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E F Stange

Publications and source records attributed to E F Stange.

At least 163 records · Page 9Linked to original sources

Cholesterol synthesis and esterification in cultured intestinal mucosa. Evidence for compartmentation.

The current studies were undertaken to define the optimal conditions for measuring the absolute rates of cholesterol synthesis in cultured rabbit intestine and to assess whether the rate of sterol synthesis affects the esterification of locally formed or absorbed cholesterol. Using both [3H]water or [14C]octanoate (3 mM) as a precursor, sterol formation was linear during the 24 h culture, resulting in comparable estimates of the rate of synthesis equivalent to 129.5 and 118.7 nmol acetyl CoA incorporated per g per h, respectively. The presence of liposomal cholesterol or the hydroxymethylglutaryl-CoA reductase inhibitor mevinolin suppressed the rates of cholesterol synthesis by 24 and 92% of controls, respectively. Only 12% of total newly synthesized cholesterol was recovered in the medium and more than 97% was in the unesterified form, in both medium and biopsy. Even when the rate of sterol synthesis was stimulated over 90-fold by increasing concentrations of [14C]mevalonolactone, less than 8% of the label in total cholesterol was found in the sterol nucleus of the esterified cholesterol. Rather, the majority of the cholesterol ester-bound radioactivity was incorporated into the fatty acid moiety. On the other hand, there was only a limited decrease in the esterification of absorbed [3H]cholesterol both when the rate of sterol synthesis was increased with 10 mM mevalonolactone and when it was inhibited with mevinolin. The data suggest that locally synthesized and absorbed cholesterol is organized in distinct functional pools with different degrees of esterification in the mucosal epithelial cell.

Animals↗

Inhibitory effects of somatostatin on growth and differentiation in cultured intestinal mucosa.

The effect of somatostatin on mucosal DNA, protein and brush border enzymes was studied in organ cultured rabbit jejunum and ileum. Compared to control cultures, somatostatin reduced the biopsy DNA and protein content in parallel in the jejunum, but was ineffective in the ileum. This was probably due to a direct growth inhibition, since DNA and brush border enzyme activity from desquamated cells in the postculture medium were unaffected. In addition, a direct inhibition of jejunal villous cell differentiation by somatostatin was reflected in a significant decrease of sucrase, maltase and alkaline phosphatase activity. In the ileum, only the specific activity of alkaline phosphatase was reduced. The key enzyme of cholesterol synthesis, HMG-CoA-reductase, was measured as an intracellular enzyme control and was not influenced by the hormone. The high somatostatin concentrations necessary to achieve the effects are not an artefact of hormone degradation during culture, as shown by radioimmunoassay, and suggest a local or "paracrine" rather than systemic, inhibitory action of somatostatin on intestinal growth and differentiation.

Animals↗

Age-related decreases in tissue sterol acquisition are mediated by changes in cholesterol synthesis and not low density lipoprotein uptake in the rat.

The present investigation compared plasma cholesterol levels and lipoprotein profiles, and absolute rates of sterol synthesis and low density lipoprotein (LDL) uptake in various organs of immature (4 weeks old) and mature (15 weeks) rats. The plasma cholesterol level and its distribution among the major lipoprotein density fractions were similar in both groups. Using [3H]water as a substrate for measuring sterol synthesis in vivo, the content of newly synthesized cholesterol (3H-labeled digitonin-precipitable sterols; [3H]DPS) was several fold higher in all tissues of the young, compared to the old, rats when normalized per g of tissue. In contrast, whole-body [3H]DPS content was identical at 29.5 and 29.3 mumol/hr in young and old rats, respectively, despite a 4.4-fold difference in body weight (102 vs. 453 g). The importance of different organs to total-body sterol synthesis remained similar with increasing age although the skin (11 vs. 24% of total) rather than the small bowel (15 vs. 8%) became the second most important organ after the liver (49 vs. 45%) in the older animals. When LDL uptake was determined in these same organs, using constant infusion technique, the rates of clearance were higher only in the adrenal glands, adipose tissue, and skin of the young animals; whereas these rates were essentially the same in the liver and gastrointestinal tract, the two organs that are quantitatively most important for LDL catabolism. Even when these clearance rates were normalized to the whole organ or to 100 g of body weight, the differences in LDL uptake in the two age groups were minor compared to the major decrease in rates of cholesterol synthesis that were observed with aging. Finally, calculation of absolute rates of tissue cholesterol acquisition from both sources indicated that, in most organs, the majority of tissue cholesterol was derived from local synthesis rather than from LDL uptake in both age groups and that, with increasing age, total cholesterol acquisition decreased several-fold primarily as a consequence of the diminished rate of sterol synthesis. These studies demonstrate that with growth and aging in the rat there is a dramatic decrease in the rate of tissue cholesterol synthesis while the uptake of LDL-cholesterol remains essentially unchanged.

