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Department of Physiology, College of Medicine, University of Arizona, Tucson, Arizona 85724
To examine the role of protein kinase C
(PKC) in organic anion (OA) secretion, we used epifluorescence
microscopy to study steady-state transepithelial secretion of 1 µM
fluorescein (FL) by isolated perfused S2 segments of rabbit renal
proximal tubules. Addition of 100 nM phorbol 12-myristate 13-acetate
(PMA), a known PKC activator, to the bathing medium decreased
steady-state secretion of FL by ~30% after 25 min. This inhibition
was irreversible and, indeed, increased to ~40% at 25 min following
removal of PMA [10 µM 1,2-dioctanoyl-sn-glycerol (DOG)
produced a comparable inhibition]. The inhibition produced by PMA
was blocked when 100 nM of either staurosporine (ST) or
bisindolylmaleimide I (BIM), both known PKC inhibitors, was added to
the bath for a 20-min preexposure followed by the addition of PMA. ST
or BIM alone had no significant effect on FL secretion, suggesting that
the basal FL secretion rate was not under influence of PKC. Addition of
1 µM of either the peptide hormone bradykinin (BK) or the
1-receptor agonist phenylephrine (PE), both of which
stimulate PKC via a ligand-receptor-PKC coupling reaction, to the bath
also inhibited FL secretion by ~22 and ~27%, respectively.
However, the inhibition was completely reversible after removal of BK
or PE. Pretreatment of tubules with 100 nM BIM eliminated the
inhibition of FL secretion produced by exposure to PE. We conclude that
PKC negatively regulates the net secretion of OAs in rabbit renal
proximal tubules. The data indicate that BK or catecholamines can play
a physiological role in regulating OA secretion via PKC activation.
fluorescein; organic anion/dicarboxylate exchanger; transepithelial transport in real time; bradykinin; phenylephrine; phorbol 12-myristate 13-acetate; 1,2-dioctanoyl-sn-glycerol; staurosporine; bisindolylmaleimide I
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