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Production of Active MMP7 in E. coli and Its Application for Metalloproteinase Inhibitors Screening

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MMP-7 is the smallest metalloproteinase. Its unregulated activities and existence in serum are recently known to be tightly related with life-threatening disease such as cardiac disease and several cancers. The protein production is thought to be useful for its characterization and antibody generation. Although many attempts at bacterial expressions have been conducted, they were recovered as insoluble and inactive protein. In this study, after soluble expression, singlestep purification and conversion to active protease, it was applied for the screening secretory metalloproteinase inhibitors in conditioned media of human cancer cells.

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Keywords: GST fusion; MMP-7/matrilysin; matrix metalloproteinase; metalloproteinase inhibitor; reverse-zymography; soluble expression in E. coli

Document Type: Research Article

Publication date: 2010-05-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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