CHANGES IN LOCALIZATION OF OUABAIN-SENSITIVE, POTASSIUM-DEPENDENT PARA-NITROPHENYLPHOSPHATASE ACTIVITY IN HUMAN THYROID-CARCINOMA CELLS

  • 1 January 1983
    • journal article
    • research article
    • Vol. 48  (4) , 411-418
Abstract
K+-dependent, ouabain-sensitive nitrophenyl phosphatase (K+-NPPase) activity, which reflects the terminal dephosphorylation step of (Na+ + K+)-ATPase action, was studied histochemically in human thyroid normal follicular cells and in human thyroid carcinoma cells, using a newly developed 1-step lead citrate method. In normal thyroid follicular cells, reaction product for K+-NPPase activity was found on the lateral plasma membrane and not on either the apical or basal plasma membrane. In thyroid carcinoma cells, a large amount of reaction product was observed on the lateral plasma membrane and also on the apical and basal plasma membrane. Appropriate control experiments indicated that the deposition of reaction product was K+ dependent and ouabain sensitive. Although there was some overlap in the distribution of reaction products for K+-NPPase and Mg2+-ATPase, significant differences were consistently observed. Biochemical findings indicated that the K+-NPPase activity per milligram of DNA in thyroid carcinoma cells was .apprx. 10 times higher than that in normal thyroid cells, and that a significant positive correlation exists between K+-NPPase and (Na+ + K+)-ATPase activity. The physiologic and pathologic implications of this localization for tracing the route of active Na+ transport, which might participate in the transport of I- in both human thyroid normal follicular cells and human thyroid carcinoma cells, are discussed.

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