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cotransporter in
vascular smooth muscle
1 Renal Division, Department of Medicine, and 3 Department of Physiology, Emory University School of Medicine, Atlanta, Georgia 30322; and 2 Department of Biophysics and Molecular Physiology, University of Cincinnati, Cincinnati, Ohio 45267
Vasoconstrictors activate the
Na+-K+-2Cl
cotransporter NKCC1 in
rat aortic smooth muscle, but the mechanism is unknown. Efflux of
86Rb+ from rat aorta in response to
phenylephrine (PE) was measured in the absence and presence of
bumetanide, a specific inhibitor of NKCC1. Removal of extracellular
Ca2+ completely abolished the activation of NKCC1 by PE.
This was not due to inhibition of Ca2+-dependent
K+ channels since blocking these channels with
Ba2+ in Ca2+-replete solution did not prevent
activation of NKCC1 by PE. Stimulation of NKCC1 by PE was inhibited
70% by 75 µM ML-9, 97% by 2 µM wortmannin, and 70% by 2 mM
2,3-butanedione monoxime, each of which inhibited isometric force
generation in aortic rings. Bumetanide-insensitive Rb+
efflux, an indication of Ca2+-dependent K+
channel activity, was reduced by ML-9 but not by the other inhibitors. Stretching of aortic rings on tubing to increase lumen diameter to
120% of normal almost completely blocked the stimulation of NKCC1 by
PE without inhibiting the stimulation by hypertonic shrinkage. We
conclude that activation of the
Na+-K+-2Cl cotransporter by PE is
the direct result of smooth muscle contraction through
Ca2+-dependent activation of myosin light chain kinase.
This indicates that the
Na+-K+-2Cl cotransporter is
regulated by the contractile state of vascular smooth muscle.
sodium-potassium-2-chloride cotransport; myosin light chain kinase; phenylephrine; contraction
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