Abstract
The amount of unesterified cholesterol within a mammalian cell is tightly controlled. Cells lack a mechanism to degrade cholesterol and excess accumulation of this sterol will cause cell death. The means by which the cell procures cholesterol, therefore, must be closely regulated. Importantly, however, cholesterol is also required for a multitude of critical cellular functions. Thus, it is vital that the cell maintain an ample and continuous supply of this sterol. For example, cholesterol is necessary for normal membrane structure and function; it is required for cell growth; cholesterol regulates the activities of key enzymes and membrane transport proteins; it is a precursor for vitamins, bile acids, and steroid hormones; and in liver and intestine, it is important for normal lipoprotein synthesis and secretion. This critical balancing act by the cell to have sufficient sterol to function normally but not too much to cause cholesterol excess has implications for the development of atherosclerotic heart and peripheral vascular disease, stroke, and cholelithiasis. Because cholesterol is central to these disease states and, therefore, has an important impact on the general health of a population, the regulation of cholesterol metabolism has been extensively studied.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Andersen, J. M., and Dietschy, J. M., 1976, Cholesterogenesis: Derepression in extrahepatic tissues with 4-aminopyrazolo [3,4-d] pyrimidine, Science 193:903–905.
Andersen, J. M., Turley, S. D., and Dietschy, J. M., 1982, Relative rates of sterol synthesis in the liver and various extrahepatic tissues of normal and cholesterol-fed rabbits. Relationship to plasma lipoprotein and tissue cholesterol levels, Biochim. Biophys. Acta 711:421–430.
Beg, Z. H., Stonik, J. A, and Brewer, J. B., Jr., 1987, Modulation of the enzymic activity of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase by multiple kinase systems involving reversible phosphorylation: A review, Metabolism 36:900–917.
Beil, F. U., and Grundy, S. M., 1980, Studies on plasma lipoproteins during absorption of exogenous lecithin in man, J. Lipid Res. 21:525–536.
Bennett-Clark, S., 1979, Mucosal coenzyme A-dependent cholesterol esterification after intestinal perfusion of lipids in rats, J. Biol Chem. 254:1534–1536.
Bhattacharyya, A. K., 1981, Uptake and esterification of plant sterols by rat small intestine, Am. J. Physiol. 240:G50–55.
Bloch, K., 1965, The biological synthesis of cholesterol, Science 150:19–28.
Bochenek, W. J., and Rogers J. B., 1979, Dietary regulation of 3-hydroxy-3-methylgutaryl-CoA reductase from rate intestine, Biochem. Biophys. Acta 575:57–62.
Brown, M. S., and Goldstein, J. L., 1980, Multivalent feedback regulation of HMG-CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth, J. LipidRes. 21:505–517.
Brown, M. S., and Goldstein, J. L., 1986, A receptor-mediated pathway for cholesterol homeostasis, Science 232:34–47.
Brown, M. S., and Goldstein, J. L., 1997, The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor, Cell 89:331–340.
Brown, M. S., Goldstein, J. L., and Dietschy, J. M., 1979, Active and inactive forms of 3-hydroxy-3-methylglu-taryl coenzyme A reductase in the liver of the rat, J. Biol. Chem. 254:5144–5149.
Chang, C. C. Y., Huh, H. Y., Cadigan, K. M., and Chang, T. Y., 1993, Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells, J. Biol. Chem. 268:20747–20755.
Chang, T. Y., Chang, C. C. Y., and Cheng, D., 1995, Acyl-coenzyme A:cholesterol acyltransferanse, J. Biol. Chem. 270:29532–29540.
Cheng, D., Chang, C. C. Y., Qu, X., and Chang, T. Y., 1995, Activation of acyl-coenzyme A: Cholesterol acyltransferase (ACAT) by cholesterol or by oxysterol in a cell-free system, J. Biol. Chem. 270:685–695.
Child, P., and Kuksis, A., 1983, Critical role of ring structure in the differential uptake of cholesterol and plant sterols by membrane preparations in vitro, J. Lipid Res. 24:1196–1209.
