TY - JOUR
T1 - Identification of protease-sensitive sites in Human Endothelial-Monocyte Activating Polypeptide II protein
AU - Liu, Jie
AU - Schwarz, Margaret A.
N1 - Funding Information:
Research supported in part by Public Health Service grants HL-60061, HL-03981, and HL-75764 from the National Heart, Lung, and Blood Institute.
PY - 2006/7/15
Y1 - 2006/7/15
N2 - 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.
AB - 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.
KW - Anti-angiogenesis
KW - Endothelial-Monocyte Activating Polypeptide II
KW - P43
KW - Proteinase
UR - http://www.scopus.com/inward/record.url?scp=33745262526&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33745262526&partnerID=8YFLogxK
U2 - 10.1016/j.yexcr.2006.03.024
DO - 10.1016/j.yexcr.2006.03.024
M3 - Article
C2 - 16674941
AN - SCOPUS:33745262526
SN - 0014-4827
VL - 312
SP - 2231
EP - 2237
JO - Experimental Cell Research
JF - Experimental Cell Research
IS - 12
ER -