alter the fate of the ligand in the adrenal cortex.

Adrenal Cortex↗
PubMed1989

Calcium-activated phospholipid-dependent protein kinases from rat liver: characterization of purified isoenzymic forms.

1. This report describes characteristics of the three isoenzymic forms of protein kinase C purified in our laboratory from rat liver. 2. All three C-kinases phosphorylated several histone preparations, and to a much lesser degree, other protein substrates and had similar Km values for ATP and histones. 3. Each isoenzyme demonstrated an absolute requirement for Ca2+ and negatively charged phospholipids. 4. Among various phospholipids tested, phosphatidylserine from bovine brain was most effective with approximately 220 fold stimulation over basal activity. 5. Both diolein and 12-O-tetradecanoylphorbol-13-acetate decreased the Ca2+ requirement of the isoenzymes and also directly stimulated C-II and C-III enzymes in the presence of suboptimal concentrations of Ca2+ and phosphatidylserine.

Adenosine Diphosphate↗
PubMed1989

Prevention of insulin resistance by environmental manipulation as young rats mature.

This study was initiated in an attempt to see if the insulin resistance associated with maturation in young rats could be prevented by environmental manipulation. Consequently, seven week-old rats were either housed in standard laboratory cages and fed a calorie-restricted diet or placed individually in exercise wheel cages and allowed to eat chow ad lib. A control group of rats was housed in standard laboratory cages from seven weeks to five months of age, and also allowed to eat chow ad lib. When studied at five months of age, the chow-fed rats weighed more (624 +/- 8 g) than either the calorie restricted (479 +/- 9 g) or exercise trained (485 +/- 13 g) rats. Insulin action was compared in the three groups by assessing the steady-state serum glucose (SSSG) and insulin (SSSI) concentrations achieved during a continuous intravenous infusion of glucose and exogenous insulin. The results of these studies indicated that SSSG concentration was significantly higher (P less than 0.001) in chow-fed rats than in the two experimental groups. Since SSSI concentrations were the same in all three groups, lower SSSG concentrations in calorie-restricted and exercise trained rats indicates that insulin-stimulated glucose uptake was preserved in these two groups as compared to the chow-fed population. In an attempt to understand why exercise training and calorie restriction prevented the development of insulin resistance, muscle glycogen synthase activity and muscle capillary density were compared in the three groups of five month-old rats.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1989

Microvillar channels: a unique plasma membrane compartment for concentrating lipoproteins on the surface of rat adrenal cortical cells.

Electron microscopic studies of perfused rat adrenals indicate that plasma lipoproteins become concentrated in a specialized cell surface compartment called microvillar channels. Closely associated plasma membranes of sinusoidal microvilli of zona fasciculata cells form channels that normally are filled with electron dense particles the size of high density lipoproteins (HDL). In rats made acutely deficient in plasma lipoproteins (by treatment with 4-aminopyrazolo[3,4-d]pyrimidine (4-APP) for 1 day), particles within the microvillar channels are decreased in number. When adrenal glands of these rats are perfused with media lacking plasma lipoproteins, many but not all of these HDL-like particles are washed out. However, when these adrenals are perfused with large amounts (100-500 micrograms protein/ml) of HDL, microvillar channels become packed with electron dense particles similar to those found in vivo. These microvillar channels become wider and filled with larger particles when low density lipoproteins (LDL) are perfused through the adrenals. Autoradiograms of 125I-labeled HDL-perfused adrenals show silver grains specifically associated with the cell surface microvillar channels, and confirm the notion that the particles filling the channels are exogenously delivered HDL. Physiologic data from similarly perfused adrenals in a parallel study show that the channel-refilling process is directly related to selective (i.e., nonendocytic) cholesterol uptake and that this cholesterol uptake is associated with corticosterone production. Together, these data suggest the hypothesis that plasma lipoprotein cholesterol utilized for corticosteroid synthesis in rat adrenal fasciculata cells may be derived from lipoproteins trapped in surface-associated microvillar channels. Although the mechanism responsible for the cholesterol transfer is not yet defined, it is clearly distinct from the classical process of receptor-mediated endocytosis and catabolism of lipoprotein particles.

Adenine↗
PubMed1989

Utilization of cholesterol-rich lipoproteins by perfused rat adrenals.