Clarke, P. R., and Hardie, D. G., 1990, Regulation of HMG-CoA reductase: Identification of the site phosphory-lated by the AMP-activated protein kinase in vitro and in intact rat liver, EMBO J. 9:2439–2446.
Corton, J. M., and Hardie, D. G., 1992, Evidence against a role for phosphorylation/dephosphorylation in the regulation of acyl-CoA:cholesterol acyltransferase, Eur. J. Biochem. 204:203–208.
Debry, P., Nash, E. A., Neklason, D. W., and Metherall, J. E., 1997, Role of multidrug resistance P-glycoproteins in cholesterol esterification. J. Biol. Chem. 272:1026–1031.
Dietschy, J. M., and Gamel, W. G., 1971, Cholesterol synthesis in the intestine of man: Regional differences and control mechanisms, J. Clin. Invest. 50:872–880.
Dietschy, J. M., and Siperstein, M. D., 1965, Cholesterol synthesis by the gastrointestinal tract: Localization and mechanisms of control. J. Clin. Invest. 44:1311–1327.
Dietschy, J. M., and Siperstein, M. D., 1967, Effect of cholesterol feeding and fasting on sterol synthesis in seventeen tissues of the rat, J. Lipid Res. 8:97–104.
Dietschy, J. M., and Wilson, J. D., 1968, Cholesterol synthesis in the squirrel monkey: Relative rates of synthesis in various tissues and mechanisms of control, J. Clin. Invest. 47:166–174.
Dietschy, J. M., Salomon, H. S., and Siperstein, M. D., 1966, Bile acid metabolism. I. Studies on the mechanisms of intestinal transport, J. Clin. Invest. 45:832–846.
Drevon, C. A., Lilljeqvist, A-C., Schreiner, B., and Norum, K. R., 1979, Influence of cholesterol/fat feeding on cholesterol esterification and morphological structures in intestinal mucosa from guinea pigs, Atherosclerosis 34:207–219.
Edwards, P. A., Lan, S.-F., Tanaka, R. D., and Fogelman, A. M., 1983, Mevalonolactone inhibits the rate of synthesis and enhances the rat of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes, J. Biol. Chem. 258:7272–7275.
Faust, J. R., Luskey, R. K., Chin, J., Goldstein, J. L., and Brown, M. S., 1982, Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by low density lipoprotein and 25-hydroxy-cholesterol in UT-1 cells, Proc. Natl. Acad. Sci. USA 79:5205–5209.
Feingold, K. R., 1989, Importance of small intestine in diabetic hypercholesterolemia, Diabetes 38:141–145.
Field, F. J., and Mathur, S. N., 1983a, β-sitosterol: Esterification by intestinal acylcoenzyme A:cholesterol acyltransferase (ACAT) and its effect on cholesterol esterification, J. Lipid Res. 24:409–417.
Field, F. J., and Mathur, S. N., 1983b, Regulation of acyl CoA: cholesterol acyltransferase by 25-hydroxycholes-terol in rabbit intestinal microsomes and absorptive cells, J. Lipid Res. 24:1049–1059.
Field, F. J., and Mathur, S. N., 1995, Intestinal lipoprotein synthesis and secretion, Prog. Lipid Res. 34:185–198.
Field, F. J., and Salome, R. G., 1982, Effect of dietary fat saturation, cholesterol and cholestyramine on acyl-CoA: cholesterol acyltransferase activity in rabbit intestinal microsomes, Biochim. Biophys. Acta 12:557–570.
Field, F. J., Erickson, S. K., Shrewsbury, M. A., and Cooper, A. D., 1982a, 3-Hydroxy-3-methylglutaryl coenzyme A reductase from rat intestine: Subcellular localization and in vitro regulation, J. Lipid Res. 23:105–113.
Field, F. J., Cooper, A. D., and Erickson, S. K., 1982b, Regulation of rabbit intestinal acyl coenzyme A-choles-terol acyltransferase in vivo and in vitro, Gastroenterol. 83:873–880.