Aging↗

Synthesis and coenzyme A-dependent esterification of cholesterol in rat intestinal epithelium. Differences in cellular localization and mechanisms of regulation.

The current studies were undertaken to characterize the localization and regulation of cholesterol synthesis and acyl-CoA:cholesterol acyltransferase activity in rat intestinal crypt and villus cells. Both parameters were determined in groups of animals with widely varying sterol fluxes across the intestinal mucosa. In animals on control diet the rates of cholesterol synthesis, measured by the incorporation of [3H]water per mg of protein, were similar along the villus/crypt axis in the jejunum, whereas in the ileum, villus cells were significantly more active than crypt cells. In both areas, however, the majority of total synthetic activity was found in cells from the crypts and lower villi. In contrast, the highest specific and total acyl-CoA:cholesterol acyltransferase activity was recovered in the villus cells of the jejunum and ileum. Dietary cholesterol did not affect sterol synthesis in any of the cell fractions but increased acyl-CoA:cholesterol acyltransferase activity approximately 2-fold in jejunal cell fractions. Inhibition of cholesterol absorption or sequestration of intestinal bile acids stimulated sterol synthetic activity up to 7-fold, and this occurred mainly in the lower villus and crypt cells in both jejunum and ileum. An increased demand for lipoprotein cholesterol, generated by triglyceride feeding, similarly was associated with enhanced synthetic rates. However, unlike cholesterol feeding, these manipulations did not increase acyl-CoA:cholesterol acyltransferase activity in any of the villus cell fractions. These studies suggest, therefore, that the intracellular pools of cholesterol that regulate the rate of cholesterol synthesis and the rate of cholesterol esterification are functionally distinct.

Animals↗

In vivo modulation of rat liver acyl-coenzyme A:cholesterol acyltransferase by phosphorylation and substrate supply.

Rats were infused intravenously with a bolus of mevalonolactone or cholesterol-rich chylomicron and microsomes prepared from the livers at times up to 2 h after the infusion. Acyl-CoA cholesterol acyltransferase (ACAT) activity was measured in the microsomes under conditions that define the activity state of the enzyme which recent evidence suggests may depend on the degree of phosphorylation of the enzyme. ACAT activity was increased by both treatments. Some of the observed increase could be attributed to an increase in the supply of substrate cholesterol to the enzyme. The remaining change in activity was consistent with a change in the activity state of ACAT occurring in vivo in response to the influx of cholesterol to the enzyme.

Acyltransferases↗

Dual modulation of hepatic and intestinal acyl-CoA: cholesterol acyltransferase activity by (de-)phosphorylation and substrate supply in vitro.

