Digestive Diseases and Sciences

, Volume 42, Issue 3, pp 453–469

Adaptation of Intestinal Nutrient Transport in Health and Disease (Part I)

  • A.B.R. Thomson
  • G. Wild


Why is it important to understand the mechanismscontrolling intestinal adaptation? There are two majoranswers to this question. Firstly, in establishing thecellular and molecular events associated with intestinal adaptation, we will formulate ageneral framework that may be applied to theunderstanding of adaptation of other cell membranes. Forexample, alterations in the synthesis of glucosecarriers and their subsequent insertion into membranesmay alter sugar entry across the intestinal brush bordermembrane (BBM) using the sodium-dependent D-glucosetransporter, SGLT1, or the BBM sodium-independent facultative fructose transporter, GLUT5, andmay alter facilitated sugar exit across the basolateralmembrane (BLM) using GLUT2. The precise role oftranscriptional and translational processes in the up- or down-regulation of sugar transport requiresfurther definition. Alterations in enterocyte microsomallipid metabolic enzyme expression occurring during thecourse of intestinal adaptation will direct the synthesis of lipids destined fortrafficking to the BBM and BLM domains of theenterocyte. This will subsequently alter the passivepermeability properties of these membranes andultimately influence lipid absorption. Therefore, establishing thephysiological, cellular and molecular mechanisms ofadaptation in the intestine will define principles thatmay be applied to other epithelia. Secondly, enterocyte membrane adaptation is subject to dietarymodification, and these may be exploited as a means toenhance a beneficial or to reduce a detrimental aspectof the intestinal adaptive process in disease states. Alterations in membrane function occur inassociation with changes in dietary lipids, and theseare observed in a variety of cells and tissues includinglymphocytes, testes, liver, adipocytes, nerve tissue, nuclear envelope and mitochondria. Therefore,the elucidation of the mechanisms of intestinaladaptation and the manner whereby dietary manipulationmodulates these processes affords the future possibility of dietary engineering aimed at using food asa therapeutic agent. It is hoped this approach will formthe centerpiece for future investigation that wouldfocus on disease prevention, as well as on the development of better therapeutic strategies toprevent the development or to treat the complications ofconditions such as diabetes mellitus, obesity,hyperlipidemia and inflammatory bowel diseases. This review deals with the physiology of glucosetransport with specific emphasis on transporters of thebrush border membrane (BBM) and the basolateral membrane(BLM). On the BBM the sodium (Na)/glucose transporters (SGLT1 and SGLT2), the Naindependenttransporter (GLUT5), and on the BLM the hexosetransporter (GLUT2) are discussed. The molecular biologyof these transporters is also reviewed.



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  1. 1.
    Buddington RK, Diamond JM: Ontogenetic development of intestinal nutrient transporters. Annu Rev Physiol 51:601–619, 1989Google Scholar
  2. 2.
    Diamond JM: Evolutionary design of intestinal nutrient absorption; enough but not too much. News Pysiol Sci 6:92–96, 1991Google Scholar
  3. 3.
    Diamond J: Hard wired local triggering of intestinal enzyme expression. Nature 324:408, 1986Google Scholar
  4. 4.
    Diamond JM, Karasov WH: Effect of dietary carbohydrate on monosaccharide uptake by mouse small intestine in vitro. J Physiol London 349:419–440, 1984Google Scholar
  5. 5.
    Ferraris RP, Diamond JM: Crypt-villus site of glucose transporter induction by dietary carbohydrate in mouse intestine. Am J Physiol 262:G1069–G1073, 1992Google Scholar
  6. 6.
    Ferraris RP, Diamond JM: Specific regulation of the intestinal nutrient transporters by their dietary substrates. Annu Rev Physiol 51:125–141, 1989Google Scholar
  7. 7.
    Ferraris RP, Diamond JM: Use of phorizin binding to demonstrate induction of intestinal glucose transporters. J Membr Biol 94:77–82, 1986Google Scholar
  8. 8.
    Ferraris RP, Villenas SA, Diamond J: Regulation of brush-border enzyme activities and enterocytes migration rates in mouse small intestine. Am J Physiol 262:G1047–G1059, 1986Google Scholar
  9. 9.
    Karasov WH, Diamond J: Adaptation of intestinal nutrient transport. In Physiology of the Gastrointestinal Tract, Volume 2. LR Johnson (ed). New York, Raven Press, 1987Google Scholar
  10. 10.
    Karasov WH, Debnam ES: Rapid adaptation of intestinal glucose transport: A brush-border or basolateral phenomenon? Am J Physiol 53:G54–G61, 1987Google Scholar
  11. 11.
    Karasov WH, Pond RS, Solberg DH, Diamond JM: Regulation of proline and glucose transport in mouse intestine by dietary substrate levels. Proc Natl Acad Sci USA 80:7674–7677, 1983Google Scholar
  12. 12.
    Karasov WH, Solberg DH, Diamond JM: Dependence of intestinal amino acid uptake on dietary protein or amino acid levels. Am J Physiol 252(5):G614–G625, 1987Google Scholar
  13. 13.
    Thomson ABR, Dietschy JM: The role of the unstirred water layer on intestinal permeation. In Pharmacology of Intestinal Permeation. TZ Csaky (ed). Berlin, Springer-Verlag, 1984, pp 165–269Google Scholar
  14. 14.
    Thomson ABR, Keelan M, Fedorak RN, Cheeseman CI, Garg ML, Sigalet D, Linden D, Clandinin MT: Enteroplasticity. In Inflammatory Bowel Disease: Selected Topics. HJ Freeman (ed). Boca Raton, CRC Press, 1989, pp 95–140Google Scholar
  15. 15.
    Thomson ABR, Keelan M, Sigalet D, Fedorak R, Garg M, Clandinin MT: Patterns, mechanisms and signals for intestinal adaptation. Dig Dis 8:99–111, 1990Google Scholar
  16. 16.
    Thomson ABR, Cheeseman CI, Keelan M, Fedorak R, Clandinin MT: Crypt cell production rate, enterocyte turnover time and appearance of transport along the jejunal villus of the rat. Biochim Biophys Acta 1191:197–204, 1994Google Scholar
  17. 17.
    Ramage JK, Hunt RH, Perdue MH: Changes in intestinal permeability and epithelial differentiation during inflammation in the rat. Gut 29:57–61, 1988Google Scholar
  18. 18.
    Thomson CS, Debnam ES: Hyperglucagonemia: effects on active nutrient uptake by the rat jejunum. J Endocrinol 111:37–42, 1986Google Scholar
  19. 19.
    Thomson CS, Debnam ES: Starvation induced changes in the autoradiographic localization of valine uptake by rat small intestine. Experientia 42:945–948, 1986Google Scholar
  20. 20.
    Riklis E, Quastel JH: Effects of cations on sugar absorption by isolated surviving guinea pig intestine. Can J Biochem Physiol 36:347, 1958Google Scholar
  21. 21.
