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. 1974 Aug 1;62(2):329–343. doi: 10.1083/jcb.62.2.329

DIFFERENTIAL LOCALIZATION OF CELL SURFACE AND SECRETORY COMPONENTS IN RAT INTESTINAL EPITHELIUM BY USE OF LECTINS

Marilynn E Etzler 1, Margaret L Branstrator 1
PMCID: PMC2109395  PMID: 4609988

Abstract

Sections through various levels of small intestine from adult male rats were examined by fluorescence microscopy after treatment with fluorescein isothiocyanate-labeled lectins from Dolichos biflorus, Lotus tetragonolobus, Ricinus communis, and Triticum vulgare (wheat germ). The latter three lectins reacted with the microvillar portion of the epithelial cells lining the crypts and villi in sections of intestine adjacent to the pylorus. This pattern of reactivity was sharply altered along the first 15 cm of intestine so that in sections distal to this point the luminal surfaces of only those epithelial cells in the crypts and at the base of the villi reacted with the L. tetragonolobus and R. communis lectins, whereas the wheat germ lectin reacted with the surfaces of the cells lining the villi. In sections from the distal end of the small intestine, all three lectins reacted with the surfaces of cells only at the base of the villi and in the crypts. These results show a difference in surface components in cells at various portions on the villi and the dependence of these differences on the region of intestine. The D. biflorus lectin reacted with approximately 25% of the goblet cells at each level of intestine studied whereas the reactivities of the goblet cells with the other three lectins were dependent upon the region of intestine.

