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(Received for publication, February 4, 1996, and in revised form, April 8, 1996)
From the Department of Physiology, UCLA School of Medicine,
Los Angeles, California 90095-1751
Cotransporters are proteins responsible for the
accumulation of nutrients, neurotransmitters, and drugs in cells. As
forskolin has been shown to stimulate intestinal
Na+/glucose cotransport, we have used electrophysiological
techniques to examine the role of protein kinases in regulating
Na+/glucose cotransporters, SGLT1, expressed in
Xenopus laevis oocytes. We monitored SGLT1 kinetics, the
number of SGLT1 cotransporters in the plasma membrane, and plasma
membrane area before and after activation of protein kinases.
8-Bromoadenosine 3
Volume 271, Number 25,
Issue of June 21, 1996
pp. 14740-14746
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,5-cyclic monophosphate (8-Br-cAMP) and
sn-1,2-dioctanoylglycerol (DOG) were used as membrane
permeable activators of protein kinases A (PKA) and C (PKC),
respectively. In oocytes expressing rabbit SGLT1 8-Br-cAMP increased by
28 ± 4% (n = 10), and DOG decreased by 51 ± 5%
(n = 13) the maximum rate of Na+/glucose
cotransport. These reversible changes in the maximum transport rate
occurred within minutes, and were accompanied by proportional changes
in the number of cotransporters in the membrane and area of the plasma
membrane. This suggests that protein kinases regulate rabbit SGLT1
activity by controlling the distribution of transporters between
intracellular compartments and the plasma membrane, and that this
occurs by exo- and endocytosis. Similar increases in maximum transport
were obtained with activation of PKA in oocytes expressing rabbit,
human, and rat SGLT1 isoforms, but with activation of PKC the response
was isoform-dependent. PKC activation decreased the maximum
rate of transport by rabbit and rat SGLT1, but increased transport by
human SGLT1. We conclude that: (i) the regulation of SGLT1 expression
in oocytes by protein kinases occurs mainly by regulated endo- and
exocytosis; (ii) it is independent of consensus phosphorylation sites
in the transporter; and (iii) the effect of a given kinase depends upon
the actual sequence of the cotransporter expressed. These
considerations may also apply to the regulation of other cotransporters
by protein kinases in oocytes, cells, and tissues.
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