Field, F. J., Hennig, B, and Mathur, S. N., 1984, In vitro regulation of 3-hydroxy-3-methylglutarylcoenzyme A reductase and acylcoenzyme A: cholesterol acyltransferase activities by phosphorylation-dephosphorylation in rabbit intestine, Biochim. Biophys. Acta 802: 9–16.
Field, F. J., Albright, E., and Mathur, S. N., 1986, The effect of hypothyroidism and thyroxine replacement on hepatic and intestinal HMG-CoA reductase and ACAT activities and biliary lipids in the rat, Metabolism 35:1085–1089.
Field, F. J., Albright, E., and Mathur, S. N., 1987a, Effect of dietary n-3 fatty acids on HMG-CoA reductase and ACAT activities in liver and intestine of the rabbit, J. Lipid Res. 28:50–58.
Field, F. J., Albright, E., and Mathur, S. N., 1987b, Regulation of cholesterol esterification by micellar cholesterol in Caco-2 cells, J. Lipid Res. 28:1057–1066.
Field, F. J., Shreves, T., Fujiwara, D., Murthy, S., Albright, E., and Mathur, S. N., 1991, Regulation of gene expression and synthesis and degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by micellar cholesterol in Caco-2 cells, J. Lipid Res. 32:1811–1821.
Field, F. J., Fujiwara, D., Born, E., Chappell, D. A., and Mathur, S. N., 1993, Regulation of LDL receptor expression by luminal sterol flux in Caco-2 cells, Arterioscler. Thromb. 13:729–737.
Field, F. J., Born, E., Chen, H., Murthy, S., and Mathur, S. N., 1994, Lysophosphatidylcholine increases the secretion of cholesteryl ester-poor triacylglycerol-rich lipoproteins by Caco-2 cells, Biochem. J. 304:35–42.
Field, F. J., Born, E., Chen, H., Murthy, S., and Mathur, S. N., 1995a, Esterification of plasma membrane cholesterol and triacylglycerol-rich lipoprotein secretion in CaCo-2 cells: Possible role of p-glycoprotein, J. Lipid Res. 36:1533–1543.
Field, F. J., Born, E., and Mathur, S. N., 1995b, Triacylglycerol-rich lipoprotein cholesterol is derived from the plasma membrane in Caco-2 cells, J. Lipid Res. 36:2651–2660.
Field, F. J., Born, E., and Mathur, S. N., 1997, Effect of micellar β-sitosterol on cholesterol metabolism in CaCo-2 cells, J. Lipid Res. 38:348–360.
Fong, L. G., Bonney, E, Kosek, J. C., and Cooper, A. D., 1989, Immunohistochemical localization of low density lipoprotein receptors in adrenal gland, liver, and intestine, J. Clin. Invest. 84:847–856.
Fong, L. G., Fujishima, S. E., Komaromy, M. C., Pak, Y. K., Ellsworth, J. L., and Cooper, A. D., 1995, Location and regulation of low-density lipoprotein receptors in intestinal epithelium, Am. J. Physiol. 269: G60–72.
Gavey, K. L., Trujillo, D. L., and Scallen, T. J., 1983, Evidence for phosphorylation/deposphorylation of rat liver acyl-CoA: cholesterol acyltransferase, Proc. Natl. Acad. Sci. USA 80:2171–2174.
Gebhard, R. L., and Cooper, A. D., 1978, Regulation of cholesterol synthesis in cultured canine intestinal mucosa, J. Biol. Chem. 8:2790–2796.
Gebhard, R. L., and Prigge, W. F., 1981, In vivo regulation of canine intestinal 3-hydroxy-3-methylglutaryl coenzyme A reductase by cholesterol, lipoprotein, and fatty acids, J. Lipid Res. 22:1111–1118.
Gebhard, R. L., Stone, B. G., and Prigge, W. F., 1985, 3-Hydroxy-3-methylglutaryl coenzyme A reductase activity in the human gastrointestinal tract, J. Lipid Res. 26:47–53.
