کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2132972 1086731 2006 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Identification of protease-sensitive sites in Human Endothelial–Monocyte Activating Polypeptide II protein
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی تحقیقات سرطان
پیش نمایش صفحه اول مقاله
Identification of protease-sensitive sites in Human Endothelial–Monocyte Activating Polypeptide II protein
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Cell Research - Volume 312, Issue 12, 15 July 2006, Pages 2231–2237
نویسندگان
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