A Newly Designed Hyperpolarized Aminopeptidase N Probe Sensitively Detects Early Therapeutic Responses Heterogeneously on Pancreatic Tumors
Motivation: Molecular imaging is a promising methodology for diagnosing cancer and monitoring treatments by noninvasively visualizing the alternations of cancer metabolisms. Goal(s): A framework for developing novel dissolution Dynamic Nuclear Polarization(dDNP) probes is needed to overcome their limited availabilities for in vivo and clinical applications. Approach: dDNP-metabolic MRI successfully monitors therapeutic responses in spatiotemporal enzymatic activities particularly at earlier stages before the volumetric changes can be observed. Results: In this presentation, we will demonstrate a model case for a rationally designed novel dDNP probe, aminopeptidase-N(CD13), which allows us to detect heterogenetic treatment responses with an anti-angiogenic/antitumor drug, sunitinib, at the earlier stages in tumors. Impact: This work exhibits a framework that a rationally designed hyperpolarized MR probe targeted to a highly-selective enzymatic activity, aminopeptidase-N, leads to monitor early therapeutic responses on cancer tissues in vivo and to observe tumor heterogeneity in their treatment responses non-invasively.
Authors
- Shinsuke Sando (ORCID: https://orcid.org/0000-0003-0275-7237)
- Yoichi Takakusagi (ORCID: https://orcid.org/0000-0002-6786-0748)
- Norikazu Koyasu
- Hiroyuki Yatabe (ORCID: https://orcid.org/0009-0004-3118-9317)
- Kazutoshi Yamamoto (ORCID: https://orcid.org/0000-0001-9405-5421)
- Yutaro Saito (ORCID: https://orcid.org/0000-0001-7610-121X)
- Murali Krishna Chatakonda (ORCID: https://orcid.org/0000-0002-6169-091X)
Publication Details
- Journal
- Proceedings on CD-ROM - International Society for Magnetic Resonance in Medicine. Scientific Meeting and Exhibition/Proceedings of the International Society for Magnetic Resonance in Medicine, Scientific Meeting and Exhibition
- Published
- 2024-11-26
- DOI
- https://doi.org/10.58530/2024/0552
- Primary Topic
- Peptidase Inhibition and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.00