Non-invasive imaging and cellular tracking of pulmonary emboli by near-infrared fluorescence and positron-emission tomography

Michael J. Page, André L. Lourenço, Tovo David, Aaron M. LeBeau, Fiore Cattaruzza, Helena C. Castro, Henry F. VanBrocklin, Shaun R. Coughlin and Charles S. Craik ()
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Michael J. Page: University of California
André L. Lourenço: University of California
Tovo David: Cardiovascular Research Institute, University of California
Aaron M. LeBeau: University of California
Fiore Cattaruzza: University of California
Helena C. Castro: LABiEMol, Postgraduate Program in Pathology, Universidade Federal Fluminense
Henry F. VanBrocklin: University of California
Shaun R. Coughlin: Cardiovascular Research Institute, University of California
Charles S. Craik: University of California

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: Abstract Functional imaging of proteolytic activity is an emerging strategy to quantify disease and response to therapy at the molecular level. We present a new peptide-based imaging probe technology that advances these goals by exploiting enzymatic activity to deposit probes labelled with near-infrared (NIR) fluorophores or radioisotopes in cell membranes of disease-associated proteolysis. This strategy allows for non-invasive detection of protease activity in vivo and ex vivo by tracking deposited probes in tissues. We demonstrate non-invasive detection of thrombin generation in a murine model of pulmonary embolism using our protease-activated peptide probes in microscopic clots within the lungs with NIR fluorescence optical imaging and positron-emission tomography. Thrombin activity is imaged deep in tissue and tracked predominantly to platelets within the lumen of blood vessels. The modular design of our probes allows for facile investigation of other proteases, and their contributions to disease by tailoring the protease activation and cell-binding elements.

Date: 2015
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DOI: 10.1038/ncomms9448

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