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Selected References

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  1. Altmann G. G., Enesco M. Cell number as a measure of distribution and renewal of epithelial cells in the small intestine of growing and adult rats. Am J Anat. 1967 Sep;121(2):319–336. doi: 10.1002/aja.1001210210. [DOI] [PubMed] [Google Scholar]
  2. Clarke R. M. Mucosal architecture and epithelial cell production rate in the small intestine of the albino rat. J Anat. 1970 Nov;107(Pt 3):519–529. [PMC free article] [PubMed] [Google Scholar]
  3. Dahlqvist A., Nordström C. The distribution of disaccharidase activities in the villi and crypts of the small-intestinal mucosa. Biochim Biophys Acta. 1966 Mar 7;113(3):624–626. doi: 10.1016/s0926-6593(66)80024-3. [DOI] [PubMed] [Google Scholar]
  4. Etzler M. E. Use of plant agglutinins in characterization of glycoproteins and glycolipids from mammalian cells. Ann N Y Acad Sci. 1974;234(0):260–275. doi: 10.1111/j.1749-6632.1974.tb53038.x. [DOI] [PubMed] [Google Scholar]
  5. Forstner G. G., Sabesin S. M., Isselbacher K. J. Rat intestinal microvillus membranes. Purification and biochemical characterization. Biochem J. 1968 Jan;106(2):381–390. doi: 10.1042/bj1060381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. GOLDSTEIN I. J., HOLLERMAN C. E., SMITH E. E. PROTEIN-CARBOHYDRATE INTERACTION. II. INHIBITION STUDIES ON THE INTERACTION OF CONCANAVALIN A WITH POLYSACCHARIDES. Biochemistry. 1965 May;4:876–883. doi: 10.1021/bi00881a013. [DOI] [PubMed] [Google Scholar]
  7. Greenaway P. J., LeVine D. Binding of N-acetyl-neuraminic acid by wheat-germ agglutinin. Nat New Biol. 1973 Feb 7;241(110):191–192. doi: 10.1038/newbio241191a0. [DOI] [PubMed] [Google Scholar]
  8. Imondi A. R., Balis M. E., Lipkin M. Changes in enzyme levels accompanying differentiation of intestinal epithelial cells. Exp Cell Res. 1969 Dec;58(2):323–330. doi: 10.1016/0014-4827(69)90512-6. [DOI] [PubMed] [Google Scholar]
  9. Imondi A. R., Lipkin M., Balis M. E. Enzyme and template stability as regulatory mechanisms in differentiating intestinal epithelial cells. J Biol Chem. 1970 May 10;245(9):2194–2198. [PubMed] [Google Scholar]
  10. Ito S. Structure and function of the glycocalyx. Fed Proc. 1969 Jan-Feb;28(1):12–25. [PubMed] [Google Scholar]
  11. JENNINGS M. A., FLOREY H. W. Autoradiographic observations on the mucous cells of the stomach and intestine. Q J Exp Physiol Cogn Med Sci. 1956 Apr;41(2):131–152. doi: 10.1113/expphysiol.1956.sp001171. [DOI] [PubMed] [Google Scholar]
  12. Kaplan M. E., Kabat E. A. Studies on human antibodies. IV. Purification and properties of anti-A and anti-B obtained by absorption and elution from insoluble blood group substances. J Exp Med. 1966 Jun 1;123(6):1061–1081. doi: 10.1084/jem.123.6.1061. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LORAN M. R., ALTHAUSEN T. L. Cellular proliferation of intestinal epithelia in the rat two months after partial resection of the ileum. J Biophys Biochem Cytol. 1960 Jul;7:667–672. doi: 10.1083/jcb.7.4.667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LeVine D., Kaplan M. J., Greenaway P. J. The purification and characterization of wheat-germ agglutinin. Biochem J. 1972 Oct;129(4):847–856. doi: 10.1042/bj1290847. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. MESSIER B., LEBLOND C. P. Cell proliferation and migration as revealed by radioautography after injection of thymidine-H3 into male rats and mice. Am J Anat. 1960 May;106:247–285. doi: 10.1002/aja.1001060305. [DOI] [PubMed] [Google Scholar]
  16. MORGAN W. T. J., WATKINS W. M. The inhibition of the haemagglutinins in plant seeds by human blood group substances and simple sugars. Br J Exp Pathol. 1953 Feb;34(1):94–103. [PMC free article] [PubMed] [Google Scholar]
  17. Moog F., Yeh K. Y. Intestinal alkaline phosphatase of the rat: development and distribution of activity with phenylphosphate and -glycerophosphate. Comp Biochem Physiol B. 1973 Mar 15;44(3):657–666. doi: 10.1016/0305-0491(73)90214-9. [DOI] [PubMed] [Google Scholar]
  18. Neutra M., Leblond C. P. Synthesis of the carbohydrate of mucus in the golgi complex as shown by electron microscope radioautography of goblet cells from rats injected with glucose-H3. J Cell Biol. 1966 Jul;30(1):119–136. doi: 10.1083/jcb.30.1.119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Nicolson G. L., Blaustein J., Etzler M. E. Characterization of two plant lectins from Ricinus communis and their quantitative interaction with a murine lymphoma. Biochemistry. 1974 Jan 1;13(1):196–204. doi: 10.1021/bi00698a029. [DOI] [PubMed] [Google Scholar]
  20. Nicolson G. L., Blaustein J. The interaction of Ricinus communis agglutinin with normal and tumor cell surfaces. Biochim Biophys Acta. 1972 May 9;266(2):543–547. doi: 10.1016/0005-2736(72)90109-5. [DOI] [PubMed] [Google Scholar]
  21. PALAY S. L., KARLIN L. J. An electron microscopic study of the intestinal villus. I. The fasting animal. J Biophys Biochem Cytol. 1959 May 25;5(3):363–372. doi: 10.1083/jcb.5.3.363. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Podolsky D. K., Weiser M. M. Specific selection of mitotically active intestinal cells by concanavalin A-derivatized fibers. J Cell Biol. 1973 Aug;58(2):497–500. doi: 10.1083/jcb.58.2.497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. RINDERKNECHT H. Ultra-rapid fluorescent labelling of proteins. Nature. 1962 Jan 13;193:167–168. doi: 10.1038/193167b0. [DOI] [PubMed] [Google Scholar]
  24. SPICER S. S. Histochemical differentiation of mammalian macopolysaccharides. Ann N Y Acad Sci. 1963 Mar 30;106:379–388. doi: 10.1111/j.1749-6632.1963.tb16652.x. [DOI] [PubMed] [Google Scholar]
  25. SPRINGER G. F., WILLIAMSON P. Immunochemical significance of L- and D-fucose derivatives. Biochem J. 1962 Nov;85:282–291. doi: 10.1042/bj0850282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. TRIANTAPHYLLOPOULOS E., TUBA J. Studies on the distribution and kinetics of the alkaline phosphatase of rat small intestine. Can J Biochem Physiol. 1959 May;37(5):699–709. [PubMed] [Google Scholar]
  27. Tomita M., Kurokawa T., Onozaki K., Ichiki N., Osawa T., Ukita T. Purification of galactose-binding phytoagglutinins and phytotoxin by affinity column chromatography using sepharose. Experientia. 1972 Jan 15;28(1):84–85. doi: 10.1007/BF01928278. [DOI] [PubMed] [Google Scholar]
  28. Webster H. L., Harrison D. D. Enzymic activities during the transformation of crypt to columnar intestinal cells. Exp Cell Res. 1969 Aug;56(2):245–253. doi: 10.1016/0014-4827(69)90009-3. [DOI] [PubMed] [Google Scholar]
  29. Weiser M. M. Concanavalin A agglutination of intestinal cells from the human fetus. Science. 1972 Aug 11;177(4048):525–526. doi: 10.1126/science.177.4048.525. [DOI] [PubMed] [Google Scholar]
  30. Weiser M. M. Intestinal epithelial cell surface membrane glycoprotein synthesis. I. An indicator of cellular differentiation. J Biol Chem. 1973 Apr 10;248(7):2536–2541. [PubMed] [Google Scholar]
  31. Weiser M. M. Intestinal epithelial cell surface membrane glycoprotein synthesis. II. Glycosyltransferases and endogenous acceptors of the undifferentiated cell surface membrane. J Biol Chem. 1973 Apr 10;248(7):2542–2548. [PubMed] [Google Scholar]

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