Goldstein, J. L., and Brown, M. S., 1990, Regulation of the mevalonate pathway, Nature 343:425–430.
Goodman, MW., Prigge, W. F., Gebhard, R. L., 1981, Hormonal regulation of canine intestinal cholesterol synthesis, Am. J. Physiol. 240:G274–G280.
Gould, R. G., Jones, R. J., LeRoy, G. V., Wissler, R. W., and Taylor, G. B., 1969, Absorbability of β-sitosterol in humans, Metabolism 18:652–662.
Haugen, R., and Norum, K. R., 1976, Coenzyme-A-dependent esterification of cholesterol in rat intestinal mucosa, Scand. J. Gastroenterol. 11:615–621.
Heinemann, T., Kullak-Ublick G. A., Pietruck, B., and vonBergmann, K., 1991, Mechanisms of action of plant sterols on inhibition of cholesterol absorption. Comparison of sitosterol and sitostanol, Eur. J. Clin. Pharmacol 40:S59–73.
Helgerud P., Saarem, K., and Norum, K. R., 1981, Acyl-CoA: cholesterol acyl-transferase in human small intestine: Its activity and some properties of the enzymic reaction, J. Lipid Res. 22:271–277.
Herold, G., Schneider, A., Ditschuneit, H., and Stange, E. F., 1984, Cholesterol synthesis and esterification in cultured intestinal mucosa. Evidence for compartmentation, Biochim. Biophys. Acta 796:27–33.
Ho, K-J., 1975, Effect of cholesterol feeding on circadian rhythm of hepatic and intestinal cholesterol biosynthesis in hamsters, Proc. Soc. Exp. Biol. Med. 150:271–277.
Howies, P. N., Carter, C. P., and Hui, D. Y., 1996, Dietary free and esterified cholesterol absorption in cholesterol esterase (bile salt-stimulated lipase) gene-targeted mice, J. Biol. Chem. 271:7196–7202.
Hua, X., Yokoyama, C., Wu, J., Briggs, M. R., Brown, M. S., Goldstein, J. L., and Wang, X., 1993, SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element, Proc. Natl. Acad. Sci. USA 90:11603–11607.
Huang, Y., and Hui, D. Y., 1990, Metabolic fate of pancreas-derived cholesterol esterase in intestine: An in vitro study using Caco-2 cells, J. Lipid Res. 31:2029–2037.
Hughes, T. E., Sasak, W. V., Ordovas, J. M., Forte, T. M., Lamon-Fava, S., and Schaefer, E. J., 1987, A novel cell line (Caco-2) for the study of intestinal lipoprotein synthesis, J. Biol. Chem. 262:3762–3767.
Kagami, A., Fidge, N., Suzuki, N., and Nestel, P., 1984, Characteristics of the binding of high-density lipoprotein, by intact cells and membrane preparations of rat intestinal mucosa, Biochim. Biophys. Acta 795:179–190.
Kuksis, A., and Huang, T. C, 1962, Differential absorption of plant sterols in the dog, Can. J. Biochem. Physiol. 40:1493–1504.
Lange, Y., 1994, Cholesterol movement from plasma membrane to rough endoplasmic reticulum, J. Biol. Chem. 269:1–4.
Lange, Y., Strebel, F., and Steck, T. L., 1993, Role of the plasma membrane in cholesterol esterification in rat hepatoma cells, 7. Biol. Chem. 268:13838–13843.
Li, A. C, Tanaka, R. D., Callaway, K., Fogelman, A. M., and Edwards, R A., 1988, Localization of 3-hydroxy-3-methylglutaryl CoA reductase and 3-hydroxy-3-methylglutaryl CoA synthase in the rat liver and intestine is affected by cholestyramine and mevinolin, J. Lipid Res. 29:781–796.
Lindsey, C. A., and Wilson, J. D., 1965, Evidence for a contribution by the intestinal wall to the serum cholesterol of the rat, J. Lipid Res. 6:173–181.
Liscum, L., and Dahl, N. K., 1992, Intracellular cholesterol transport, J. Lipid Res. 33:1239–1253.
