Regulation of endothelial monocyte-activating polypeptide II release by apoptosis

Ulrike E. Knies, Heike A. Behrensdorf, Christopher A. Mitchell, Urban Deutsch, Werner Risau, Hannes C.A. Drexler, Matthias Clauss

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Abstract

Endothelial monocyte-activating polypeptide II (EMAP II) is a proinflammatory cytokine and a chemoattractant for monocytes. We show here that, in the mouse embryo, EMAP II mRNA was most abundant at sites of tissue remodeling where many apoptotic cells could be detected by terminal deoxynucleotidyltransferase-mediated dUTP end labeling. Removal of dead cells is known to require macrophages, and these were found to colocalize with areas of EMAP II mRNA expression and programmed cell death. In cultured cells, post-translational processing of pro-EMAP II protein to the mature released EMAP II form (23 RDa) occurred coincidentally with apoptosis. Cleavage of pro-EMAP II could be abrogated in cultured cells by using a peptide-based inhibitor, which competes with the ASTD cleavage site of pro-EMAP II. Our results suggest that the coordinate program of cell death includes activation of a caspase-like activity that initiates the processing of a cytokine responsible for macrophage attraction to the sites of apoptosis.

Original languageEnglish (US)
Pages (from-to)12322-12327
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number21
StatePublished - Oct 13 1998
Externally publishedYes

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    Knies, U. E., Behrensdorf, H. A., Mitchell, C. A., Deutsch, U., Risau, W., Drexler, H. C. A., & Clauss, M. (1998). Regulation of endothelial monocyte-activating polypeptide II release by apoptosis. Proceedings of the National Academy of Sciences of the United States of America, 95(21), 12322-12327.