Identification of protease-sensitive sites in Human Endothelial-Monocyte Activating Polypeptide II protein
Identification of protease-sensitive sites in Human Endothelial-Monocyte Activating Polypeptide II protein
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DOI：
10.1016/j.yexcr.2006.03.024
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发表时间：
2006-07-15
影响因子：
3.7
通讯作者：
Schwarz, Margaret A.
中科院分区：
文献类型：
--
作者：
Liu, Jie;Schwarz, Margaret A.
切割的约22 kDa形式的内皮单核细胞激活多肽[成熟（in）EMAP II]作为肿瘤生长的有效抑制剂发挥作用。虽然mEMAP II的抗肿瘤作用已被描述，但关于mEMAP II从其前体形式（pEMAP II）裂解的情况知之甚少。我们确定pEMAP II在细胞膜表面表达，并且蛋白酶MMP-9、弹性蛋白酶和组织蛋白酶L释放与mEMAP II分子量一致的蛋白片段。MMP-9和弹性蛋白酶产生大约25-26 kDa的跨越片段，而组织蛋白酶L产生大约22 kDa的片段。虽然有几个片段是从pEMAP II的44个氨基酸残基的延伸，组织蛋白酶L切割pEMAP II的4个氨基酸内确定的N-末端序列，这表明该地区是敏感的蛋白酶。(c)2006年爱思唯尔公司All rights reserved.
The cleaved approximate to 22-kDa form of Endothelial-Monocyte Activating Polypeptide [mature (in) 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 approximate to 25-26 kDa spanning fragments, while cathepsin L generates a approximate to 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. (c) 2006 Elsevier Inc. All rights reserved.