Meiner, V., Tarn, C., Gunn, M. D., Dong, L-M., Weisgraber, K. H., Novak, S., Myers, H. M., Erickson, S. K., and Farese R. V., Jr., 1997, Tissue expression studies on the mouse acyl-CoA: cholesterol acyltransferase gene (Acact): Findings supporting the existence of multiple cholesterol esterification enzymes in mice, J. Lipid Res. 38:1928–1933.
Meiner, V. L., Cases, S., Myers, H. M., Sande, E. R., Bellosta, S., Schambelan, M., Pitas, R. E., McGuire, J., Herz, J., and Farese, R. V., Jr., 1996, Disruption of the acyl-CoA: cholesterol acyltransferase gene in mice: Evidence suggesting multiple cholesterol esterification enzymes in mammals, Proc. Natl. Acad. Sci. USA 93:14041–14046.
Merchant, J. L., and Heller, R. A., 1977, 3-Hydroxy-3-methylglutaryl coenzyme A reductase in isolated villus and crypt cells of the rat ileum, J. Lipid Res. 18:722–732.
Muir, L. V., Born, E., Mathur, S. N., and Field, J. F., 1996, Lysophosphatidylcholine increases 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase gene expression in Caco-2 cells, Gastroenterol. 110:1068–1076.
Muroya, H., Sodhi, H. S., and Gold, R. G., 1977, Sterol synthesis in intestinal villi and crypt ceils of rats and guinea pigs, J. Lipid Res. 18:301–308.
Murthy, S., Albright, E., Mathur, S. N., and Field, F. J., 1988, Modification of Caco-2 cell membrane fatty acid composition by eicosapentaenoic acid and palmitic acid: Effect on cholesterol metabolism, J. Lipid Res. 29:773–780.
Nagy, L., and Freeman, D. A., 1990, Effect of cholesterol transport inhibitors on steroidogenesis and plasma membrane cholesterol transport in cultured MA-10 Leydig tumor cells, Endocrinology 126:2267–2276.
Nakanishi, M., Goldstein, J. L., and Brown, M. S., 1988, Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase, J. Biol. Chem. 263: 8929–8937.
Nordstrom, J. L., Rodwell, V. W., and Mitschelen, J. J., 1977, Interconversion of active and inactive forms of rat liver hydroxymethylglutaryl-CoA reductase,J. Biol. Chem. 252:8924–8934.
Norum, K. R, Lilljeqvist, A-C., and Drevon, C. A., 1977, Coenzyme-A-dependent esterification of cholesterol in intestinal mucosa from guinea-pig. Influence of diet on the enzyme activity, Scan. J. Gastroenterol. 12:281–288.
Oku, H., Ide, T., and Sugano, M., 1984, Reversible inactivation-reactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase of rat intestine, J. Lipid Res. 25:254–261.
Panini, S. R., Lehrer, G., Rogers, D. H., and Rudney, H., 1979, Distribution of 3-hydroxy-3-methylglutaryl coenzyme A reductase and alkaline phosphatase actitives in isolated ileal epithelial cells of fed, fasted, cholestyra-nine-fed, and4-aminopyrazolo [3,4-d] pyrimidine-treated rats, J. Lipid Res. 20:879–889.
Pape, M. E., Schultz, P. A., Rea, T. J., DeMattos, R. B., Kieft, K., Bisgaier, C. L., Newton, R. S., and Krause, B. R., 1995, Tissue specific changes in acyl-CoA: cholesterol acyltransferase (ACAT) mRNA levels in rabbits, J. Lipid Res. 36:823–838.
Purdy, B. H., and Field, F. J., 1984, Regulation of acylcoenzyme A: cholesterol acyltransferase and 3-hydroxy-3-methylglutaryl coenzyme A reductase activity by lipoproteins in the intestine of parabiont rats, J. Clin. Invest. 74:351–357.
Quaroni, A., and May, R. J., 1980, Establishment and characterization of intestinal epithelial cell cultures, Methods Cell. Biol. 21:403–427.