Acyl-CoA: cholesterol acyltransferase (ACAT) activity in microsomes from rat liver and rat intestinal epithelial cells was increased by incubation of the microsomes with the 100 000 x g supernatant fraction in the presence of ATP/MgCl2 and NaF. The measured activity was further increased by including cholesterol-rich liposomes in the preincubation. The ACAT activity in rat liver microsomes could be inhibited by preincubation in the presence of 100 000 x g supernatant and MgCl2 and microsomes preactivated by ATP/MgCl2 could also be inhibited in this way. The results suggest that ACAT activity in vitro is modulated by substrate supply and also reversibly by an ATP-dependent process which may be protein phosphorylation.

Acyltransferases↗

Emergency endoscopic sclerotherapy for bleeding esophageal varices: a prospective study in patients not responding to balloon tamponade.

To assess the efficacy of endoscopic paravariceal sclerotherapy (EPS) compared to balloon tamponade, 25 patients with massive hemorrhage from esophageal varices not responding to Sengstaken or Linton tube tamponade were treated by emergency EPS. None of the patients had received vasopressin. Immediate control of hemorrhage was achieved in 92%. Recurrent bleeding occurred in 17.4% of patients during their primary admission. Minor complications resulting from EPS were observed in three patients (12%): esophageal ulcer, esophageal stenosis, and pleural effusion. Ten patients (40%) died in the hospital, seven of them despite arrested hemorrhage. Fifteen patients were discharged and followed at 3-month intervals for a mean of 21.3 months (range, 8.8 to 29.7). During this period one death due to liver failure without recurrent hemorrhage and three rebleeding events in two patients were observed (rebleeding risk per patient month, 9.4 x 10(-3). We conclude that EPS is very effective in controlling acute bleeding from esophageal varices, even in poor risk patients with ineffective balloon tamponade.

Adult↗

Cholesterol synthesis and low density lipoprotein uptake are regulated independently in rat small intestinal epithelium.

We have compared the rates of low density lipoprotein (LDL) uptake and cholesterol synthesis in the rat intestine. By using a constant infusion technique, total and receptor-independent uptake was determined with homologous rat LDL (rLDL) and methylated human LDL (Me-hLDL), respectively. The absolute rates of sterol synthesis were measured with [1-(14) C]-octanoate and [3H]water. The rates of rLDL uptake in whole gut segments were similar along the length of the small intestine, whereas the rates of sterol synthesis varied over a 5-fold range and were highest in the duodenum and distal ileum. When the mucosal epithelium was fractionated along the villus/crypt axis, both rLDL and Me-hLDL clearance by the enterocytes increased approximately 3-fold in going from the upper villus to the crypt cell fractions, in both jejunum and ileum. In both the whole gut segments and isolated cells, approximately 60% of LDL uptake was receptor dependent. When the rates of rLDL cholesterol uptake were calculated and related to the absolute rates of sterol synthesis in the same cell fractions in vivo, both processes were found to be distributed similarly along the villus/crypt axis. Furthermore, the majority of mucosal cholesterol (64-86%) was derived from local synthesis rather than from rLDL uptake at all locations along the intestinal villus. Finally, when sterol synthesis in the epithelial cells was varied up to 7-fold by feeding cholesterol, triglyceride, cholestyramine, or surfomer, rLDL uptake was essentially unchanged. Thus, in intestinal epithelial cells in vivo, the rate of LDL uptake was constant under circumstances in which changing needs for cellular cholesterol were met by changes in the rates of sterol synthesis.

Animals↗

Absolute rates of cholesterol synthesis in rat intestine in vitro and in vivo: a comparison of different substrates in slices and isolated cells.

