ArticleBioorganic & medicinal chemistry letters2014
Near-infrared triple-helical peptide with quenched fluorophores for optical imaging of MMP-2 and MMP-9 proteolytic activity in vivo.
Article in Bioorganic & medicinal chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Dissecting MMP PThe Journal of biological chemistry · 2018Article
- Imaging the Tumor Microenvironment.Advances in experimental medicine and biology · 2017Review
- Matrix Metalloproteinase-Targeted Imaging of Lung Inflammation and Remodeling.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2017Article
- Regulation and involvement of matrix metalloproteinases in vascular diseases.Frontiers in bioscience (Landmark edition) · 2016Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The gelatinase members of the MMP family have consistently been associated with tumor invasiveness, which make them an attractive target for molecular imaging. We report new activatable proteolytic optical imaging agents that consist of triple-helical peptide (THP) conjugates, with high specificity to the gelatinases, bearing quenched cypate dyes. With quenching efficiencies up to 51%, the amplified fluorescence signal upon cypate3-THP hydrolysis by the gelatinases (kcat/KM values of 6.4×10(3) M(-1) s(-1) to 9.1×10(3) M(-1) s(-1) for MMP-2 and MMP-9, respectively) in mice bearing human fibrosarcoma xenografted tumors was monitored with fluorescence molecular tomography. There was significant fluorescence enhancement within the tumor and this enhancement was reduced by treatment with pan-MMP inhibitor, Ilomastat. These data, combined with the gelatinase substrate specificity observed in vitro, indicated the observed fluorescence at the site of the tumor was due to gelatinase mediated hydrolysis of cypate3-THP.
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Registered trials
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