    Hirayama BA, Smith CD, Wright EM: Secondary structure of the Na+/glucose cotransporter. J Gen Physiol 100:19a–20, 1992Google Scholar
  22. 22.
    Veyhl M, Spangenberg J, Phschel B, Poppe R, Dekel C, Fritzsch G, Haase W, Koepsell H: Cloning of a membrane-associated protein which modifies activity and properties of the Na+/D-glucose cotransporter. J Biol Chem 268:25041–25053, 1993Google Scholar
  23. 23.
    Veyhl M, Puschel B, Spangenberg J, Dekel C, Koepsell H: Cloning of the B-subunit of the Na+-D-glucose symporter. FASEB J 6:A1459, 1992Google Scholar
  24. 24.
    Weber WM, Puschel B, Steffgen J, Koepsell H, Schwarz W: Comparison of a Na+/D-glucose cotransporter from rat intestine expressed in oocytes of Xenopus laevis with the endogenous cotransporter. Biochim Biophys Acta 1063:73–80, 1991Google Scholar
  25. 25.
    Caspary WF, Crane RK: Inclusion of L-glucose within the specificity limits of the active sugar transport system of hamster small intestine. Biochim Biophys Acta 163:395–400, 1968Google Scholar
  26. 26.
    Thomson ABR: Limitations of Michaelis-Menten kinetics in presence of intestinal unstirred layers. Am J Physiol 236:E701–E709, 1979Google Scholar
  27. 27.
    Thomson ABR: Effect of age on uptake of homologous series of unsaturated fatty acids into rabbit jejunum. Am J Physiol 239:G363–G371, 1980Google Scholar
  28. 28.
    Thomson ABR: A theoretical discussion of the use of the Lineweaver-Burke plot to estimate kinetic parameters of intestinal transport in the presence of unstirred water layers. Can J Physiol Pharm 59:932–948, 1981Google Scholar
  29. 29.
    Thomson ABR: Ileal resection and dietary content of sucrose influence the intestinal uptake of monosaccharides. Can J Physiol Pharmacol 65:2281–2286, 1987Google Scholar
  30. 30.
    Stevens BR, Fernandez A, Hirayama B, Wright EM, Kempner ES: Intestinal brush border membrane Na+/glucose cotransporter functions in situ as a homotetramet. Proc Natl Acad Sci USA 87:1456–1460, 1990Google Scholar
  31. 31.
    Takata K, Kasahara T, Kasahara M, Ezaki O, Hirano H: Immunohistochemical localization of Na+ (+)-dependent glucose transporter in rat jejunum. Cell Tissue Res 276:3–9, 1992Google Scholar
  32. 32.
    Thomson ABR, Dietschy JM: Derivation of the equations that describe the effects of unstirred water layers on the kinetic parameters of active transport processes in the intestine. J Theor Biol 64:277–294, 1977Google Scholar
  33. 33.
    Thomson ABR, Dietschy JM: Experimental demonstration of the effect of the unstirred water layer on the kinetic constants of the membrane transport of D-glucose in rabbit jejunum. J Membr Biol 54:221–229, 1980Google Scholar
  34. 34.
    Smith MW: Expression of digestive and absorptive function in differentiating enterocytes. Annu Rev Physiol 47:247–260, 1985Google Scholar
  35. 35.
    Stewart CP, Turnberg LA: Glucose depolarizes villous but not crypt cell apical membrane potential difference: A micropuncture study of crypt-villus heterogeneity in the rat. Biochim Biophys Acta 902:293–300, 1987Google Scholar
  36. 36.
    Parent L, Supplisson S, Loo DD, Wright EM: Electrogenic properties of the cloned Na+/glucose cotransporter: II. A transport model under nonrapid equilibrium conditions. J Membr Biol 125:63–79, 1992Google Scholar
  37. 37.
    Karasov WH, Diamond JM: Adaptive regulation of sugar and amino acid transport by vertebrate intestine. Am J Physiol 243:G443–G462, 1983Google Scholar
  38. 38.
    Field CJ, Ryan EA, Thomson ABR, Clandinin MT: Dietary fat and the diabetic state alter insulin binding and the fatty acid composition of adipocyte plasma membrane. Biochem J 253:417–424, 1988Google Scholar
  39. 39.
    Malo C, Berteloot A: Analysis of kinetic data in transport studies: New insights from kinetic studies of Na+-D-glucose cotransport in human intestinal brush border membrane vesicles using a fast sampling, rapid filtration apparatus. J Med Biol 122:127–141, 1991Google Scholar
  40. 40.
    Rand EB, Depaoli AM, Davidson NO, Bell GI, Burrant CF: Sequence tissue distribution and functional characterization of the rat fructose transporter GLUT5. Am J Physiol 264:1169–1176, 1993Google Scholar
  41. 41.
    Thomson ABR, Gardner MLG, Atkins GL: Alternate models for shared carriers for a single maturing carrier in hexose uptake into rabbit jejunum in vitro. Biochim Biophys Acta 903:229–240, 1987Google Scholar
  42. 42.
    Thomson ABR, Dietschy JM: Intestinal lipid absorption: Major extracellular and intracellular events. In Physiology of the Gastrointestinal Tract. LR Johnson (ed). New York, Raven Press, 1981, pp 1147–1220Google Scholar
  43. 43.
    King IS, Sepulveda FB, Smith MW: Cellular distribution of neutral and basic amino acid transport systems in rabbit ileal mucosa. J Physiol 319:355–368, 1981Google Scholar
  44. 44.
    Calamia J, Manoil C: Lac permease of Escherichia coli: Topology and sequence elements promoting membrane insertion. Proc Natl Acad Sci USA 87:4936–4941, 1990Google Scholar
  45. 45.
    Henderson PJF, Griffith JK, Martin GEM, Walmsley AR, McDonald TP, Liang WJ, Gunn FJ: Molecular analysis of “12-helix” sugar transport proteins. J Gen Physiol 100:5a, 1992Google Scholar
  46. 46.
    Maloney PC, Wilson TH: The evolution of membrane carriers. Society of General Physiologists Series 48:147–160, 1993Google Scholar
  47. 47.
    Bihler I: Intestinal sugar transport: Ionic activation and chemical specificity. Biochim Biophys Acta 183:169–181, 1962Google Scholar
  48. 48.
    Debnam ES, Ebrahim HY: Autoradiographic localization of Na+-dependent L-valine uptake by the jejunum of streptozotocin-diabetic rats. Eur J Clin Invest 20:61–65, 1990Google Scholar
  49. 49.
    Dudeja PK, Wali RK, Klitzke A, Brasitus TA: Intestinal D-glucose transport and membrane fluidity along crypt villus axis of streptozocin-induced diabetic rats. Am J Physiol 259:G571–G577, 1990Google Scholar
  50. 50.
