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Am J Physiol Lung Cell Mol Physiol 282: L1239-L1244, 2002. First published January 18, 2002; doi:10.1152/ajplung.00141.2001
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Vol. 282, Issue 6, L1239-L1244, June 2002

Pro-EMAP II is not primarily cleaved by caspase-3 and -7

F. R. Zhang1 and M. A. Schwarz1,2

1 Departments of Pediatrics, Cardiothoracic Surgical Research, and Surgery, Childrens Hospital Research Institute, Los Angeles 90027; Keck School of Medicine, University of Southern California, Los Angeles, California 90089; and 2 Departments of Surgery and Pediatrics, University of Medicine and Dentistry of New Jersey- Robert Wood Johnson Medical School, New Brunswick, New Jersey 08903

Endothelial monocyte-activating polypeptide (EMAP) II is a unique cytokine, also known as p43, the active mature form of which exhibits antiangiogenic properties in vivo and in vitro. The proteolytic enzymes associated with the cleavage and release of the active mature form, however, remain unclear. Here we show that, in contrast to prior observations, purified pro-EMAP II is not cleaved by either caspase-3 or -7 in vivo or in vitro. Thus other proteolytic processes, which allow it to induce apoptosis via caspase-3 activation in migrating and dividing endothelium, may be involved in the release of the active mature EMAP II.

neovascularization; endothelial monocyte-activating polypeptide II; antiangiogenesis; p43; caspase-7; endothelial monocyte activating polypeptide


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