Identification of protease-sensitive sites in Human Endothelial-Monocyte Activating Polypeptide II protein

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The cleaved ≈22-kDa form of Endothelial-Monocyte Activating Polypeptide [mature (m)EMAP II] functions as a potent inhibitor of tumor growth. Although the anti-tumor effect of mEMAP II has been described, little is known regarding the cleavage of mEMAP II from its precursor form (pEMAP II). We determined that pEMAP II is expressed at the cell membrane surface and proteinases MMP-9, elastase, and cathepsin L release protein fragments consistent with mEMAP II molecular mass. MMP-9 and elastase generate a  ≈25-26 kDa spanning fragments, while cathepsin L generates a  ≈22 kDa fragment. Although several fragments are processed from pEMAP II within a 44 AA residue stretch, cathepsin L cleaves pEMAP II within 4 amino acids of the determined N-terminal sequence, suggesting that this region is sensitive to proteinases.

Original languageEnglish (US)
Pages (from-to)2231-2237
Number of pages7
JournalExperimental Cell Research
Volume312
Issue number12
DOIs
StatePublished - Jul 15 2006
Externally publishedYes

Fingerprint

Cathepsin L
Peptide Hydrolases
Pancreatic Elastase
Matrix Metalloproteinases
Growth Inhibitors
Proteins
Monocytes
Neoplasms
Cell Membrane
Amino Acids
Peptides
small inducible cytokine subfamily E, member 1

Keywords

  • Anti-angiogenesis
  • Endothelial-Monocyte Activating Polypeptide II
  • P43
  • Proteinase

ASJC Scopus subject areas

  • Cell Biology

Cite this

Identification of protease-sensitive sites in Human Endothelial-Monocyte Activating Polypeptide II protein. / Liu, Jie; Schwarz, Margaret.

In: Experimental Cell Research, Vol. 312, No. 12, 15.07.2006, p. 2231-2237.

Research output: Contribution to journalArticle

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