    Fukumoto H, Seinoss, Imura H, Seino Y, Eddy RL, Fukushima Y, Byers MG, Shows TB, Bell GI: Sequence, tissue distribution and chromosomal localization of MRNA encoding a human glucose transporter-like protein. Proc Natl Acad Sci USA 85:5434–5438, 1988Google Scholar
  51. 51.
    Gould GW, Holman GD: The glucose transporter family: Structure, function and tissue specific expression. Biochem J 295:329–341, 1993Google Scholar
  52. 52.
    Gould GW, Bell GI: Facilitative glucose transporters; an expanding family. Trends Biochem Sci 15:18–23, 1990Google Scholar
  53. 53.
    Maiden MC, David EO, Baldwin SA, Moore DC, Henderson PJ: Mammalian and bacterial sugar transport proteins are homologous. Nature 325:641–643, 1987Google Scholar
  54. 54.
    Vera JC, Rosen OM: Functional expression of mammalian glucose transporters in Xenopus laevis oocytes: Evidence for cell-dependent insulin sensitivity. Mol Cell Biol 9:4187–4195, 1989Google Scholar
  55. 55.
    Burant CF, Takeda J, Brot-Laroche E, Bell GI, Davidson N: Fructose transporter in human spermatozoa and small intestine is GLUT5. J Biol Chem 267:14523–14526, 1992Google Scholar
  56. 56.
    Hediger MA, Coady MJ, Ikeda TS, Wright EM: Expression cloning and cDNA sequencing of the Na+/glucose cotransporter. Nature (London) 330:379–381, 1987Google Scholar
  57. 57.
    Hediger MA, Turk E, Wright EM: Homology of the human intestinal Na+/glucose and Escherichia coli Na+/proline cotransporters. Proc Natl Acad Sci USA 86:5748–5752, 1991Google Scholar
  58. 58.
    Hargreaves KM, Clandinin MT: Phosphatidylethanolamine methyltransferase: Evidence for influence of diet fat on selectivity of substrate for methylation in rat brain synaptic plasma membranes. Biochim Biophys Acta 918:97–105, 1987Google Scholar
  59. 59.
    Haase W, Koepsell H: Electron microscopic immunohistochemical localization of components of Na+-cotransporters along the rat nephron. Eur J Cell Biol 48:360–374, 1989Google Scholar
  60. 60.
    Haglund U, Jodal M, Lundgren O: An autoradiographic study of the intestinal absorption of palmitic and oleic acid. Acta Physiol Scand 89:306–317, 1973Google Scholar
  61. 61.
    Hediger MA, Turk E, Wright EM: Homology of the human intestinal Na+/glucose and Escherichia coli Na+/proline cotransporters. Proc Natl Acad Sci USA 86:5748–5752, 1989Google Scholar
  62. 62.
    Hediger MA, Budarf ML, Emanuel BS, Mohandas TK, Wright EM: Assignment of the human intestinal Na+/glucose cotransporter gene (SGLT1) to the q11.2-qter region of chromosome 22. Genomics 4:297–300, 1989Google Scholar
  63. 63.
    Hediger MA, Idedia T, Coady M, Gondersen CB, Wright EM: Expression of size selected mRNA encoding the intestinal Na+/glucose cotransporter in Xenopus laevis oocytes. Proc Natl Acad Sci USA 2634-2637, 1987Google Scholar
  64. 64.
    Henderson PJ, Baldwin SA, Cairns MT, Charalambous BM, Dent HC, Gunn F, Liang WJ, Lucas VA, Martin GE, McDonald TP, et al: Sugar-cation symport stytems in bacteria. Int Rev Cytol 137:149–208, 1992Google Scholar
  65. 65.
    Hirayama BA, Wong HC, Smith CD, Hagenbuch BA, Hediger MA, Wright EM: Intestinal and renal Na+/glucose cotransporters share common structures. Am J Physiol 261:C296–C304, 1991Google Scholar
  66. 66.
    Venkatraman JT, Toohey T, Clandinin MT: Does a threshold for the effect of dietary omega-3 fatty acids on the fatty acid composition of nuclear envelop phospholipids exist? Lipids 27:94–97, 1992Google Scholar
  67. 67.
    Thorens B, Cheng ZQ, Brown D, Lodish HF: Liver glucose transporter: A basolateral protein in hepatocytes and intestine and kidney cells. Am J Physiol 259:C279–C285, 1990Google Scholar
  68. 68.
    Smith CD, Hirayama BA, Wright EM: Baculovirus mediated expression of the Na+/glucose cotransporter. Biochim Biophys Acta 1104:151–159, 1992Google Scholar
  69. 69.
    Cinader B, Clandinin MT, Koh SW, Brown WR, Ramsay CA: Dietary fat alters progression of some age-related changes of the immune system. Immunol Lett 12:175–179, 1986Google Scholar
  70. 70.
    Neale RJ, Wiseman G: Active intestinal absorption of L-glucose. Nature 218:437–474, 1968Google Scholar
  71. 71.
    Smith MW: Effect of post-natal development and weaning upon the capacity of pig intestinal villi to transport alanine. J Agric Sci 102:625, 1984Google Scholar
  72. 72.
    Loo DDF, Hazam A, Supplisson S, Turk E, Wright EM: Charge translocation and associated with conformational transitions of the Na+/glucose cotransporter. J Gen Physiol 100:19a, 1992Google Scholar
  73. 73.
    Hediger MA, Mendlein J, Lee HS, Wright EM: Biosynthesis of the cloned intestinal Na+/glucose transporter. Biochim Biophys Acta 1064:360–364, 1991Google Scholar
  74. 74.
    Kessler M, Semenza G: The small-intestinal Na+ D-glucose cotransporter: An asymmetric gated channel (or pore) responsive to delta psi. J Membr Biol 76:27–56, 1983Google Scholar
  75. 75.
    Kimmich GA: Intestinal absorption of sugar. In Physiology of the Gastrointestinal Tract. LR Johnson (ed). New York, Raven Press, 1981, pp 1035–1061Google Scholar
  76. 76.
    Kennelly PJ, Krebs EG: Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 266:15555–15558, 1991Google Scholar
  77. 77.
    Koepsell HK, Korn A, Raszeja-Specht S, Bernotat-Danielowski D, Ollig D: Characterization and histochemical localization of the rat intestinal Na+-D-glucose cotransporter by monoclonal antibodies. J Biol Chem 263:18419–18429, 1988Google Scholar
  78. 78.
    Gould GW, Thomas HM, Jess TJ, Bell GI: Expression of human glucose transporters in Xenopus oocytes: Kinetic characterization and substrate specificities of the erytherocyte, liver, and brain isoforms. Biochemistry 30:5139–5145, 1991Google Scholar
  79. 79.
    Koepsell H, Madrala A: Interaction of phlorizin with the Na+-D-glucose cotransporter from intestine and kidney. Top Mol Pharmacol 4:169–202, 1987Google Scholar
  80. 80.
