Identification of substrate sequences for membrane type-1 matrix metalloproteinase using bacteriophage peptide display library

被引：41

作者：

Ohkubo, S ^{[1
]}

Miyadera, K ^{[1
]}

Sugimoto, Y ^{[1
]}

Matsuo, K ^{[1
]}

Wierzba, K ^{[1
]}

Yamada, Y ^{[1
]}

机构：

[1] Taisho Pharmaceut Co Ltd, Hanno Res Ctr, Canc Res Lab, Hanno, Saitama 3578527, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 266卷 / 02期

关键词：

D O I：

10.1006/bbrc.1999.1816

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Membrane type-1 matrix metalloproteinase (MT1-MMP) has been reported to mediate the activation of progelatinase A (proMMP-2) which is associated with tumor invasion and metastasis, and also known to have an ability to digest extracellular matrix components. To clarify substrate specificity of MT1-MMP, we have searched for amino acid sequences cleaved by this protease using the hexamer substrate phage library consisting of a large number of randomized amino acids sequences. The consensus substrate sequences for MT1-MMP were deduced from the selected clones and appeared to be P-X-G/P-L at the P3-P1' sites. Peptide cleavage assay revealed that MT1-MMP preferentially digested a synthetic substrate containing Pro of the P1 position compared to that being substituted with Gly. Our results may have an important implication to identifying new target proteins for MT1-MMP and leading to the design of its selective inhibitors suitable for cancer chemotherapy. (C) 1999 Academic Press.

引用

页码：308 / 313

页数：6

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