Hostname: page-component-77c89778f8-vpsfw Total loading time: 0 Render date: 2024-07-16T18:20:28.550Z Has data issue: false hasContentIssue false
  • English
  • Français

Genetic regulation of enterocyte differentiation

Published online by Cambridge University Press:  28 February 2007

Michael W. Smith
Michael W. Smith
Affiliation:
Department of Cell Biology, AFRC Institute of Animal Physiology and Genetics Research, Babraham, Cambridge CB2 4AT
Rights & Permissions [Opens in a new window]

Abstract

An abstract is not available for this content so a preview has been provided. As you have access to this content, a full PDF is available via the ‘Save PDF’ action button.
Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
Symposium on ‘The digestive tract in nutritional adaptation’
Information
Proceedings of the Nutrition Society , Volume 52 , Issue 2 , August 1993 , pp. 293 - 300
Copyright
Copyright © The Nutrition Society 1993

References

REFERENCES

Boller, K., Arpin, M., Pringault, E., Mangeat, P. & Reggio, H. (1988). Differential distribution of villin and villin mRNA in mouse intestinal epithelial cells. Differentiation 39, 51–57.CrossRefGoogle ScholarPubMed
Brown, A. L. J. (1962). Microvilli of the human jejunal epithelial cells. Journal of Cell Biology 12, 623–627.CrossRefGoogle Scholar
Cheeseman, C. I. (1986). Expression of amino acid and peptide transport systems in rat small intestine. American Journal of Physiology 251, G636–G641.Google ScholarPubMed
Collins, A. J., James, P. S. & Smith, M. W. (1989). Sugar-dependent selective induction of mouse jejunal disaccharidase activities. Journal of Physiology 419, 157–167.CrossRefGoogle ScholarPubMed
Cremaschi, D., James, P. S., Meyer, G., Rossetti, C. & Smith, M. W. (1986). Intracellular potassium as a possible inducer of amino acid transport across hamster jejunal enterocytes. Journal of Physiology 375, 107–119.CrossRefGoogle ScholarPubMed
Dupret, J. M., Brun, P., Perret, C., Lumri, N., Thomasset, M. & Cuisinier-Gleizes, P. (1987). Transcriptional and post-translational regulation of vitamin-D-dependent calcium binding protein gene expression in the rat duodenum by 1,25-dihydroxycholecalciferol. Journal of Biological Chemistry 262, 16553–16557.CrossRefGoogle Scholar
Freeman, T. C., Tivey, D. R. & Collins, A. C. (1992). Expression of lactase mRNA in rabbit small intestine. Gut 33, Suppl., S35.Google Scholar
Freiburghaus, A. U., Schmitz, J., Shindler, M., Rotthauwe, H. W., Kuitunen, P., Launiala, K. & Hadorn, B. (1976). Protein patterns of brush-border fragments in congenital lactose malabsorption and in specific hypolactasia in the adult. New England Journal of Medicine 294, 1030–1032.CrossRefGoogle ScholarPubMed
Haase, W., Heitmann, K., Friese, W., Ollig, D. & Koepsell, H. (1990). Characterization and histochemical localization of the rat intestinal Na+-D-glucose cotransporter by monoclonal antibodies. European Journal of Cell Biology 52, 297–309.Google ScholarPubMed
Haffen, K., Kedinger, M. & Simon-Assmann, P. (1989). Cell contact dependent regulation of enterocyte differentiation. In Human Gastrointestinal Development, pp. 19–39 [Lebenthal, E., editor]. New York: Raven Press.Google Scholar
Hauft, S. M., Kim, S. H., Schmidt, G. H., Pease, S., Rees, S., Harris, S., Roth, K. A., Hansbrough, J. R., Cohn, S. M., Ahnen, D. J., Wright, N. A., Goodlad, R. A. & Gordon, J. I. (1992). Expression of SV-40T antigen in the small intestinal epithelium of transgenic mice results in proliferative changes in the crypt and re-entry of villus-associated enterocytes into the cell cycle but has no apparent effect on cellular differentiation programs and does not cause neoplastic transformation. Journal of Cell Biology 117, 825–839.CrossRefGoogle Scholar
Iseki, S. & Kondo, H. (1990). Light microscopic localization of hepatic fatty acid binding protein mRNA in jejunal epithelia of rats using in situ hybridization, immunochemical and autoradiographic techniques. Journal of Histochemistry and Cytochemistry 38, 111–115.CrossRefGoogle Scholar
Kedinger, M., Simon, P. M., Grenier, J. F. & Haffen, K. (1981). Role of epithelial-mesenchymal interactions in the ontogenesis of intestinal brush-border enzymes. Developmental Biology 86, 339–347.CrossRefGoogle ScholarPubMed
King, I. S., Paterson, J. Y. F., Peacock, M. A., Smith, M. W. & Syme, G. (1983). Effect of diet upon enterocyte differentiation in the rat jejunum. Journal of Physiology 344, 465–481.CrossRefGoogle ScholarPubMed
Kinter, W. B. & Wilson, T. H. (1965). Autoradiographic study of sugar and amino acid absorption by everted sacs of hamster intestine. Journal of Cell Biology 25, 19–39.CrossRefGoogle ScholarPubMed
Kiyama, H., Wu, J. C. Y., Smith, M. W., Lawson, E. D. M. & Emson, P. C. (1991). Developmental control over vitamin-D-induced calbindin gene expression during early differentiation of chicken enterocytes. Differentiation 46, 69–73.CrossRefGoogle Scholar
Leblond, C. P. (1965). The time dimension in histology. American Journal of Anatomy 116, 1–28.CrossRefGoogle ScholarPubMed