Quaroni, A., Wands, J. Trestad, R. L., and Isselbacher, K. J., 1979, Epithelioid cell cultures from rat small intestine. Characterization by morphologic and immunologic criteria,J. Cell Biol. 80:248–265.
Raul, F., Simon, P., Kendinger, M., and Haffen, K., 1977, Intestinal enzymes activities in isolated villus and crypt cells during post-natal development of the rat, Cell Tissue Res. 176:167–178.
Rogler, G., Herold G., and Stange, E. F., 1991, HDL3-retroendocytosis in cultured small intestinal crypt cells: A novel mechanism of cholesterol efflux, Biochim. Biophys. Acta 1095:30–38.
Salen, G., Ahrens, E. H., Jr., and Grundy, S. M., 1970, Metabolism of (β-sitosterol in man, J. Clin. Invest. 49:952–967.
Shakir, K. M. M., Sundaram, S. G., and Margolis, S., 1978, Lipid synthesis in isolated intestinal cells, J. Lipid Res. 19:433–442.
Shefer, S., Hauser, S. Lapar V., and Mosbach E. H., 1973, Regulatory effects of dietary sterols and bile acids on rat intestinal HMG CoA reductase, J. Lipid Res. 14:400–405.
Shimano, H., Horton, J. D., Hammer, R. E., Shimomura, I., Brown, M. S., and Goldstein, J. L., 1996, Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-la, J. Clin. Invest. 98:1575–1584.
Shimano, H., Shimomura, I., Hammer, R. E., Herz, J., Goldstein, J. L., Brown, M. S., and Horton, J. D., 1997, Elevated levels of SREBP-2 and cholesterol synthesis in livers of mice homozygous for a targeted disruption of the SREBP-1 gene, J. Clin. Invest. 100:2115–2124.
Singer, I.I., Kawka, D. W., McNally, S. E., Scott, S., Alberts, A. W., Chen, J. S., and Huff, J. W., 1987, Hydroxy-methylglutaryl-coenzyme A reductase exhibits graded distribution in normal and mevionolin-treated ileum, Arteriosclerosis 7:144–151.
Spady, D. K., and Dietschy, J. M., 1983, Sterol synthesis in vivo in 18 tissues of the squirrel monkey, guinea pig, rabbit, hamster, and rat, J. LipidRes. 24:303–315.
Spady, D. K., Bilheimer, D. W., and Dietschy, J. M., 1983, Rates of receptor-dependent and independent low density lipoprotein uptake in the hamster, Proc. Natl. Acad. Sci. USA 80:3499–3503.
Stange, E. F., and Dietschy, J. M., 1983a, Absolute rates of cholesterol synthesis in rat intestine in vitro and in vivo: A comparison of different substrates in slices and isolated cells, J. Lipid Res. 24:72–82.
Stange, E. F., and Dietschy, J. M., 1983b, Cholesterol synthesis and low density lipoprotein uptake are regulated independently in rat small intestinal epithelium, Proc. Natl. Acad. Sci. USA 80:5739–5743.
Stange, E. F., Preclik, G., Schneider, A., Seiffer, E., and Ditschuneit, H., 1981a, Hormonal regulation of 3-hydoxy-3-methylglutaryl coenzyme A reductase and alkaline phosphatase in cultured intestinal mucosa, Biochim. Biophys. Acta 678:202–206.
Stange, E.F., Alavi, M., Schneider, A., Ditschuneit, H., and Poley, J. R., 1981b, Influence of dietary cholesterol, saturated and unsaturated lipid on 3-hydroxy-3-methylglutaryl CoA reductase activity in rabbit intestine and liver, J. Lipid Res. 22:47–56.
Stange, E. F., Suckling, K. E., and Dietschy, J. M., 1983, Synthesis and coenzyme A-dependent esterification of cholesterol in rat intestinal epithelium, J. Biol. Chem. 258:12868–12875.
Suckling, K. E., and Stange, E. F., 1985, Role of acyl-CoA:cholesterol acyltransferase in cellular cholesterol metabolism, J. Lipid Res. 26:647–671.
