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J. Biol. Chem., Vol. 259, Issue 6, 3519-3525, 03, 1984
ME Handlogten and MS Kilberg
System A-mediated amino acid transport in liver tissue is stimulated by
diabetes or by exogenous glucagon. The present report describes the decay
process for stimulated System A activity in isolated rat hepatocytes.
Transport induced by glucagon, insulin, or spontaneous diabetes (BB/G rats)
decayed rapidly after initiation of primary cultures; the estimated
half-life was about 1.5 h. In contrast, the stimulated activity in cultured
hepatocytes from streptozotocin- diabetic rats had a half-life of about 2.5
h. It is not known if the loss of System A activity is the result of
proteolysis or of another form of inactivation. The decay was blocked by
either actinomycin or cycloheximide, but was unaffected by leupeptin,
methylamine, chloroquine, dinitrophenol, rotenone, or tunicamycin. Studies
with cycloheximide and actinomycin suggest the following: 1) within 30 min
after initiation of cell cultures, synthesis of the corresponding mRNA for
the transport-inactivating protein has begun; 2) the mRNA for
transport-inactivating protein is relatively long-lived, but the
inactivating protein itself has a half-life of less than 1 h; and 3)
actinomycin blocks the decay through inhibition of transport- inactivating
protein biosynthesis rather than by protection of the mRNA for the protein
responsible for System A activity. A working model for the synthesis and
decay of System A activity is presented. Cationic amino acid transport,
System y+, was also stimulated severalfold after induction of diabetes or
glucagon injection of rats. Systems ASC, X-, and N were enhanced to varying
degrees in hepatocytes from diabetic or glucagon-injected rats, but the
level of stimulation for each was not as great as that found for Systems A
or y+.
Induction and decay of amino acid transport in the liver. Turnover of transport activity in isolated hepatocytes after stimulation by diabetes or glucagon
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