    Koepsell H, Seibicke S: Reconstitution of renal brush border transport proteins. Methods Enzymol 191:583–605, 1990Google Scholar
  81. 81.
    Pajor AM, Hirayama BA, Wright EM: Molecular biology approaches to comparative study of Na(+)-glucose cotransport. Am J Physiol 263:R489–R495, 1992Google Scholar
  82. 82.
    Shirazi-Beechey SP, Hirayam BA, Wang Y, Scott D, Smith MW, Wright EM: Ontogenetic development of lamb intestinal sodium-glucose cotransporter is regulated by diet. J Physiol (London) 437:699–708, 1991Google Scholar
  83. 83a.
    Shirazi-Beechey SP, Smith MW, Wang Y, James PS: Post-natal development of lamb intestinal digestive enzymes is not related by diet. J Physiol 437:691–708, 1991Google Scholar
  84. 83b.
    Freeman TC, Wood IS, Beechey RB, Dyer J, Shirazi-Beechey SP: The expression of the Na/glucose cotransporter SGLT1 gene in lamb small intestine during post-natal development. Biochim Biophys Acta 1146:203–212, 1993Google Scholar
  85. 84.
    Field CJ, Toyomizu M, Clandinin MT: Relationship between dietary fat, adipocyte membrane composition and insulin binding in the rat. J Nutr 199:1483–1489, 1989Google Scholar
  86. 85.
    Crane RF: Intestinal absorption of sugars. Physiol Rev 40:789–825, 1960Google Scholar
  87. 86.
    Davidson NO, Hausman AML, Ifkovits CA, Buse JB, Gould GW, Burant CF, Bell GI: Human intestinal glucose transporter expression and localization of GLUT5. Am J Physiol 262:C795–C800, 1992Google Scholar
  88. 87.
    Field CJ, Ryan EA, Thomson ABR, Clandinin MT: Dietary fat and the diabetic state alter insulin binding and the fatty acid composition of adipocyte plasma membrane. Biochem J 253:417–424, 1988Google Scholar
  89. 88.
    Freeman TC, Collins AJ, Heavens RP, Tivey DR: Genetic regulation of enterocyte function: A quantitative in situ hybridization study of lactose-phlorizin hydrolase and intestine. Pflugers Arch 422:570–576, 1993Google Scholar
  90. 89.
    Gurdon JB, Lane CD, Woodland HR, Marbaix G: Use of frog eggs and its translation in living cells. Nature 233:177–182, 1971Google Scholar
  91. 90.
    Sigrist-Nelson K, Hopper U: A distinct D-fructose transport system in isolated brush border membrane. Biochim Biophys Acta 367:179–184, 1974Google Scholar
  92. 91.
    Singh B, Lauzon J, Venkatraman J, Thomson ABR, Rajotte RV, Clandinin MT: Effect of high/low dietary linoleic acid levels on the function and fatty acid composition of T-lymphocytes of normal and diabetic rats. Diabetes Res 8:129–134, 1988Google Scholar
  93. 92.
    Smith MW: Autoradiographic analysis of alanine uptake by newborn pig intestine. Experientia 37:868–870, 1981Google Scholar
  94. 93.
    Smith MW: Cell biology and molecular genetics of enterocyte differentiation. Curr Top Membr 39:153, 1991Google Scholar
  95. 94.
    Morson LA, Clandinin MT: Dietary linoleic acid modulates liver plasma membrane unsaturated fatty acid composition, phosphatidylcholine and cholesterol content, as well as glucagon stimulated adenylate cyclase activity. Nutr Res 5:1113–1120, 1985Google Scholar
  96. 95.
    Paterson JY, Sepulveda FV, Smith MW: Distribution of transported amino acid within rabbit ileal mucosa. J Physiol (London) 331:523–535, 1982Google Scholar
  97. 96.
    Birk HW, Koepsell H: Reaction of monoclonal antibodies with plasma membrane proteins after binding on nitrocellulose: Renaturation of antigenic sites and reduction of nonspecific antibody binding. Anal Biochem 164:12–22, 1987Google Scholar
  98. 97.
    Neelands PJ, Clandinin MT: Diet fat influences liver plasma-membrane lipid composition and glucagon-stimulated adenylate cyclase activity. Biochem J 212:573–583, 1983Google Scholar
  99. 98.
    Kayano T, Burant CF, Fukumoto J, Gould GW, Fan YS, Eddy RL, Byers MG, Shaws TB, Bell GI: Human facilitative glucose transporters. J Biol Chem 265:B276–B282, 1990Google Scholar
  100. 99.
    Birnir B, Lee HS, Hediger MA, Wright EM: Expression and characterization of the intestinal Na+/glucose cotransporter in COS-7 cells. Biochim Biophys Acta 1048:100–104, 1990Google Scholar
  101. 100.
    Blais A, Bissonette P, Berteloot A: Common characteristics for Na+-dependent sugar transport in Caco-2 cells and human fetal colon. J Membr Biol 99:113–125, 1987Google Scholar
  102. 101.
    Lucke H, Berner W, Menge H, Murer H: Sugar transport by brush border membrane vesicles isolated from human small intestine. Pfluegers Arch 373:243–248, 1978Google Scholar
  103. 102.
    Alvarado F: Hypothesis for the interaction of phlorizin and phloretin with membrane carriers for sugars. Biochim Biophys Acta 135:483–495, 1967Google Scholar
  104. 103.
    Blais A: Expression of Na+ coupled sugar transport in HT-29 cells: Modulation by glucose. Am J Physiol 260:C1245–C1252, 1991Google Scholar
  105. 104.
    Thorens B: Facilitated glucose transporters in epithelial cells. Annu Rev Physiol 55:591–608, 1993Google Scholar
  106. 105.
    Thorens B, Sarkar HK, Kaback HR, Lodish HF: Cloning and functional expression in bacteria of a novel glucose transporter present in liver, intestine, kidney and beta-pancreatic islet cells. Cell 55:281–290, 1988Google Scholar
  107. 106.
    Barfuss DW, Schafter JA: Differences in active and passive glucose transport along the proximal nephron. Am J Physiol 241:F322–F322, 1981Google Scholar
  108. 107.
    Vera JC, Rosen OM: Reconstitution of an insulin signaling pathway in Xenopus laevis oocytes: Coexpression of a mammalian insulin receptor and their different mammalian hexose transporters. Mol Cell Biol 10:743–751, 1990Google Scholar
  109. 108.
    Freeman TC, Wood IS, Sirinathsinghji DJS, Beechey RB, Dyer J, Shirazi-Beechey SP: The expression of the Na+-glucose cotransporter (SGLT1) gene in lamb small intestine during postnatal development. Biochim Biophys Acta 1146:203–212, 1993Google Scholar
  110. 109.
    Venkatraman JT, Clandinin MT: Ribonucleic acid efflux from isolated mouse liver nuclei is altered by diet and genotypically determined change in nuclear envelope composition. Biochim Biophys Acta 940:33–42, 1988Google Scholar
  111. 110.
