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Lectin-binding pattern on the surface epidermis of Ambystoma tigrinum larvae

A light- and electron-microscopic study

Histochemistry volume 87, pages 431–438 (1987)Cite this article

Summary

The surface epidermis of Ambystoma tigrinum larvae was examined at the light- and electron-microscope levels using five different lectin conjugates as probes for the detection of sugar residues on the cell membranes. Concanavalin A (Con-A), wheat-germ agglutinin (WGA), Ricinus communis agglutinin I (RCA-I), Dolichos biflorus agglutinin and soybean agglutinin (SBA) conjugates clearly labelled the surface cells, especially their apical surfaces. At electron microscopy, the labelling on plasma membranes was found to exhibit regional differences. Among the lectins tested WGA displayed a particularly characteristic binding pattern. WGA also bound to basolateral cell surfaces, including the tight-junction zone wich was also stained by the RCA-I conjugate. The different labelling intensity and staining patterns obtained with the conjugates indicated the polarity of the cell surfaces. It is also assumed that the WGA staining of the basolateral membranes and intercellular spaces reflected transcellular transport, which is facilitated by acidic glycoconjugates. Other functional aspects of the polarized distribution of the lectin conjugates were also correlated with the receptor sites of certain sugar residues.

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Affiliations

  1. Department of Animal Biology and Marine Ecology, Messina University, Via dei Verdi 75, I-98100, Messina, Italy

    G. Zaccone, S. Fasulo, P. Lo Cascio, A. Licata, L. Ainis & R. Affronte

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  1. G. Zaccone
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  2. S. Fasulo
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  3. P. Lo Cascio
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  4. A. Licata
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  5. L. Ainis
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  6. R. Affronte
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Zaccone, G., Fasulo, S., Cascio, P.L. et al. Lectin-binding pattern on the surface epidermis of Ambystoma tigrinum larvae. Histochemistry 87, 431–438 (1987). https://doi.org/10.1007/BF00496814

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  • DOI: https://doi.org/10.1007/BF00496814

Keywords

  • Basolateral Membrane
  • Concanavalin
  • Apical Surface
  • Characteristic Binding
  • Binding Pattern