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Vol. 273, Issue 2, 1144-1149, January 9, 1998
From the Pulmonary Center, Boston University School of Medicine,
Boston, Massachusetts 02118, the ¶ Departments of Medicine and
Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, and
the Interleukin-16, a proinflammatory cytokine
produced in CD8+ lymphocytes, is synthesized as a
precursor protein (pro-IL-16). It is postulated that the C-terminal
region of pro-IL-16 is cleaved, releasing bioactive IL-16. To
characterize IL-16 cleavage, we transfected COS cells with a cDNA
encoding a ~50-kDa form of pro-IL-16. Transfected COS cells released
a ~20-kDa IL-16 cleavage product shown to consist of the 121 C-terminal residues of pro-IL-16 by immunoblotting and amino acid
sequencing. Cleaved IL-16, but not pro-IL-16, exhibited lymphocyte
chemoattractant activity. A C-terminal ~20-kDa IL-16 polypeptide was
also released when pro-IL-16 was treated with concanavalin A-stimulated
CD8+ lymphocyte lysate. Cleavage occurred after an Asp,
suggesting involvement of a caspase (interleukin-1
Processing and Activation of Pro-Interleukin-16 by Caspase-3
, and ImmuLogic Pharmaceutical Corporation,
Waltham, Massachusetts 02154
-converting
enzyme/CED-3) family protease. Using recombinant caspases and granzyme
B, we determined that pro-IL-16 cleavage is mediated only by caspase-3. Relevance to pro-IL-16 processing in primary lymphocytes was supported by identifying the p20 subunit of activated caspase-3 in stimulated CD8+ lymphocytes and by inhibition of CD8+
lymphocyte lysate-mediated cleavage with Ac-DEVD-CHO. Pro-IL-16 is a
substrate for caspase-3, and cleavage by this enzyme releases biologically active IL-16 from its inactive precursor.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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