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The acidic glucagon-degrading activity of hepatic endosomes has
been attributed to membrane-bound forms of cathepsins B and D.
Endosomal lysates processed full-length nonradiolabeled glucagon to 32
different peptides that were identified by amino acid analysis and
full-length sequencing. These indicated C-terminal carboxypeptidase,
endopeptidase as well as N-terminal tripeptidyl-aminopeptidase
activities in endosomes. Glucagon proteolysis was inhibited 95% by E-64
and pepstatin A, inhibitors of cathepsins B and D, respectively. This
was confirmed by the pH 6-dependent chemical cross-linking of
[
Volume 270,
Number 26,
Issue of June 30, pp. 15798-15807, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
I]iodoglucagon to a polypeptide of 30 kDa,
which was immunodepleted by polyclonal anti-cathepsin B antibody, and
the removal of greater than 80% of glucagon-degrading activity by
polyclonal antibodies to cathepsins B and D. By similar criteria,
insulin-degrading enzyme was ruled out as a candidate enzyme for
endosomal proteolysis of glucagon. Lysosomal contamination was unlikely
since all forms of cathepsin B in endosomes, i.e. the major
45-kDa inactive precursor as well as the lesser amounts of the 32- and
28-kDa active forms, were tightly bound to endosomal membranes.
Furthermore the mature 29-kDa single-chain and 22-kDa heavy-chain forms
of cathepsin L were undetectable in endosomes, although high levels of
the 37-kDa proform were observed. Membrane association of the
cathepsins B and D was not to the mannose 6-phosphate receptor since
association was unaffected by mannose 6-phosphate and/or EDTA, thereby
indicating a distinct endosomal receptor. Hence, a pool of active
cathepsins B and D as well as a poorly defined tripeptidyl
aminopeptidase is maintained in endosomes by selective membrane
retention. These hydrolases degrade glucagon internalized into liver
parenchyma early in endocytosis.
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