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The cellular specificity of lectin binding in the kidney

I. A light microscopical study in the rat

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Summary

In order to estimate the usefulness of lectins in the study of the functional segmentation of the nephron, the sites of binding of five lectins were identified in the rat kidney. Lectin-peroxidase conjugates were applied to cryostat sections. The bound conjugates were stained with 3,3′-diaminobenzidine for light microscopical observation. Each lectin has a specific binding pattern along the nephron. Reversely, the different segments of the nephron defined by other histological methods can be identified on the basis of their affinity for lectins. The different parts of the thick ascending limb, namely the medullary segment, the cortical segment and the macula densa, can be distinguished even more readily with lectin histochemistry than with any other histochemical procedure. The binding of lectins to luminal membranes in some segments indicate the possibility to use lectins for the separation of particular cell types and for the modification of the transport properties of their membranes.

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References

  • Crayen M, Thoenes W (1975) Architektur und cytologische Charakterisierung des distalen Tubulus der Rattenniere. Fortschr Zool 23:279–288

    Google Scholar 

  • Cuatrecasas P, Tell GPE (1973) Insulin-like activity of concanavalin A and wheat-germ agglutinin. Direct interaction with insulin receptors. Proc Natl Acad Sci USA 70:485–489

    Google Scholar 

  • Dunn M, Malluci L (1980) Effect of concanavalin A and succinyl-concanavalin A on nucleoside and sugar uptake in mouse embryo fibroblasts. Biochem Biophys Res Commun 95:118–125

    Google Scholar 

  • Gilboagarber N, Mizrahi L (1980) Estimation of non-specific lectin-mediated staining of glutaraldehyde-fixed cells. Experientia 36:1416–1417

    Google Scholar 

  • Greven G, Schreibmüller F (1981) Effect of carbohydrate binding lectins on sodium and chloride transport in the loop of Henle. Pflügers Arch 389 (Suppl): R41

    Google Scholar 

  • Holthöfer H, Virtanen I, Pettersson E, Törnroth T, Alfthan O, Linder E, Miettinen A (1981) Lectins as fluorescence microscopic markers for saccharides in the human kidney. Lab Invest 45:391–399

    Google Scholar 

  • Horisberger M, Vonlanthen M (1978) Simultaneous localization of a hepatic binding protein specific for galactose and of galactose-containing receptors on rat hepatocytes. J Histochem Cytochem 26:960–966

    Google Scholar 

  • Inbar M, Ben-Hassat H, Sachs L (1971) Location of amino acid and carbohydrate transport sites in the surface membrane of normal and transformed mammalian cells. J Memb Biol 6:195–209

    Google Scholar 

  • Kaissling B, Kriz W (1979) Structural analysis of the rabbit kidney. Adv Anat Embryol Cell Biol 56:1–123

    Google Scholar 

  • Kaissling B, Peter S, Kriz W (1977) The transition of the thick ascending limb of Henle's loop into the distal convoluted tubule in the nephron of the rat kidney. Cell Tissue Res 182:111–118

    Google Scholar 

  • Kimura A, Wigzell H, Holmquist G, Ersson B, Carlsson P (1979) Selective affinity fractionation of murine cytotoxic lymphocytes (CTL). Unique lectin specific binding of the CTL associated surface glycoprotein, T 145. J Exp Med 149:473–484

    Google Scholar 

  • Kinzel V, Richards J, Kübler D (1977) Lectin receptor sites at the cell surface employed for affinity separation of tissue culture cells. Exp Cell Res 105:389–400

    Google Scholar 

  • Le Hir M, Kaissling B, Koeppen BM, Wade JB (1982) Binding of peanut lectin to specific epithelial cell types in the kidney. Am J Physiol 242:C117-C120

    Google Scholar 

  • Majerus PW, Brodie GN (1972) The binding of phytohaemagglutinin to human platelet plasma membrane. J Biol Chem 247:4253–4257

    Google Scholar 

  • Maunsbach AB (1966) Observations on the segmentation of the proximal tubule of the rat kidney. comparison of results from phase contrast, fluorescence and electron microscopy. J Ultrastruct Res 16:239–258

    Google Scholar 

  • Morel F, Imbert-Teboul M, Chabardès D (1981) Distribution of hormone-dependent adenylate cyclase in the nephron and its physiological significance. Annu Rev Physiol 43:569–581

    Google Scholar 

  • Oemar BS, Buss H, Hollweg G (1980) Influence of the lectins and polycations on the configuration of renal podocytes. Renal Physiol 3:330–335

    Google Scholar 

  • Pena SDJ, Gordon BB, Karpati G, Carpenter S (1981) Lectin histochemistry of human skeletal muscle. J Histochem Cytochem 29:542–546

    Google Scholar 

  • Pereira MEA, Kabat EA (1979) A versatile immunoadsorbant capable of binding lectins of various specificities and its use for the separation of cell populations. J Cell Biol 82:185–194

    Google Scholar 

  • Peters JH, Hausen P (1971) Effect of phytohaemagglutinin on lymphocyte membrane transport. 2. Stimulation of facilitated diffusion of 3-O-methyl-glucose. Eur J Biochem 19:509–513

    Google Scholar 

  • Pinto da Silva P, Torrisi MR, Kachar B (1981) Freeze-fracture cytochemistry: localization of wheat germ agglutinin and concanavalin A binding sites on freeze-fractured pancreatic cells. J Cell Biol 91:361–372

    Google Scholar 

  • Reisner Y, Linker-Israeli M, Sharon N (1976) Separation of mouse thymocytes into two subpopulations by the use of peanut agglutinin. Cell Immunol 25:129–134

    Google Scholar 

  • Renau-Piqueras J, Knecht E, Hernandez-Yago J (1981) Effects of different fixative solutions on labeling of concanavalin A receptor sites in human T-lymphocytes. Histochemistry 71:559–565

    Google Scholar 

  • Resch K, Schneider S, Szamel M (1981) Separation of right-side-out-oriented subfraction from purified thymocyte plasma membrane by affinity chromatography on concanavalin A-sepharose. Anal Biochem 117:282–292

    Google Scholar 

  • Schechter Y, Ben-Ami S (1981) Insulin-like effects of wax bean agglutinin in rat adipocytes. Biochem Biophys Res Commun 98:367–373

    Google Scholar 

  • Sikri KL, Foster CL, Bloomfield FJ, Marshall RD (1979) Localization by immunofluorescence and by light- and electron-microscopic immunoperoxidase techniques of Tamm-Horsfall glycoprotein in adult hamster kidney. Biochem J 181:525–532

    Google Scholar 

  • Sikri KL, Foster CL, MacHugh N, Marshall RJ (1981) Localization of Tamm-Horsfall glycoprotein in the human kidney using immunofluorescence and immunoelectron microscopical techniques. J Anat 132:597–605

    Google Scholar 

  • Stoward PJ, Spicer SS, Miller RL (1980) Histochemical reactivity of peanut lectin-horseradish peroxidase conjugate. J Histochem Cytochem 28:979–990

    Google Scholar 

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This research has been supported by the Swiss National Science Foundation, Grant No. 3.900-0.79

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Le Hir, M., Dubach, U.C. The cellular specificity of lectin binding in the kidney. Histochemistry 74, 521–530 (1982). https://doi.org/10.1007/BF00496666

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  • DOI: https://doi.org/10.1007/BF00496666

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