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J. Biol. Chem., Vol. 269, Issue 40, 24575-24580, 10, 1994
WC Duckworth, RG Bennett and FG Hamel
The insulin-degrading enzyme (IDE) and the multicatalytic proteinase (MCP)
can be isolated as components of a cytosolic proteolytic complex. IDE is
the primary enzyme involved in cellular degradation of insulin, and insulin
has been shown to interact with cytosolic IDE. MCP is believed to be
important in non-ubiquitin pathways of cellular protein degradation.
Insulin has a dose- and time-dependent inhibitory effect on MCP degradation
of N-succinyl-Leu-Leu-Val-Tyr 7-amino-4- methylcoumarin (LLVY), a substrate
for MCP. Proinsulin also inhibits LLVY degradation in a dose-dependent
manner. The effect of insulin is immediate as measured in a continuously
monitored assay of LLVY degradation. Purification of the IDE-MCP complex
using a variety of approaches, including affinity and conventional
chromatography, retains the insulin effect on LLVY degradation as long as
the complex remains intact. After ion-exchange chromatography, which
separates IDE and MCP, insulin no longer has an inhibitory effect.
Recombination of purified IDE and MCP does not restore the effect of
insulin, but inclusion of additional components from the ion-exchange
column does. These results support the existence of a functional cytosolic
complex that contains IDE and MCP. Insulin interacts with IDE and alters
the activity of MCP, suggesting a functional relationship between these two
components and a mechanism for an intracellular action of insulin.
A direct inhibitory effect of insulin on a cytosolic proteolytic complex containing insulin-degrading enzyme and multicatalytic proteinase
University of Nebraska Medical Center, Omaha, Nebraska 69198-3020.
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