Linked Life Data

9422780

Source:http://linkedlifedata.com/resource/pubmed/id/9422780

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pubmed-article:9422780pubmed:abstractTextInterleukin-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 approximately 50-kDa form of pro-IL-16. Transfected COS cells released a approximately 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 approximately 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-1beta-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.lld:pubmed
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pubmed-article:9422780pubmed:articleTitleProcessing and activation of pro-interleukin-16 by caspase-3.lld:pubmed
pubmed-article:9422780pubmed:affiliationPulmonary Center, Boston University School of Medicine, Boston, Massachusetts 02118, USA. yzhang@bupula.bu.edulld:pubmed
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pubmed-article:9422780pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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