    Venkatraman JT, Pehowich D, Singh B, Rajotte RV, Thomson AB, Clandinin MT: Effect of dietary fat on diabetes-induced changes in liver microsonal fatty acid composition and glucose-6-phosphatase activity in rats. Lipids 26:441–444, 1991Google Scholar
  112. 111.
    Colombo VE, Semenza G: An example of mutual competition between transport inhibitors of different kinetic type: The inhibition of intestinal transport of glucalogues by phloretic and phlorizin. Biochim Biophys Acta 288:145–152, 1972Google Scholar
  113. 112.
    Amerongen HM, Mack JA, Wilson JM, Neutra MR: Membrane domains of intestinal epithelial cells: Distribution of the Na+K+-ATPase and the membrane skeleton in adult rat intestine during fetal development and after epithelial isolation. J Cell Biol 109:2129–2138, 1989Google Scholar
  114. 113.
    Riecken EO, Stallmach A, Zeitz M, Shulzke JD, Menge H, Gregor M: Growth and transformation of the small intestinal mucosa. Gut 30:1630–1640, 1989Google Scholar
  115. 114.
    Jackowski S, Alix JH: Cloning, sequence, and expression of the pantothenate permease (panF) gene of Escherichia coli. J Bacteriol 172:3842–3848, 1990Google Scholar
  116. 115.
    Brot-Laroche E, Mahraoui L, Dussaulx E, Rousset M, Zweibaum A: cAMP-dependent control of the expression of GLUT5 in Caco-2 cells. J Gen Physiol 100:72a, 1992Google Scholar
  117. 116.
    Burant CF, Sivitz WI, Fukumoto H, Kayano T, Nagamatsu S, Seino S, Pessin J, Bell GI: Mammalian glucose transporters—structure and molecular regulation. Recent Prog Horm Res 47:343–481, 1991Google Scholar
  118. 117.
    Kinter WH, Wilson TH: Autoradiographic study of sugar and amino acid absorption by everted sacs of hamster intestine. J Cell Biol 25:19–39, 1965Google Scholar
  119. 118.
    Blakely RD, Clark JA, Rudnick G, Amara SG: Vaccinia T RNA polymerase expression system: Evaluation for the expression cloning of plasma membrane transporters. Anal Biochem 194:302–308, 1991Google Scholar
  120. 119.
    Parent L, Wright EM: Functional studies of cloned Na+/glucose cotransporter. J Gen Physiol 100:9a, 1992Google Scholar
  121. 120.
    Rothman JE, Orci L: Molecular dissection of the secretory pathway. Nature 355:409–415, 1992Google Scholar
  122. 121.
    Bishop WR, Bell RM: Assembly of the endoplasmic reticulum phospholipid bilayer: The phosphatidylcholine transporter. Cell 42:51–60, 1985Google Scholar
  123. 122.
    Fantl WJ, Johnson DE, Williams LT: Signalling by receptor tyrosine kinases. Annu Rev Biochem 62:453–481, 1993Google Scholar
  124. 123.
    Massague J, Pawdiella A: Membrane anchored growth factors. Annu Rev Biochem 62:515, 1993Google Scholar
  125. 124.
    Hardie DG: Biochemical Messengers: Hormones, Neurotransmitters and Growth Factors. London, Chapman and Hall, 1990Google Scholar
  126. 125.
    Raff MC: Social control on cell survival and cell death. Nature 356:397–400, 1992Google Scholar
  127. 126.
    Schimke RT: On the roles of synthesis and degradation in regulation of enzyme levels in mammalian tissues. Curr Top Cell Regul 1:77–124, 1969Google Scholar
  128. 127.
    Andres AJ, Thummel CS: Hormones, puffs and flies—the molecular control of metamorphosis by ecdysone. Trends Genet 8:132–138, 1992Google Scholar
  129. 128.
    Parker MG (ed): Nuclear Hormone Receptors: Molecular Mechanisms, Cellular Functions and Clinical Abnormalities. London, Academic Press, 1991Google Scholar
  130. 129.
    Anonymous: Signal transduction: Crosstalk, Trends Biochem Sci 17:367–443, 1992Google Scholar
  131. 130.
    Bourne HR, Nicoll R: Molecular machines integrate coincident synaptic signals. Cell/Neuron 72(10):65–75, 1993Google Scholar
  132. 131.
    Cohen P: Signal integration at the level of protein kinases, protein phosphatases and their substrates. Trends Biochem Sci 17:408–413, 1992Google Scholar
  133. 132.
    Pelech SL: Networking with protein kinases. Curr Biol 3:513–515, 1993Google Scholar
  134. 133.
    Posada J, Cooper J: Molecular signal integration. Interplay between serine, threonine, and tyrosine phosphorylation. Mol Biol Cell 3:593–592, 1992Google Scholar
  135. 134.
    Birnbaumer L: G proteins in signal transduction. Annu Rev Pharmacol Toxicol 30:675–705, 1990Google Scholar
  136. 135.
    Houslay MD, Milligan G (eds): G-Proteins as Mediators of Cellular Signalling Processes. Chichester, Wiley, 1990Google Scholar
  137. 136.
    Linder ME, Gilman AG: G proteins. Sci Am 267(1):36–43, 1992Google Scholar
  138. 137.
    Bourne HR, Sanders DA, McCormick F: The GTPase superfamily: Conserved structure and molecular mechanism. Nature 349:117–127, 1991Google Scholar
  139. 138.
    Hepta JR, Gilman AG: G proteins. Trends Biochem Sci 17:383–387, 1992Google Scholar
  140. 139.
    Tang WJ, Gilman AG: Adenylyl cyclases. Cell 70:869–872, 1992Google Scholar
  141. 140.
    Birnbaumer L: Receptor-to-effector signalling through G proteins: Roles for beta gamma dimers as well as alpha subunits. Cell 71:1069–1072, 1992Google Scholar
  142. 141.
    Iniguez-Lluhi J, Kleuss C, Gilman AG: The importance of G-protein bg subunits. Trends Cell Biol 3:230–235, 1993Google Scholar
  143. 142.
    Brindle PK, Montminy MR: The CREB family of transcription activators. Curr Opin Gen Dev 2:199–204, 1992Google Scholar
  144. 143.
    Taylor SS, Buechler JA, Yonemoto W: cAMP-dependent protein kinase: Framework for a diverse family of regulatory enzymes. Annu Rev Biochem 59:971–1005, 1990Google Scholar
  145. 144.
    Cohen P: Structure and regulation of protein phosphatases. Annu Rev Biochem 58:453–508, 1989Google Scholar
  146. 145.
    Koch GIE: The endoplasmic reticulum and calcium storage. Bioessays 12:527–531, 1990Google Scholar
  147. 146.