In an effort to localize small intestinal sterol synthesis both along the length of the intestine and along the villus-crypt axis, we defined the optimal conditions to measure absolute rates of digitonin-precipitable sterol (DPS) synthesis in whole intestinal slices and in isolated epithelial cells. When [1-(14)C]acetate and [1-(14)C]octanoate were compared in midgut slices, [1-(14)C]octanoate was preferentially metabolized to CO(2) and DPS. Because of its rapid intramitochondrial degradation, [1-(14)C]octanoate effectively swamped-out other sources of acetyl CoA (C(2)) and achieved rates of C(2) flux into DPS virtually identical to the absolute rates determined with [(3)H]water. On the other hand, unlabeled acetate decreased the apparent C(2) flux from [1-(14)C]octanoate into DPS, but not into CO(2), in a dose-dependent fashion up to 8 mM. Under comparable incubation conditions, intestinal epithelial cells isolated by the EDTA chelation technique differed from slices in several respects. First, DPS synthesis from the various substrates was proportional to time only for 30 min compared to 90 min in slices. Second, the preferred (14)C-labeled substrate for DPS and CO(2) synthesis was acetate rather than octanoate. Third, neither of the (14)C-labeled substrates achieved the rates of synthesis found with [(3)H]water. Fourth, sterol synthesis from any of the substrates was essentially zero in the absence of glucose in the incubation medium. When the optimal rates of sterol synthesis in vitro were estimated using [(3)H]water in villus and crypt cell fractions of the jejunum and ileum, all ileal fractions were more active. However, ileal villus cells exceeded the jejunal villus cells by 5.2-fold in their capacity to incorporate [(3)H]water into DPS, whereas the crypt cell fractions differed by only 1.4-fold. The majority of the sterol synthetic capacity resided in the lower villus region in both the proximal and distal intestine and the crypts accounted for about 30% and 14%, respectively, of the total found in the jejunum and ileum. A similar distribution pattern along both the vertical and horizontal axes of the intestine was found after [(3)H]water administration in vivo, although under these conditions the proportion recovered in the crypts increased to 38% and 31%, respectively, of the total [(3)H]DPS found in the jejunum and ileum. These studies demonstrate that [(3)H]water yields optimal rates of sterol synthesis both in intestinal slices and in isolated epithelial cells and is incorporated into DPS mainly in cells of the lower villus and crypt region both in vitro and in vivo.-Stange, E. F., and J. M. Dietschy. Absolute rates of cholesterol synthesis in rat intestine in vitro and in vivo: a comparison of different substrates in slices and isolated cells.

Acetates↗

Upper gastrointestinal hemorrhage from downhill esophageal varices.

Two cases of proximal esophageal varices due to a primary and a recurrent goiter are reported. One of the patients presented with massive upper gastrointestinal hemorrhage 44 years after subtotal resection of a thyroid gland. "Downhill" esophageal varices may serve as collaterals either to bypass superior vena caval obstruction via azygous vein or to drain the superior systemic system to the portal vein when both the superior vena cava and the azygous vein are occluded. They may also arise, as in our bleeding patient, from previous thyroid surgery without any symptoms of superior vena caval congestion. Therefore, downhill varices should be suspected as the origin of upper gastrointestinal hemorrhage not only in patients with obvious superior vena caval obstruction, buy also in any case of thyroid disease or a history of thyroid surgery. If conservative measures are insufficient, emergency management may include balloon tamponade or endoscopic sclerotherapy.

Aged↗

3-Hydroxy-3-methylglutaryl CoA reductase in cultured hepatocytes. Regulation by heterologous lipoproteins and hormones.

Regulation of the key enzyme of cholesterol synthesis, 3-hydroxy-3-methylglutaryl CoA reductase (EC: 1.1.1.34), by heterologous human lipoproteins and hormones was studied in a maintenance culture of rat hepatocytes. The liver cells were cultured under hormone and serum free conditions and maintained differentiated morphology and specific function. Under control conditions total HMG-CoA reductase increased by 50% after 24 h culture compared to 0 h values immediately after isolation. Thereafter a plateau of enzyme activity was reached lasting until 48 h, with a slight decline at 72 h. Concomitantly the "expressed" enzyme activity increased steadily, probably through dephosphorylation of latent reductase, the activation was largely complete at 48 h. During the steady state period of total reductase VLDL added to the medium at concentrations up to 50 microgram/ml protein had no effect o HMG-CoA reductase activity. In contrast, LDL suppressed the enzyme in a dose-dependent fashion to 40% of controls at 100 microgram/ml. On the other hand, HDL had the opposite effect with a significant induction up to 252% of controls at 50 microgram/ml. Insulin also caused a comparable dose-dependent stimulation of enzyme activity at 10(-8) and 10(-7)M, whereas glucagon inhibited reductase activity. Compared to the insulin action, triiodothyronine and triamcinolone prompted a minor, but still significant increase of reductase activity. Insulin and triamcinolone acted synergistically, but the combination of triamcinolone and tri-iodothyronine was only additive. All hormonal inductions of reductase could be blocked by cycloheximide. The present data establish that HMG-CoA reductase of maintenance cultured hepatocytes is subject to a complex regulation by heterologous lipoproteins as well as pancreatic, adrenal and thyroid hormones.

