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Am J Physiol Lung Cell Mol Physiol (January 18, 2002). doi:10.1152/ajplung.00141.2001
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Articles in PresS, published online ahead of print January 18, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00141.2001
Submitted on April 24, 2001
Accepted on January 8, 2002

Pro-Endothelial-Monocyte Activating Polypeptide (EMAP) II is not primarily cleaved by caspase 3 and 7

Fangrong Zhang1 and Margaret A Schwarz2*

1 Critical Care and Pediatrics, Childrens Hospital Los Angeles, Unversity of Southern California Keck School of Medicine, Los Angeles, CA, USA
2 Surgical Sciences, UMDNJ Robert Wood Johnson Medical School, New Brunswick, NJ, USA

* To whom correspondence should be addressed. E-mail: m.schwarz{at}umdnj.edu.

Endothelial-Monocyte Activating Polypeptide (EMAP) II is a unique cytokine, also known as P43, the active mature form of which exhibits anti-angiogenic properties in vivo and in vitro. The proteolytic enzymes that are 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 implicates that other proteolytic processes are involved in the release of the active mature EMAP II that allows it to induce apoptosis via caspase 3 activation in migrating and dividing endothelium.




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