    Bensal VS, Majerus PW: Phosphatidylin ositol-derived precursors and signals. Annu Rev Cell Biol 6:41–67, 1990Google Scholar
  148. 147.
    Harden TK: G-protein-regulated phospholipase C: Identification of component proteins. Adv Second Messenger Phosphoprotein Res 26:11–34, 1992Google Scholar
  149. 148.
    Margerus PW: Inositol phosphate biochemistry. Annu Rev Biochem 61:225–250, 1992Google Scholar
  150. 149.
    Mitchell TJ: Compare and contrast actin filaments and microtubules. Mol Biol Cell 3:1309–1315, 1992Google Scholar
  151. 150.
    Berridge MJ: Inositol trisphosphate and calcium signalling. Nature 361:315–325, 1993Google Scholar
  152. 151.
    Ferris CD, Snyder SH: Inositol 1,4,5-trisphosphate-activated calcium channels. Annu Rev Physiol 54:469–488, 1992Google Scholar
  153. 152.
    Meldolesi J: Multifarious IP3 receptors. Curr Biol 2:393–394, 1992Google Scholar
  154. 153.
    Taylor CW, Marshall ICB: Calcium and inositol 1,4,5-triphosphate receptors: A complex relationship. Trends Biochem Sci 17:403–407, 1992Google Scholar
  155. 154.
    Head JF: A better grip on calmodulin. Curr Biol 2:609–611, 1992Google Scholar
  156. 155.
    O'Neil KT, DeGrado WF: How calmodulin binds its targets: Sequence independent recognition of amphiphatic a-helices. Trends Biochem Sci 15:59–64, 1990Google Scholar
  157. 156.
    Hanson PI, Schulman H: Neuronal Ca2+/calmodulin-dependent protein kinases. (review). Annu Rev Biochem 61:559–601, 1992Google Scholar
  158. 157.
    Schulman G: A review of the concept of biocompatibility. Kidney Int Supplement 41:5209–5212, 1993Google Scholar
  159. 158.
    Cohen P: Protein phosphorylation and hormone action. Proc R Soc London (Biol) 234:115–144, 1988Google Scholar
  160. 159.
    Lamb TD, Pugh EN Jr: G-protein cascades: Gain and kinetics. Trends Neurosci 15:291–298, 1992Google Scholar
  161. 160.
    Mack T: Receptors of atrial natriuretic factor. Annu Rev Physiol 54:11–27, 1992Google Scholar
  162. 161.
    Yuen PST, Garbers DL: Guanylyl cyclase-linked receptors. Annu Rev Neurosci 15:193–225, 1992Google Scholar
  163. 162.
    Schlessinger J, Ullrich A: Growth factor signalling in receptor tyrosine kinases. Neuron 9:383–391, 1992Google Scholar
  164. 163.
    Ullrich A, Schlessinger J: Signal transduction by receptors with tyrosine kinase activity. Cell 61:203–212, 1990Google Scholar
  165. 164.
    Clark SG, Stern MJ, Horvitz JRC: Elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains. Nature 356:340–344, 1992Google Scholar
  166. 165.
    Koch CA, Anderson D, Moran MF, Ellis C, Pawson T: SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science 252:668–674, 1991Google Scholar
  167. 166.
    Mayer BJ, Baltimore D: Signalling through SH2 and SH3 domains. Trends Cell Biol 3:8–13, 1993Google Scholar
  168. 167.
    Pausenn T, Schlessinger J: SH2 and SH3 domains. Curr Biol 3:434–442, 1993Google Scholar
  169. 168.
    Bollag G, McCormick F: Regulators and effectors of ras proteins. Annu Rev Cell Biol 7:601–632, 1991Google Scholar
  170. 169.
    Downward J: Ras regulation: putting back the GTP. Curr Biol 2:329–331, 1992Google Scholar
  171. 170.
    Hall A: Ras-related proteins. Curr Opin Cell Biol 5:265–268, 1993Google Scholar
  172. 171.
    Lowy DR, Willumsen BM: Function and regulation of Ras. Annu Rev Biochem 62:851–891, 1993Google Scholar
  173. 172.
    Greenberg ME, Ziff EB: Stimulation of 3T3 cells induces transcription of the C-Fos proto-oncogene. Nature 311:433–438, 1984Google Scholar
  174. 173.
    Lamph WW, Wamsley P, Sassone-Corsi P, Verma IM: Induction of proto-oncogene JUN/AP-1 by serum and TPA. Nature 334:629–631, 1988Google Scholar
  175. 174.
    Rozakis-Adcock M, Fernly MR, Wade J, Pawson T, Bowtell D: The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSOSI. Nature 363:83–85, 1993Google Scholar
  176. 175.
    McCormick F: How receptors turn Ras on. Nature 363:15–16, 1993Google Scholar
  177. 176.
    Egan SE, Giddings BW, Brooks NW, Buday L, Sizeland AM, Weinberg RA: Association of Sos Ras exchange protein with Grb 2 is implicated in tyrosine kinase signal transduction and transformation. Nature 36:45–51, 1993Google Scholar
  178. 177.
    Hemming R, Wild GE, Berneron JJM: L-Tyrosine phosphorylation of SHC in acetic acid induced colitis in the rat. 1994 (submitted)Google Scholar
  179. 178.
    Miyajima A, Hara T, Kitamura T: Common subunits of cytokine receptors and the functional redundancy of cytokines. Trends Biochem Sci 17:378–382, 1992Google Scholar
  180. 179.
    Mustelin T, Burn P: Regulation of src family tyrosine kinases in lymphocytes. Trends Biochem Sci 18:215–220, 1993Google Scholar
  181. 180.
    Schreurs J, Gorman DM, Miyajima A: Cytokine receptors: A new superfamily of receptors. Int Rev Cytol 137B:121–155, 1993Google Scholar
  182. 181.
    Stahl N, Yancopoulos GD: The alphas, betas, and kinases of cytokine receptor complexes. Cell 74:587–590, 1993Google Scholar
  183. 182.
    Lin HY, Lodish HF: Receptors for the TGF-b superfamily: Multiple polypeptides and serine/threonine kinases. Trends Cell Biol 3:14–19, 1993Google Scholar
  184. 183.
    Massague J: The transforming growth factor-b family. Annu Rev Cell Biol 6:597–641, 1990Google Scholar
  185. 184.
    Massague J: Receptors for the TGF-b family. Cell 69:1067–1070, 1992Google Scholar
  186. 185.
    Taylor SS, Knighton DR, Zheng J, Ten-Eyck LF, Sovadski JM: Structural framework for the protein kinase family. Annu Rev Cell Biol 8:429–462, 1992Google Scholar
  187. 186.
    Van Meer G: Transport and sorting of membrane lipids. Curr Opin Cell Biol 5:661–674, 1993Google Scholar
  188. 187.
    Hauri HP, Schweizer A: The endoplasmic reticulum-Golgi intermediate compartment. Curr Opin Cell Biol 4:600–608, 1992Google Scholar
  189. 188.