Adrenal Cortex Hormones↗

Hormonal regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase and alkaline phosphatase in cultured intestinal mucosa.

The endocrine regulation of the key enzyme of cholesterol synthesis, 3-hydroxy-3-methylglutaryl-CoA reductase (EC 1.1.1.34) and of the brush border enzyme alkaline phosphatase (EC 3.1.3.1) was studied in short (2 h) and long term (24 h) organ culture of rabbit ileum mucosa. In contrast to the hepatic enzyme, intestinal reductase is not subject to regulation by insulin or glucagon even at a pharmacological level. This applies to both 'total' and 'active' reductase, prepared in the absence or presence of sodium fluoride, respectively. During culture, there is a gradual, time-dependent increase in the active, dephosphorylated enzyme form. This endogenous activation was found to be unaffected by all hormones tested. Similarly, alkaline phosphatase was not influenced by both pancreatic hormones. In contrast, triamcinolone significantly (P less than 0.05) suppressed reductase in a dose-dependent fashion to 38% of controls after 24 h, but not after 2 h culture. Alkaline phosphatase was induced after both periods, but the effect was more marked after 24 h. A parallel minor stimulation of both enzyme activities was noted in the presence of 10(-9)M triiodothyronine (P less than 0.05), lower and very high (10(-5)M) concentrations were ineffective. In view of the role of glucocorticoids as intestinal growth inhibitors and of thyroid hormones as growth stimulators, it is suggested that changes in reductase reflect alterations of crypt membrane cholesterol synthesis, whereas the induction of alkaline phosphatase is mediated through an enhanced enterocyte regeneration and/or maturation.

Alkaline Phosphatase↗

Bile acid induced interconversion of 3-hydroxy-3-methylglutaryl Coenzyme A reductase in cultured intestine.

The effect of bile acids and bile acid/cholesterol micelles on 3-hydroxy-3-methylglutaryl coenzyme A reductase, the key enzyme of cholesterol synthesis, was investigated in cultured intestine. Glycocholic and glycodeoxycholic acid both suppressed total (fully activated) reductase activity after 3 h culture. The portion of expressed reductase, determined in the presence of NaF, was unaffected at 3 h, but decreased after 24 h of bile acid treatment. In contrast, total enzyme activity was stimulated up to 2.5-fold at 24 h; this bile acid effect was blocked by additional cholesterol. These results suggest that bile acids modulate both total reductase activity and the activation state of the enzyme in cultured intestine.

Animals↗

Regulation of 3-hydroxy-3-methylglutaryl-CoA reductase by endogenous sterol synthesis in cultured intestinal mucosa.

