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      Parathyroid hormone leads to the lysosomal degradation of the renal type II Na/Pi cotransporter.

      Proceedings of the National Academy of Sciences of the United States of America
      Acetylcysteine, analogs & derivatives, pharmacology, Animals, Carrier Proteins, metabolism, Cell Compartmentation, Cells, Cultured, Cycloheximide, Cysteine Endopeptidases, Cysteine Proteinase Inhibitors, Kidney, Leupeptins, Lysosomes, Microscopy, Confocal, Multienzyme Complexes, Opossums, Parathyroid Hormone, Phosphates, Proteasome Endopeptidase Complex, Protein Synthesis Inhibitors, Sodium-Phosphate Cotransporter Proteins, Sodium-Phosphate Cotransporter Proteins, Type II, Symporters

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          Abstract

          We have studied the involvement of proteolytic pathways in the regulation of the Na/Pi cotransporter type II by parathyroid hormone (PTH) in opossum kidney cells. Inhibition of lysosomal degradation (by leupeptin, ammonium chloride, methylamine, chloroquine, L-methionine methyl ester) prevented the PTH-mediated degradation of the transporter, whereas inhibition of the proteasomal pathway (by lactacystin) did not. Moreover it was found (i) that whereas lysosomal inhibitors prevented the PTH-mediated degradation of the transporter they did not prevent the PTH-mediated inhibition of the Na/Pi cotransport and (ii) that treating opossum kidney cells with lysosomal inhibitors led to an increased expression of the transporter without any concomitant increase in the Na/Pi cotransport. Further analysis by subcellular fractionation and morphological techniques showed (i) that the Na/Pi cotransporter is constitutively transported to and degraded within late endosomes/lysosomes and (ii) that PTH leads to the increased degradation of the transporter in late endosomes/lysosomes.

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