    Lippincott-Schwartz J: Bidirectional membrane traffic between the endoplasmic reticulum and Golgi apparatus. Trends Cell Biol 3:81–88, 1993Google Scholar
  190. 189.
    Pelham HR: Recycling of proteins between the endoplasmic reticulum and Golgi complex. Curr Opin Cell Biol 3:585–591, 1991Google Scholar
  191. 190.
    Graham TR, Scott PA, Emr SD: Brefeldin A reversibly blocks early but not late protein transport steps in the yeast secretory pathway. EMBO J 12:869–877, 1993Google Scholar
  192. 191.
    Lippincott-Schwartz J, Yuan L, Tipper C, Anhedt M, Orci L, Klausner RD: Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell 67:601–616, 1991Google Scholar
  193. 192.
    Hong W, Tang BL: Protein trafficking along the exocytotic pathway. Bioessays 15:231–238, 1993Google Scholar
  194. 193.
    Kelly RB: Secretory granule and synaptic vesicle formation. Curr Opin Cell Biol 3:654–660, 1991Google Scholar
  195. 194.
    Hubbard AL: Targeting of membrane and secretory proteins to the apical domain in epithelial cells. Semin Cell Biol 2:365–374, 1991Google Scholar
  196. 195.
    Hunziker W, Mellman I: Relationships between sorting in the exocytic and endocytic pathways of MDCK cells. Semin Cell Biol 2:397–410, 1991Google Scholar
  197. 196.
    Lisanti MP, Rodriguez-Boulan E: Ploarized sorting of GPI-linked proteins in epithelia and membrane microdomains. Cell Biol Int Rep 15:1023–1049, 1991Google Scholar
  198. 197.
    Mostov K, Apodaca G, Aroeti B, Okamoto C: Plasma membrane protein sorting in polarized epithelial cells. J Cell Biol 116:577–583, 1992Google Scholar
  199. 198.
    Bennett MK, Scheller RH: The molecular machinery for secretion is conserved from yeast to neurons. Proc Natl Acad Sci USA 90:2559–2563, 1993Google Scholar
  200. 199.
    Franzusoff A: Beauty and the yeast: Compartmental organization of the secretory pathway. Semin Cell Biol 3:309–324, 1992Google Scholar
  201. 200.
    Kreis TE: Regulation of vesicular and tubular membrane traffic of the Golgi complex by coat proteins. Curr Opin Cell Biol 4:609–615, 1992Google Scholar
  202. 201.
    Rothman JE: The reconstitution of intracellular protein transport in cell-free systems. Harvey Lect 86:65–85, 1992Google Scholar
  203. 202.
    Schekman R: Genetic and biochemical analysis of vesicular traffic in yeast. Curr Opin Cell Biol 4:587–592, 1992Google Scholar
  204. 203.
    Warren G: Intracellular transport: vesicular consumption. Nature 345:382–383, 1990Google Scholar
  205. 204.
    Waters MG, Griff IC, Rothman JD: Proteins involved in vesicular transport and membrane fusion. Curr Opin Cell Biol 3:615–620, 1991Google Scholar
  206. 205.
    Anderson RGW: Plasmalemma caveolae and GPI-anchored membrane proteins. Curr Opin Cell Biol 5:647–652, 1993Google Scholar
  207. 206.
    Dupree P, Parton RG, Raposo G, Kurzchalia TV, Simons K: Caveolae and sorting in the trans-Golgi netword of epithelial cells. EM BO J 12:1597–1605, 1993Google Scholar
  208. 207.
    Sargiacomo M, Sudol M, Tang ZL, Llsanti MP: Signal transducing molecules and glycos-phosphatidylinositol-linked proteins form caveolin-rich insoluble complex in MDCK cells. Cell Biol 122:789–808, 1993Google Scholar
  209. 208.
    Anderson R: Dissecting clathrin-coated pits. Trend Cell Biol 2:177–179, 1992Google Scholar
  210. 209.
    DeLuca-Flaherty C, McKay DB, Parham P, Hill BL: Uncoating protein (hsc70) binds a conformationaly labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell 62:875–887, 1990Google Scholar
  211. 210.
    Gao B, Biosca J, Craig EA, Greene LE, Eisenberg E: Uncoating of coated vesicles by yeast hsp70 proteins. J Biol Chem 266:19565–19571, 1991Google Scholar
  212. 211.
    Nathke IS, Heuser J, Lupas A, Stock A, Turck J, Brodsky FM: Folding and trimerization of clathrin subunits at the triskelion hub. Cell 68:899–910, 1992Google Scholar
  213. 212.
    Pepperkok R, Scheel J, Horstmann H, Horstomann H, Hauri HP, Griffiths G, Kreis TE: Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74:71–82, 1993Google Scholar
  214. 213.
    Pfeffer SR, Roghman JE: Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu Rev Biochem 56:829–852, 1987Google Scholar
  215. 214.
    Balch WE: From G minor to G major. Curr Biol 2:157–160, 1992Google Scholar
  216. 215.
    Bourne HR, Sanders DA, McCormick F: The GTPase superfamily: A conserved switch for diverse cell functions. Nature 348:125–132, 1990Google Scholar
  217. 216.
    Goud B, McCaffrey M: Small GTP-binding proteins and their role in transport. Curr Opin Cell Biol 3:626–633, 1991Google Scholar
  218. 217.
    Melancon P: Vesicle traffic: “G whizz.” Curr Biol 3:230–233, 1993Google Scholar
  219. 218.
    Magee T, Newman C: The role of lipid anchors for small G proteins in membrane trafficking. Trends Cell Biol 2:318–323, 1992Google Scholar
  220. 219.
    Orci L, Palmer DJ, Amherdt M, Rothman JE: Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature 364:732–734, 1993Google Scholar
  221. 220.
    Serafini T, Orci I, Amherdt M, Brunner M, Kahn RA, Rothman JE: ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein. Cell 67:239–253, 1991Google Scholar
  222. 221.
    Bennett MK, Garcia-Arraras JE, Elferink LA, Peterson K, Fleming AM, Hazuke CD, Scheller RH: The syntaxin family of vesicular transport receptors. Cell 74:863–873, 1993Google Scholar
  223. 222.
    Sollner T, Whiteheart SW, Brunner M, Erdjument-Bromage H, Geromanos S, Tempst P, Rothman JE: SNAP receptors implicated in vesicle targeting and fusion. Nature 362:318, 1993Google Scholar
  224. 223.
    Goud B: Small GTP-binding proteins as compartmental markers. Semin Cell Biol 3:301–307, 1992Google Scholar
  225. 224.
    Lombardi D, Soldati T, Riederer MA, Goda Y, Zerial M, Pfeffer SR: Rab9 functions in transport between late endosomes and the trans Golgi network. EM BO J 12:677–682, 1993Google Scholar
  226. 225.
