Volume 67, Issue 2 pp. 103-114
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Wheat germ agglutinin (WGA) reduces ADH-induced water flow and induces cell surface changes in epithelial cells of frog urinary bladder

Pierre Favard

Pierre Favard

Centre de Biologie Cellulaire, CNRS, 67, rue Maurice-Günsbourg, 94205 Ivry-sur-Seine Cedex, France

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Nina Favard

Corresponding Author

Nina Favard

Centre de Biologie Cellulaire, CNRS, 67, rue Maurice-Günsbourg, 94205 Ivry-sur-Seine Cedex, France

Centre de Biologie Cellulaire, CNRS, 67, rue Maurice-Günsbourg, 94205 Ivry-sur-Seine Cedex, FranceSearch for more papers by this author
Qian Long Zhu

Qian Long Zhu

Centre de Biologie Cellulaire, CNRS, 67, rue Maurice-Günsbourg, 94205 Ivry-sur-Seine Cedex, France

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Jacques Bourguet

Jacques Bourguet

Département de Biologie, CEN de Saclay, 91191 Gif-sur-Yvette Cedex, France

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Jean-Pierre Lechaire

Jean-Pierre Lechaire

Centre de Biologie Cellulaire, CNRS, 67, rue Maurice-Günsbourg, 94205 Ivry-sur-Seine Cedex, France

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Maryvonne Maillard

Maryvonne Maillard

Centre de Biologie Cellulaire, CNRS, 67, rue Maurice-Günsbourg, 94205 Ivry-sur-Seine Cedex, France

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Abstract

The functional and structural changes induced by apical wheat germ agglutinin (WGA) 100 μg/ml exposure on frog urinary bladder have been investigated and the possible correlation between these effects discussed. Bladders, apically exposed to WGA for 30 min to 3 hr exhibit a marked reduction of their response to antidiuretic hormone (ADH) challenge and of their hydrosmotic reactivity. Structural changes triggered by WGA trreatmentare: 1. apical invaginations of the plasma membrane, interpreted as endocytotic in nature, taking into account the results of carbohydrate cytochemical detection and horseradish peroxidase (HRP) exposure: 2. cytoskeleton disorganization and microvilli collapse. These phenomena do not interfere with cortical granule traffic and are independent of ADH challenge: they occur in ADH-stimulated bladders as well as in bladders at rest. These findings could be interpreted as follows: binding of the divalent lectin WGA to its coat specific receptors would induce changes in the apical membrane structure which in turn could provoke disorganization and disruption of apical cytoskeletal elements associated with plasma membrane. Reduction of bladder response to ADH challenge could result from a reduced recyling of aggrephores, as they are associated with cytoskeletal elements in the subapical cytoplasm. Collapse of microvilli and endocytotic events also could result from apical cytoskeleton disruption, as microvilli are sustained by bundles of actin filaments interconnected with apical cytoskeleton filaments and as plasma membrane is associated with apical cytoskeleton. However, these two last events evidently occur in ADH-challenged or non-challenged bladders.

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