Mayel-Afshar, S., Lane, S. M. & Lawson, D. E. M. (1988). Relationship between the levels of calbindin synthesis and calbindin mRNA in chick intestine. Journal of Biological Chemistry 263, 4355–4361.CrossRefGoogle ScholarPubMed
Menge, H., Sepúlveda, F. V. & Smith, M. W. (1983). Cellular adaptation of amino acid transport following intestinal resection in the rat. Journal of Physiology 334, 213–223.CrossRefGoogle ScholarPubMed
Milne, M. D. (1974). Hereditary disorders of intestinal transport. In Intestinal Absorption, vol. 4B, pp. 961–1013 [Smyth, D. H. editor]. London: Plenum Press.CrossRefGoogle Scholar
Nordström, C., Dahlqvist, A. & Josefsson, L. (1968). Quantitative determination of enzymes in different parts of the villi and crypts of rat small intestine. Comparisons of alkaline phosphatase, disaccharidases and dipeptidases. Journal of Histochemistry and Cytochemistry 15, 713–721.CrossRefGoogle Scholar
Norén, O., Dabelsteen, E., Høyer, P. E., Olsen, J., Sjöström, H. & Hansen, G. H. (1989). Onset of transcription of the aminopeptidase N (leucemia antigen CD13) gene at the crypt/villus transition zone during rabbit enterocyte differentiation. FEBS Letters 259, 107–112.CrossRefGoogle Scholar
Norman, A. W., Friedlander, E. J. & Henry, H. L. (1981). Determination of the rates of synthesis and degradation of vitamin D-dependent chick intestinal and renal calcium-binding proteins. Archives of Biochemistry and Biophysics 206, 305–317.CrossRefGoogle ScholarPubMed
Phillips, A. D. & Schmitz, J. (1992). Familial microvillous atrophy: A clinicopathological survey of 23 cases. Journal of Pediatric Gastroenterology and Nutrition 14, 380–396.CrossRefGoogle ScholarPubMed
Savidge, T. C., Smith, M. W., James, P. S. & Aldred, P. (1991). Salmonella-induced M-cell formation in germ-free mouse Peyer's patch tissue. American Journal of Pathology 139, 177–184.Google ScholarPubMed
Siebert, P., Hunziker, W. & Norman, A. W. (1982). Cell-free translation analysis of the vitamin D-dependent calcium binding protein mRNA activity present in total RNA and polysomal extracts from chick intestine. Archives of Biochemistry and Biophysics 219, 286–296.CrossRefGoogle ScholarPubMed
Smith, M. W. (1991). Cell biology and molecular genetics of enterocyte differentiation. Current Topics in Membrane Transport 39, 153–179.CrossRefGoogle Scholar
Smith, M. W. (1992). Diet effects on enterocyte development. Proceedings of the Nutrition Society 51, 173–179.CrossRefGoogle ScholarPubMed
Smith, M. W. & Brown, D. (1989). Dual control over microvillus elongation during enterocyte development. Comparative Biochemistry and Physiology 93A, 623–628.CrossRefGoogle Scholar
Smith, M. W., Paterson, J. Y. F. & Peacock, M. A. (1984). A comprehensive description of brush border membrane development applying to enterocytes taken from a wide variety of mammalian species. Comparative Biochemistry and Physiology 77A, 655–662.CrossRefGoogle Scholar
Smith, M. W., Turvey, A. & Freeman, T. C. (1992). Appearance of phloridzin-sensitive glucose transport is not controlled at mRNA level in rabbit jejunal enterocytes. Experimental Physiology 77, 525–528.CrossRefGoogle Scholar
Spencer, R., Charman, M. & Lawson, D. E. M. (1978). Stimulation of intestinal calcium-binding-protein mRNA synthesis in the nucleus of vitamin D-deficient chicks by 1,25-dihydroxycholecalciferol. Biochemical Journal 175, 1089–1094.CrossRefGoogle Scholar
Stirling, C. E. & Kinter, W. B. (1967). High-resolution radioautography of galactose-3H accumulation in rings of hamster intestine. Journal of Cell Biology 35, 585–604.CrossRefGoogle ScholarPubMed
Takata, K., Kasahara, T., Kasahara, M., Ezaki, O. & Hirano, H. (1992). Immunohistochemical localization of Na+-dependent glucose transporter in rat jejunum. Cell and Tissue Research 267, 3–9.CrossRefGoogle ScholarPubMed
Theofan, G., Nguyen, A. P. & Norman, A. W. (1986). Regulation of calbindin-D28k gene expression by 1,25-dihydroxyvitamin D3 is correlated to receptor occupancy. Journal of Biological Chemistry 261, 16943–16947.CrossRefGoogle ScholarPubMed
Traber, P. G. (1990). Regulation of sucrase-isomaltase gene expression along the crypt-villus axis of rat small intestine. Biochemical and Biophysical Research Communications 173, 765–773.CrossRefGoogle ScholarPubMed
Weiser, M. M. (1973). Intestinal epithelial cell surface membrane glycoprotein synthesis. I. An indicator of cellular differentiation. Journal of Biological Chemistry 248, 2536–2541.CrossRefGoogle ScholarPubMed
Wu, J. C. Y., Smith, M. W. & Lawson, D. E. M. (1992). Time dependency of 1,25(OH)2D3 induction of calbindin mRNA and calbindin expression in chick enterocytes during their differentiation along the crypt-villus axis. Differentiation 51, 195–200.CrossRefGoogle ScholarPubMed
Wu, J. C. Y., Smith, M. W., Mitchell, M. A., Peacock, M. A., Turvey, A. & Keable, S. J. (1993). Enterocyte expression of calbindin, calbindin mRNA and calcium transport increases in jejunal tissue during onset of egg production in the fowl (Gallus domesticus). Comparative Biochemistry and Physiology (In the Press).CrossRefGoogle ScholarPubMed