Suckling, K. E., Stange, E. F., and Dietschy, J. M., 1983, Dual modulation of hepatic and intestinal acyl-CoA: cholesterol acyltransferase activity by (de-)phosphorylation and substrate supply in vitro, FEBS Let 151:111–116.
Suzuki, N., Fidge, N., Nestel, P., and Yin, J., 1983, Interaction of serum lipoproteins with the intestine. Evidence for specific high density lipoprotein-binding sites on isolated rat intestinal mucosal cells, J. Lipid Res. 24:253–264.
Sviridov, D. D., Safonova, I. G., Gusev, V. A., Talalaev, A. G., Tsibulsky, V. P., Ivanov, V. O., Preobrazensky, S. N., Repin, V. S., and Smirnov, V. N., 1986, Specific high affinity binding and degradation of high density lipoproteins by isolated epithelial cells of human small intestine, Metabolism 35:588–595.
Sviridov, D. D., Ehnholm C., Tenkanen H., Pavlov, M-Yu., Safonova, I. G., and Repin, V. S., 1992, Studies on the proteins involved in the interaction of high-density lipoprotein with isolated human small intestine epithelial cells, FEBS Let 303:202–204.
Swann, A., Wiley, M. H., and Siperstein, M. D., 1975, Tissue distribution of cholesterol feedback control in the guinea pig,J. Lipid Res. 16:360–366.
Sylvin, C., and Borgström, B., 1969, Absorption and lymphatic transport of cholesterol and sitosterol in the rat, J. Lipid Res. 10:179–182.
Sylvin, C., and Nordstrom, C., 1970, The site of absorption of cholesterol and sitosterol in the rat small intestine, Scand. J. Gastroenterol. 5:57–63.
Tabas, L, Rosoff, W. J., and Boykow, G. C., 1988, Acylcoenzyme A: cholesterol acyltransferase in macrophages utilizes a cellular pool of cholesterol oxidase-accessible cholesterol as substrate, J. Biol. Chem. 263:1266–1272.
Turley, S. D., and Dietschy, J. M., 1988, The metabolism and excretion of cholesterol by the liver, in: The Liver: Biology and Pathobiology, 2nd ed. (I. M. Arias, W. B. Jakoby, H. Popper, D. Schachter, and D. A. Shafritz, eds.), Raven Press, New York, pp. 617–641.
Uelmen, P. J., Oka, K., Sullivan, M., Chang, C. C. Y., Chang, T. Y., and Chan, L., 1995, Tissue-specific expression and cholesterol regulation of acylcoenzyme A:cholesterol acyltransferase (ACAT) in mice, J. Biol. Chem. 270:26192–26201.
Wang, X., Sato, R., Brown, M. S., Hua, X., and Goldstein, J. L., 1994, SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis, Cell 77:53–62.
Weiser, M. M., 1973, Intestinal epithelial cell surface membrane glycoprotein synthesis, J. Biol. Chem. 248:2536– 2541.
Yokoyama, C., Wang, X., Briggs, M. R., Admon, A., Wu, J., Hua, X., Goldstein, J. L., and Brown, M. S., 1993, SREBP-1 , a basic helix-loop-helix-leucine zipper protein that controls transcription of the LDL receptor gene, Cell 75:187–197.
Zammit, V. A., and Caldwell A. M., 1992, Direct demonstration that increased phosphorylation of 3-hydroxy-3-methylglutaryl-CoA reductase does not increase its rate of degradation in isolated rat hepatocytes, Biochem. J. 284:901–904.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2001 Springer Science+Business Media New York
About this chapter
Cite this chapter
Field, F.J. (2001). Regulation of Intestinal Cholesterol Metabolism. In: Mansbach, C.M., Tso, P., Kuksis, A. (eds) Intestinal Lipid Metabolism. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1195-3_13
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1195-3_13
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5435-2
Online ISBN: 978-1-4615-1195-3
eBook Packages: Springer Book Archive