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- W996824503 abstract "Intestinal absorption and renal reabsorption of vitamin C (L-ascorbic acid, L-Asc) is mediated by the epithelial Na+/L-Asc cotransporter SVCT1 (SLC23A1). L-Asc transport is downregulated in Caco-2 cells after pretreatment with ascorbic acid (MacDonald et al [2002] Br J Nutr 87, 97) suggesting that high-dose supplements are not an efficient means of increasing the body pool of vitamin C, and highlighting the need to understand the regulation of SVCT1. Since pro-oxidant environments potently inactivate protein kinase C (PKC), we examined a possible role for PKC in regulating SVCT1, using radiotracer and voltage-clamp techniques in Xenopus oocytes expressing SVCT1. Uptake of 100 μM L-[14C]Asc (100 mM Na+, pH 7.5) was inhibited 91% ± 11% by the PKC activator phorbol 12-myristate 13-acetate (PMA, 100 nM) (P < 0.001) but not by its inactive analogue 4αPMA (P = 0.27). The PMA effect was blocked by the PKC inhibitors Gö6850 and Gö6976, implicating a conventional-type PKC isozyme. PMA treatment resulted in internalization of SVCT1 protein since a 94% ± 7% reduction in L-Asc-evoked currents was associated with (1) a decrease in presteady-state charge (∝ the number of functional units in the plasma membrane), (2) a decrease in membrane capacitance (∝ surface area), and (3) an increase in cell resistance. PMA reduced the Vmax without effect on the K0.5 for L-Asc. Our data support a role for a conventional PKC isozyme in downregulating SVCT1 via derecruitment of SVCT1 from the plasma membrane." @default.
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- W996824503 date "2008-03-01" @default.
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- W996824503 title "PKC activation downregulates the human Na + /L‐ascorbic acid transporter SVCT1 via its derecruitment from the plasma membrane" @default.
- W996824503 doi "https://doi.org/10.1096/fasebj.22.1_supplement.936.16" @default.
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