This study describes high density lipoprotein (HDL) uptake in the rat adrenal using a newly developed nonrecycling perfusion technique to control both the quality and quantity of the supplied lipoprotein. The aim of the study was to quantify a nonendocytic (alternative) pathway in the delivery of HDL-cholesterol. All experiments were conducted using an acute lipoprotein-deficient rat model (24 h 4-aminopyrazolo-[3, 4-d]-pyrimidine, 4-APP) in which circulating levels of cholesterol were reduced by one half, but various adrenal gland measurements of cholesterol metabolism were unchanged. Both rat HDL (rHDL) and affinity-purified human HDL3 (hHDL3) were used throughout the study. Microscopic autoradiographs (ARGs) indicate that both ligands bind avidly and exclusively to cells of the adrenal fasciculata and reticularis zones. Despite differences in binding affinity, both ligands deliver approximately the same total cholesterol to the cell interior as estimated by double-labeled residualizing tags on HDL (i.e., 125I-labeled dilactitol tyramine-[3H]cholesteryl linoleyl ether (DTT-CLE) HDL). The internalized cholesterol can account for much of the corticosterone produced during the 90-min time frame; however, only a small fraction of this cholesterol could have been provided via the endocytic pathway. Data obtained with the use of 125I-labeled DTT-[3H]CLE-HDL show that only 8.0% (or 0.7%) of corticosterone produced with rHDL (or hHDL3) could have come from cholesterol internalized as a component of intact HDL (i.e., via the endocytic pathway). These calculations strengthen the electron microscopy autoradiographic data that show that few exposed silver grains (representing the localization of the 125I-isotope) are found within the cell cytoplasm. Thus, despite differences in the uptake characteristics of the two ligands, most of the HDL-cholesterol internalized and used for corticosterone production during adrenal perfusion apparently comes from a pathway in which intact HDL are not internalized.

Adenine↗
PubMed1988

Cultivation of rat granulosa cells in a serum-free chemically defined medium--a useful model to study lipoprotein metabolism.

We have developed a chemically defined, serum-free medium for the culture of rat granulosa cells. This medium contains Dulbecco's modified Eagle's medium/Ham's nutrient F12 (DME:F12) (1:1) plus insulin (2 micrograms/ml), hydrocortisone (100 ng/ml), transferrin (5 micrograms/ml) and fibronectin (2 micrograms/cm2). Granulosa cells grown in this medium have an absolute requirement for added cholesterol-rich lipoproteins for steroidogenesis. When cells are cultured in basal medium, progestin production is low; when cells are cultured in the presence of follicle-stimulating hormone (FSH) or dibutyryl cAMP [Bu)2 cAMP), progestin secretion is increased 10-100-fold. Both heterologous and homologous lipoproteins synergistically increased the effects of (Bu)2 cAMP or FSH: e.g., addition to the medium of human (h)-HDL3 produced a significant increase in both basal (approx. 15-fold) and (Bu)2 cAMP-stimulated (approx. 1000-2000-fold) progestin production. LDL were less effective than HDL at equivalent concentrations of lipoprotein cholesterol. FSH invoked changes similar to that of (Bu)2 cAMP, although the magnitude of the FSH-induced change was less dramatic than that seen with (Bu)2 cAMP. The effect of h-HDL3 and h-LDL on both basal and hormone-stimulated progestin production was concentration- and time-dependent. The maximum effect of h-HDL3 was achieved at a protein concentration of 500 micrograms/ml, with an ED50 of approx. 90 micrograms/ml. In contrast, h-LDL was most effective at a concentration of 30-40 micrograms protein/ml. Likewise, rat (r-)HDL and r-LDL supported steroidogenesis in a concentration-dependent manner. Maximal responses to all additions were observed after 72 h of treatment. Granulosa cells secreted 20 alpha-hydroxypregn-4-ene-3-one as the predominant steroid in response to (Bu)2 cAMP. However, with the addition of h-HDL3, the major secreted product was progesterone. In conclusion, rat granulosa cells maintained in the described serum-free medium are exquisitely sensitive to supplied cholesterol-rich lipoproteins. When cultured in the presence of both lipoproteins and stimulatory agents, they produce from 1000-2000-times the progestins made by comparable cells maintained in medium alone. This responsiveness of the cells to both lipoprotein and hormone stimulation makes them uniquely suitable for studies involving the uptake and metabolism of lipoproteins during steroidogenesis.

Animals↗
PubMed1988

Differential secretion of proteins and glycoproteins by livers of immature and adult rats. Effect of antimicrotubule drugs.