In vitro regulation of the key enzyme of cholesterol synthesis, 3-hydroxy-3-methylglutaryl-CoA reductase (EC 1.1.1.34) by compactin, a competitive inhibitor of the enzyme, and mevalonate was studied in rabbit ileum organ culture. Addition of compactin suppressed ileum homogenate reductase activity by over 80% at concentrations up to 0.5 microgram/ml. In contrast, compactin at the same concentrations added to the culture medium induced reductase activity up to 240% of controls. This increase was blocked by cycloheximide and mevalonolactone at 10 mM, but not by mevalonate (salt form) and cholesterol. Similarly, in contrast to ionized mevalonate, mevalonolactone significantly suppressed reductase activity of cultured intestine at 1 and 10 mM by 23 and 62%, respectively. A minor effect was also observed with preformed enzyme in fresh mucosal homogenate. When endogenous cholesterol synthesis was blocked by compactin, mucosal alkaline phosphatase activity decreased progressively, whereas medium activity from desquamated cells did not change. This distribution of the villous cell marker enzyme is characteristic of a decrease in crypt cell renewal and/or villous cell differentiation. This effect of compactin was also reversible with mevalonolactone. The reductase enzyme induced by compactin was probably latent intracellularly, since tissue cholesterol contents dropped sharply after blockade of endogenous sterol synthesis.

Alkaline Phosphatase↗

Regulation of 3-hydroxy-3-methylglutaryl CoA reductase by analogs of cholesterol and bile acids in cultured intestinal mucosa.

Sodium fusidate and its glycine conjugate, which have the same detergent properties as bile acids, significantly (p less than 0.05) stimulate HMG-CoA reductase of cultured intestine below the critical micellar concentration (CMC) without affecting brush border enzymes. Above CMC, both amphiphiles are cytotoxic. At concentrations between 1 and 5 mM, sodium fusidate decreased cholesterol contents of cultured mucosa (P less than 0.05), the increase in synthesis only partially compensating for the sterol loss. Oxygenated sterols, 7-keto- and 25-hydroxycholesterol, also depleted mucosal cholesterol at 0.5 mM, exerting their effect differently by inhibiting HMG-CoA reductase (p less than 0.01). In contrast to their marked effect on total mucosal cholesterol contents, brush border cholesterol was unaffected by both cholesterol and bile acid analogs.

Animals↗

Influence of dietary cholesterol, saturated and unsaturated lipid on 3-hydroxy-3-methylglutaryl CoA reductase activity in rabbit intestine and liver.

To characterize further the behavior of the rate-limiting enzyme of cholesterol biosynthesis in animal species, we studied the kinetic properties and the influence of dietary lipid on intestinal and hepatic HMG-CoA reductase activity in the rabbit. In intestinal crypt and villous cells isolated by a dual buffer technique, the KM value was 4.2 and 4.6 microM, respectively for DL-HMC-CoA. The specific activity of HMG-CoA reductase in the jejunum was 0.86 nmol/mg per hr, and evenly distributed between crypt and villous cells. By contrast, reductase activity was considerably lower in the ileum: in villous cells it was 0.40 nmol/mg per hr, and in crypt cells only 0.26 nmol/mg per hr. Liver microsomes had a KM value of 3.0 microM, while the reductase activity averaged 2 nmol/mg per hr. An unexpected finding was the uneven distribution of HMG-CoA reductase in the various lobes of the liver in the single animal. The addition of 1% cholesterol to the diet for 48 hours was followed by an average decline of 73% (P less than 0.005) of HMG-CoA reductase activity in villous and crypt cells of the jejunum. In the ileum, the decrease was less marked (38%, P less than 0.01). Whereas the addition of 5% corn oil to a 1% cholesterol diet did not have an additional suppressant effect on intestinal reductase, the addition of 5% coconut oil to 1% cholesterol caused further decrease of HMG-CoA reductase in jejunum and ileum (P less than 0.05). The 1% cholesterol diet resulted in a 25% decrease of hepatic reductase after 24 hours, whereas after 6 days, the enzyme activity was reduced by 90% of normal. Both 5% corn oil or 5% coconut oil, in addition to 1% cholesterol, further suppressed hepatic reductase activity. The weight of the experimental evidence presented in these studies suggests that cholesterol has a major regulatory effect on both intestinal and hepatic reductase in the rabbit.

Animals↗