Na+/Pi co-transport alters rapidly cytoskeletal protein polymerization dynamics in opossum kidney cells
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چکیده
منابع مشابه
Na+/Pi co-transport alters rapidly cytoskeletal protein polymerization dynamics in opossum kidney cells.
We studied with biochemical and immunofluorescent techniques the interactions between the actin microfilament and tubulin microtubule cytoskeleton and Na+/P1 co-transport in opossum kidney cells, a line with proximal tubular characteristics. On brief (5 min) incubation of the cells with a low (0.1 mM) concentration of Pi, a rapid F-actin depolymerization takes place, which fails to occur in cel...
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The main nonhormonal mechanism for controlling inorganic phosphate (P(i)) homeostasis is renal adaptation of the proximal tubular P(i) transport rate to changes in dietary phosphate content. Opossum kidney (OK) cell line is an in vitro renal model that maintains the ability of renal adaptation to the extracellular P(i) concentration. We have studied how two competitive inhibitors of P(i) transp...
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Renal secretion of organic cations and anions are pleiotropic, active processes in mammals. Some nucleosides such as deoxyadenosine (dAdo), 2-chlorodeoxyadenosine, and azidothymidine are secreted by human and rodent kidneys. Previous work (J. A. Nelson, J. F. Kuttesch, Jr., and B. H. Herbert. Biochemical Pharmacology 32: 2323-2327, 1983) indicated a role for the classic organic cation transport...
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Parathyroid hormone (PTH) inhibits proximal tubular brush border membrane Na+/Pi cotransport activity; this decrease in the transport activity was found to be associated with a decrease in type II Na+/Pi cotransporter protein content in rat brush border membranes. In the present study we investigated the PTH-dependent regulation of the type II Na+/Pi cotransporter in opossum kidney cells, a pre...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1996
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3150241