James McIntyre
Research Professor
Last active: 7/25/2014

Near-infrared optical proteolytic beacons for in vivo imaging of matrix metalloproteinase activity.

McIntyre JO, Scherer RL, Matrisian LM
Methods Mol Biol. 2010 622: 279-304

PMID: 20135290 · PMCID: PMC4495730 · DOI:10.1007/978-1-60327-299-5_18

The exuberant expression of proteinases by tumor cells has long been associated with the breakdown of the extracellular matrix, tumor invasion, and metastasis to distant organs. There are both epidemiological and experimental data that support a causative role for proteinases of the matrix metalloproteinase (MMP) family in tumor progression. Optical imaging techniques provide an extraordinary opportunity for non-invasive "molecular imaging" of tumor-associated proteolytic activity. The application of optical proteolytic beacons for the detection of specific proteinase activities associated with tumors has several potential purposes: (1) Detection of small, early-stage tumors with increased sensitivity due to the catalytic nature of the proteolytic activity, (2) diagnosis and prognosis to distinguish tumors that require particularly aggressive therapy or those that will not benefit from therapy, (3) identification of tumors appropriate for specific anti-proteinase therapeutics and optimization of drug and its dose based on determination of target modulation, and (4) as an indicator of the efficacy of proteolytically activated pro-drugs. This chapter describes the synthesis, characterization, and application of reagents that use visible and near-infrared fluorescence resonance energy transfer (FRET) fluorophore pairs to detect and measure MMP proteolytic activity in tumors in murine models of cancer.

MeSH Terms (14)

Adenoma Animals Fluorescence Resonance Energy Transfer Humans Infrared Rays Intestinal Neoplasms Matrix Metalloproteinases Mice Molecular Imaging Molecular Probes Optical Phenomena Protein Processing, Post-Translational Spectrometry, Fluorescence Xenograft Model Antitumor Assays

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