This study was initiated to re-examine reported differences in the action of antimicrotubule agents on plasma protein secretion from livers of immature versus adult rats. The aim was (1) to determine the composition and to monitor the secretion of various plasma proteins and glycoproteins from liver slices labeled in vitro with specific amino acids and sugar residues, and (2) to correlate observed differences in secretion of these proteins with structural changes in the hepatocytes of the different aged animals. For the most part, slices of liver from fetal (term), neonatal (4- to 5 days old), and adult rats (70 days old) were incubated with radioactive amino acids or various tritiated sugars specific for N-linked core oligosaccharide and/or N-linked terminal oligosaccharide chains. Our findings indicate that liver slices of fetal and neonatal rats are efficient in synthesizing plasma proteins including fully glycosylated glycoproteins. The secretion of glycosylated and nonglycosylated proteins believed to be processed through Golgi complexes was inhibited to the same extent (approximately 70-80%) by antimicrotubule agents, regardless of the age of the host animal. However, other proteins and glycoproteins secreted by livers of immature rats were found to be relatively insensitive (i.e. inhibited to only 30-40%) to the action of various antimicrotubule drugs. The glycoproteins were found to lack N-linked terminal sugars (although the glycoproteins did contain N-linked core sugars), and it is likely that the drug-insensitive proteins bypassed critical glycosylating sites in the Golgi compartment prior to release. Overall, these findings support earlier data showing that antimicrotubule drugs have a special impact on Golgi-associated events in liver cells. To what extent these findings are related to the action of microtubules remains to be seen.

Acetylglucosaminidase↗
PubMed1988

Evidence for age-related changes in pyridine nucleotide content of isolated rat islets.

The purpose of this study was to document the effect of age on alpha-glycerophosphate activity and pyridine nucleotide concentration in pancreatic islets isolated from rats. In order to do this, islets were isolated from pancreases of 2 and 12 month-old rats, and measurements made of alpha-glycerophosphate activity and of NAD+ and NADH, determinations were made following incubation at both basal (5.6 mM) and elevated glucose concentrations (28 mM). The results indicated that islet alpha-glycerophosphate dehydrogenase activity was decreased (P less than 0.001) by approximately 50% in the older rats. This was associated with an increase in mean (+/- SEM) basal NADH content (pmol/microgram DNA) in 12 month-old (4.48 +/- 0.31) as compared to 2 month-old rats (2.73 +/- 0.49). Although mean (+/- SEM) basal NAD+ levels (pmol/microgram DNA) were the same in 2 and 12 month-old rats (29.4 +/- 2.5 and 30.8 +/- 2.8, respectively), NAD+ content following incubation at elevated levels of glucose declined (absolutely and relatively) to a significantly greater degree in the younger rats. The incremental rise in islet NADH concentration following incubation at the elevated glucose concentration was similar in the two groups, but the relative increase was only approximately half as great in islets from 12 month-old rats. These data indicate that the age-related decline in the activity of alpha-glycerophosphate dehydrogenase, the enzyme regulating the glycerophosphate shuttle system in 12 month-old rats, is associated with alterations in islet pyridine nucleotide composition.(ABSTRACT TRUNCATED AT 250 WORDS)

Aging↗
PubMed1988

Structure and function changes in rat adrenal glands during aging.

The current study examines corticosterone production in young and old rats with a view to understanding how hormone production is related to aging changes in the adrenal gland. For this purpose, we compared total (plasma volume-corrected) values for adrenocorticotropic hormone (ACTH)-induced maximal corticosterone production in young, mature (5-mo-old), and aging (18-mo-old) rats. These values were subsequently corrected for measured age-related differences in adrenal weight, adrenal cortex volume, specific adrenal zone volumes, and total number of corticosterone-producing cells in the adrenals of the differently aged rats. In addition, corticosterone disposal rates were measured in the two groups of rats, and adrenal cortical ACTH binding sites were identified by autoradiography after perfusion with 125I-labeled ACTH analogue. The results show that maximal serum ACTH-induced corticosterone concentrations (per ml serum) in the 18-mo-old rats are somewhat less than those seen in the younger animals. However, because the plasma volume is greater in the older animals (and corticosterone disposal rates do not vary), total circulating corticosterone production is, in fact, equivalent in the two groups of animals. When these total values for corticosterone are corrected for various structural changes in the adrenal gland with age, corticosterone production was found to be lower in the older group of rats: i.e., one sees an approximately 50% decline when corticosterone is expressed per adrenal weight or zonal volume and an approximately 20% decline when expressed per number of endocrine cells per adrenal.(ABSTRACT TRUNCATED AT 250 WORDS)

Adrenal Glands↗
PubMed1988

Characterization of apoB, E receptor function in the luteinized ovary.