    Marsh M, Cutler D: Membrane traffic: Taking the Rabs off endocytosis. Curr Biol 3:30–33, 1993Google Scholar
  227. 226.
    Walworth NC, Brennwald P, Kabcenell AK, Garrett M, Novick P: Hydrolysis of GTP by Sec4 protein plays an important role in vesicular transport and is stimulated by a GTPaseactivating protein in Saccharomyces cerevisiae. Mol Cell Biol 12:2017–2028, 1992Google Scholar
  228. 227.
    Bradbury NA, Bridges RJ: Role of membrane trafficking in plasma membrane sulute transport. Am J Physiol 267:C1–C24, 1994Google Scholar
  229. 228.
    Weinman EJ, Steplock D, Bui G, Yuan N, Shenolikar S: Regulation of renal Na+-H+ exchanger by cAMP-dependent protein kinase. Am J Physiol 258(Renal Fluid Electrolyte Physiol 27):F1254–F1258, 1990Google Scholar
  230. 229.
    Hanrahan JW, Tabcharani JA, Grygorezyk R: Patch clamp studies of apical membrane chloride channels. In Cystic Fibrosis—Current Topics. JA Dodge, DJH Brock, JH Widdicombe (eds). New York, Wiley, 1993, Vol 1, pp 93–138Google Scholar
  231. 230.
    Goodyear LJ, Hirshman MF, Smith RJ, Horton ES: Glucose transporter number, activity, and isoform content in plasma membranes of red and white skeletal muscle. Am J Physiol 261(Endocrinol Metab 24):E556–E561, 1991Google Scholar
  232. 231.
    Lienhard GE: Regulation of cellular membrane transport by exocytic insertion and endocytic retrieval of transporters. TIBS 8:125–127, 1983Google Scholar
  233. 232.
    Prince LS, Tousson A, Marchase RB: Cell surface labeling of CFTR in T84 cells. Am J Physiol 264(Cell Physiol. 33):C491–C498, 1993Google Scholar
  234. 233.
    Robinson LJ, Pang S, Harris DS, Heuser J, James DE: Translocation of the glucose transporter (GLUT4) to the cell surface in permeabilized 3T3-L1 adipocytes: Effects of ATP, insulin, and GTPgS and localization of GLUT4 to clathrin latices. J Cell Biol 117:1181–1196, 1992Google Scholar
  235. 234.
    Bourget J, Hugon JS, Valenti G, Svelto M: ADH induced water permeability: what role for the microtubular network? Comp Biochem Physiol 90:669–672, 1988Google Scholar
  236. 235.
    Foffer A, Tatham PER, Gomperts BP: Changes in the state of actin during the exocytic reaction in permeabilized rat mast cells. J Cell Biol 111:919–927, 1990Google Scholar
  237. 236.
    Perrin D, Moller K, Hanke K, Soling SD: cAMP and Ca2+-mediated secretion in parotid acinar cells is associated with reversible changes in the organization of the cytoskeleton. J Cell Biol 116:127–134, 1992Google Scholar
  238. 237.
    Black JA, Forte TM, Forte JG: The effects of microfilament disrupting agents on HC1 secretion and ultrastructure of piglet oxyntic cells. Gastroenterology 83:595–604, 1982Google Scholar
  239. 238.
    Blok J, Scherven AA, Mulder-Stapel AA, Ginsel LW, Deams WT: Endocytosis in absorptive cells of cultured human small intestinal tissue: effect of cytochalasin B and D. Cell Tissue Res 222:113–126, 1982Google Scholar
  240. 239.
    Ohta Y, Akiyama T, Nishida E, Sakai H: Protein kinase C and cAMP-dependent protein kinase induce opposite effects on actin polymerization. FEBS Lett 222:305–310, 1987Google Scholar
  241. 240.
    Gottardi CJ, Caplan MJ: An ion-transporting ATPase encodes multiple apical loc-alization signals. J Cell Biol 121:283–293, 1993Google Scholar
  242. 241.
    Gottardi CJ, Caplan MJ: Delivery of Na+,K+-ATPase in polarized epithelial cells. Science Washington DC 260:552–554, 1993Google Scholar
  243. 242.
    Zurzolo C, Rodriguez-Boulan E: Delivery of Na+,K+-ATPase in polarized epithelial cells. Science Washington DC 260:550–551, 1993Google Scholar
  244. 243.
    Notis WM, Orellana SA, Field M: Inhibition of intestinal secretion in rats by colchicine and vinblastine. Gastroenterology 81:766–772, 1981Google Scholar
  245. 244.
    Beckers CJM, Balch WE: GTP: essential components in vesicular trafficking between the endoplasmic reticulum and Golgi apparatus. J Cell Biol 108:1245–1256, 1989Google Scholar
  246. 245.
    Cruetz CE: The annexins and exocytosis. Science Washington DC 258:924–931, 1992Google Scholar
  247. 246.
    Salminen A, Novick P: A ras-like protein is required for post-Golgi event in yeast secretion. Cell 47:527–538, 1987Google Scholar
  248. 247.
    Weidman PJ, Melancon P, Block MR, Rothman JE: Binding of an N-ethylmaleimide sensitive fusion protein to Golgi membranes requires both a soluble protein(s) and an integral membrane receptor. J Cell Biol 108:1589–1596, 1989Google Scholar
  249. 248.
    Opleta-Madsen K, Hardin J, Gall DG: Epidermal growth factor upregulates intestinal electrolyte and nutrient transport. Am J Physiol 260:G807–G814, 1991Google Scholar
  250. 249.
    Opleta-Madsen K, Meddings JB, Gall DG: Epidermal growth factor and postnatal development of intestinal transport and membrane structure. Pediatric Research 30:342–350, 1991Google Scholar
  251. 250.
    Fantl WJ, Johnson DE, Williams LT: Signalling by receptor tyrosine kinases. Annu Rev Biochem 62:453–481, 1993Google Scholar
  252. 251.
    Liddle RA, Carter JD, McDonald AR: Dietary regulation of rat intestinal cholecystokinin gene expression. J Clin Invest 81:2015–2019, 1988Google Scholar
  253. 252.
    Podolsky DK: Regulation of intestinal epithelial proliferation: A few answers, many questions. Am J Physiol 264:G179G186, 1993Google Scholar
  254. 253.
    Gallo-Payet N, Hugon JS: Epidermal growth factor receptors in isolated adult mouse intestinal cells: Studies in vivo and in organ culture. Endocrinology (Baltimore) 116:194–201, 1985Google Scholar
  255. 254.
    Laburth M, Rouyer-Fessard C, Gammeltoft S: Receptors for insulin-like growth factors I and II in rat gastrointestinal epithelium. Am J Physiol 254:G457–G462, 1988Google Scholar

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© Plenum Publishing Corporation 1997

Authors and Affiliations

  • A.B.R. Thomson
  • G. Wild

There are no affiliations available

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