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

F. R. Zhang, M. A. Schwarz

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Lung Cellular and Molecular Physiology
Volume282
Issue number6 26-6
StatePublished - 2002

Fingerprint

Caspase 7
Caspase 3
Endothelium
Peptide Hydrolases
Apoptosis
Cytokines
small inducible cytokine subfamily E, member 1
In Vitro Techniques

Keywords

  • Antiangiogenesis
  • Caspase-7
  • Endothelial monocyte activating polypeptide
  • Endothelial monocyte-activating polypeptide II
  • Neovascularization
  • p43

ASJC Scopus subject areas

  • Pulmonary and Respiratory Medicine
  • Cell Biology
  • Physiology

Cite this

Pro-EMAP II is not primarily cleaved by caspase-3 and -7. / Zhang, F. R.; Schwarz, M. A.

In: American Journal of Physiology - Lung Cellular and Molecular Physiology, Vol. 282, No. 6 26-6, 2002.

Research output: Contribution to journalArticle

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