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Direct Production of Functional Matrix metalloproteinase--14 Without Refolding or Activation and Its Application for in Vitro Inhibition Assays

Direct Production of Functional Matrix metalloproteinase--14 Without Refolding or Activation and Its Application for in Vitro Inhibition Assays

Dong Hyun Nam, Xin Ge

Biotechnol Bioeng. 2016 Apr;113(4):717-23.

PMID: 26416249

Abstract:

Human matrix metalloproteinase (MMP)-14, a membrane-bound zinc endopeptidase, is one of the most important cancer targets because it plays central roles in tumor growth and invasion. Large amounts of active MMP-14 are required for cancer research and the development of chemical or biological MMP-14 inhibitors. Current methods of MMP-14 production through refolding and activation are labor-intensive, time-consuming, and often associated with low recovery rates, lot-to-lot variation and heterogeneous products. Here, we report direct production of the catalytic domain of MMP-14 in the periplasmic space of Escherichia coli. 0.5 mg/L of functional MMP-14 was produced without tedious refolding or problematic activation process. MMP-14 prepared by simple periplasmic treatment can be readily utilized to evaluate the potencies of chemical and antibody-based inhibitors. Furthermore, co-expression of both MMP-14 and antibody Fab fragments in the periplasm facilitated inhibitory antibody screening by avoiding purification of MMP-14 or Fabs. We expect this MMP-14 expression strategy can expedite the development of therapeutic drugs targeting MMPs with biological significance.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42412343	MT1-MMP, Catalytic Domain, Human, Recombinant, E. coli			Price

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