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Pseudopod membrane in TSH-stimulated thyroid cells: a specialized domain in the neighboring apical plasma membrane

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Summary

Pseudopod formation in response to thyrotropin can be obtained with porcine thyroid cell monolayers attached to floating collagen gels or collagen-coated Millipore filters, a model system that allows free access to ligands and antibodies to the apical plasma membrane. To obtain new insight concerning the molecular composition of the pseudopod membrane, (1) ligands were used allowing identification of anionic sites (ruthenium red, cationized ferritin) or carbohydrate units (wheat germ agglutinin, WGA) and (2) antibodies elicited against isolated porcine thyroid membranes or dog intestinal aminopeptidase were employed.

Wheat germ agglutinin-binding sites, detected by fluorescence and electron microscopy, were heterogeneously dispersed on the apical membrane. In TSH-stimulated cells, the absence of WGA-binding sites was showed on the pseudopod membrane of thyroid cells, in addition to the previously reported absence of anionic sites. This absence of binding appeared to be independent of the conditions of incubation and/or times of stimulation. Aminopeptidase, which is an apical marker in thyroid cells, was redistributed and clustered on the pseudopod membrane in the cells exposed to TSH stimulation.

These present findings support the view that the pseudopod surface constitutes a highly specialized microdomain within the thyroid apical plasma membrane during TSH acute stimulation.

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With the technical assistance of Brigitte Nguyen Than Dao, Laboratoire de Neuroendocrinologie A, U.S.T.L., Montpellier. Preliminary accounts of this study were presented at the “XXI-Vème Colloque de la Société Française de Biologie Cellulaire”, Montpellier, 1984

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Barriere, H., Chambard, M., Muranyi-Kovacs, I. et al. Pseudopod membrane in TSH-stimulated thyroid cells: a specialized domain in the neighboring apical plasma membrane. Cell Tissue Res. 245, 159–170 (1986). https://doi.org/10.1007/BF00218096

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  • DOI: https://doi.org/10.1007/BF00218096

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