Paper
3 February 2007 In vivo detecting matrix metalloproteinase (MMP) activity by a genetically engineered fluorescent probe
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Abstract
Degradation of the extracellular matrix (ECM) by matrix metalloproteinases (MMPs) enhances tumor invasion and metastasis. To monitor MMP activity, we constructed plasmid that encoded a fluorescent sensor DC, in which an MMP substrate site (MSS) is sandwiched between DsRed2 and ECFP. MMPs are secretory proteins, only acting on the outside of cells; hence, an expressing vector was used that displayed the fluorescent sensor on the cellular surface. The DC was expressed in cells with high secretory MMP, so MSS was cleaved by MMP. Also, GM6001, an MMP inhibitor, causes DsRed2 signals to increase in living cells and on the chick embryo chorioallantoic membrane (CAM). Thus, this fluorescent sensor was able to sensitively monitor MMP activation in vivo. Potential applications for this sensor include high-throughput screening for MMP inhibitors for anti-cancer research, and detailed analysis of the effects of MMP inhibitors.
© (2007) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Jie Yang, Zhihong Zhang, Ting Su, and Qingming Luo "In vivo detecting matrix metalloproteinase (MMP) activity by a genetically engineered fluorescent probe", Proc. SPIE 6449, Genetically Engineered and Optical Probes for Biomedical Applications IV, 644919 (3 February 2007); https://doi.org/10.1117/12.701627
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KEYWORDS
Luminescence

Tumors

Content addressable memory

Fluorescence resonance energy transfer

Sensors

Proteins

Signal detection

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