Recent findings from this laboratory have led to the suggestion that the hormone-producing cells of the rat luteinized ovary in situ may obtain a large share of low density lipoprotein (LDL) cholesterol without actually internalizing the intact lipoprotein particles. We have shown that the lipoproteins are trapped at the surface of the luteal cells in a rich network of "microvillar channels" and have theorized that these channel membranes, with their large surface area for interacting with lipoprotein particles, may function in the cholesterol transfer process. In the current study, we try to establish what proportion of the human (h)LDL-cholesterol transfer in the in situ perfused tissue occurs by a classical apoB, E receptor-mediated process versus a surface extraction process. We examine the tissue for the presence of apoB, E receptors, and characterize the structural/functional interaction of hLDL with the apoB, E receptor utilizing a variety of modified hLDL particles as probes. Then, using nonmetabolizable radiolabels for both the protein and cholesteryl ester moieties of these LDL probes, we attempt to quantify the extent to which apoB, E receptors in the ovary contribute to the uptake of hLDL-cholesterol during steroidogenesis. Our experiments show that although the luteinized ovary contains apoB, E receptor protein, hLDL interacts with the tissue atypically. That is, despite modifications of LDL amino acid residues to prevent interaction with the apoB, E receptor, the modified ligands continue to contribute cholesterol for luteal cell internalization and/or steroidogenesis. We conclude, therefore, that in this tissue much of the LDL-cholesterol is not delivered by the apoB, E receptor pathway.

Animals↗
PubMed1987

Calcium-activated, phospholipid-dependent protein kinases from rat liver: subcellular distribution, purification, and characterization of multiple forms.

Three forms of Ca2+- and phospholipid-dependent protein kinase (protein kinase C) were extensively purified from rat liver homogenate. Subcellular fractionation analysis indicated that the majority (approximately 85%) of the activity was associated with particulate fractions of the liver. Among these, the microsomal and nuclear fractions accounted for approximately 63% and approximately 10% of total activity. The remaining 15% of protein kinase C was recovered in the soluble fraction following differential centrifugation. It was also found that most of the membrane-associated protein kinase C was latent, with 4-6-fold stimulation with detergents such as 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-1-propanesulfonate, octyl beta-glucoside, or Triton X-100. The activity of both the bound form and the soluble enzyme was enhanced by the addition of Ca2+ and phosphatidylserine, when histone H1 was used as substrate. The bound protein kinase C activity was dissociated by homogenization of liver in buffer containing ethylene glycol bis(beta-aminoethyl ether)-N,-N,N',N'-tetraacetic acid, ethylenediaminetetraacetic acid, and various proteolytic inhibitors, and the solubilized extract was used to purify multiple forms of the enzyme. The purification procedure sequentially utilized (NH4)2SO4 fractionation, ion-exchange chromatography on DEAE-cellulose, gel permeation chromatography on Fractogel TSK HW-55 (F), ion-exchange chromatography on hydroxylapatite, gel permeation chromatography on Ultrogel AcA34, and affinity chromatography on polyacrylamide-immobilized phosphatidylserine. On hydroxylapatite columns, protein kinase C activity was resolved into three isoenzymic forms designated C-I, C-II, and C-III. The molecular weights of the three isoenzymic forms were in the range of 208,000-225,000 as shown by chromatography on calibrated Ultrogel AcA34 columns and sucrose density gradient centrifugation. Furthermore, all three isoenzymes demonstrated a single peak with a sedimentation coefficient (s20.w) in the range of 9.0-9.2. However, with polyacrylamide gel electrophoresis, all the forms showed a single protein component with average molecular weight of 64K, suggesting that the native isoenzymes may be composed by subunits. Finally, all three isoenzymes exhibited nearly identical enzymatic properties.

Amino Acids↗
PubMedDate not supplied

Diabetic hypertriglyceridemia.

The conference opened with the clinical presentation of a 50-year-old male with fasting hyperglycemia (296 mg per cent) and hypertriglyceridemia (2736 mg per cent). The discussion began with a summary of current concepts regarding the manner in which chylomicra (intestine) and very low density lipoproteins (intestine and liver) are formed, transported into the plasma, and removed from the circulation. This was followed by a consideration of diabetic hypertriglyceridemia in which this syndrome was subdivided into two categories. The first form is seen in patients with severe fasting hyperglycemia, and is characterized by marked insulin deficiency, decreased very low density lipoprotein production, a fall in the activity of lipoprotein lipase, and hypertriglyceridemia secondary to a defect in removal of lipoproteins from the plasma. In contrast the other form of diabetic hypertriglyceridemia is seen in patients with minimal abnormalities of carbohydrate tolerance, and in this instance insulin resistance, not insulin lack, seems to play the pivotal role. In these patients, the rise in plasma triglyceride levels seems to be secondary to increased production of very low density lipoproteins, presumably as a result of the hyperinsulinemia associated with the insulin resistance. The conference ended with an attempt to relate the patient presented to the models of diabetic hypertriglyceridemia that had been defined.

Animals↗