Synthesis and biological evaluation of [18F](2S,4S)4-(3-fluoropropyl) arginine as a tumor imaging agent

Wu, Renbo; Liu, Song; Liu, Yajing; Sun, Yi; Cheng, Xuebo; Huang, Yong; Yang, Zhaoguang; Wu, Zehui

doi:10.1016/j.ejmech.2019.111730

Cited by 17 publications

(16 citation statements)

References 49 publications

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Section: Molecular Imaging Of Arginasementioning

confidence: 99%

“…Thus, although fluorine is not present in natural amino acids, the longer physical half-life of 18 F and the greatest sterical and electronic similarities to hydrogen (which enable the conservation of bond length, strength, and atomic radius when substituting a C-H or C-OH group for a C-F), made this radioisotope very desirable for the radiolabeling of amino acid derivatives [240][241][242]. The addition of fluorine can, however, modify the lipophilicity, pKa, and the biological properties of natural substrates, especially in small molecules such as L-arginine (Figure 8), since slight structural changes or the addition of prosthetic groups are needed to accommodate 18 Although they were not designed or evaluated to specifically or selectively bind arginase, the 18 F-labeled arginine derivatives reported in the literature showed good potential for PET imaging of the arginine metabolism in tumors [243][244][245], especially if compared with the image pattern theoretically expected for the natural substrate analog [ 13 N/ 11 C]arginine [236]. If cleverly designed, the advantage of using radiolabeled modified amino acids, from a PET-imaging point of view, is that they do not metabolize in the same way as the natural ones [241].…”

Section: Development Of Arginase-targeted Radiotracers For Nuclear Imagingmentioning

confidence: 99%

“…This selective accumulation will amplify the radioactive signal, correlating the uptake with the arginase activity or expression. Meanwhile, the not-metabolized fraction of the radiotracer and the Although they were not designed or evaluated to specifically or selectively bind arginase, the 18 F-labeled arginine derivatives reported in the literature showed good potential for PET imaging of the arginine metabolism in tumors [243][244][245], especially if compared with the image pattern theoretically expected for the natural substrate analog [ 13 N/ 11 C]arginine [236]. If cleverly designed, the advantage of using radiolabeled modified amino acids, from a PET-imaging point of view, is that they do not metabolize in the same way as the natural ones [241].…”

Section: Development Of Arginase-targeted Radiotracers For Nuclear Imagingmentioning

confidence: 99%

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Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective

Clemente

Waarde

Antunes

et al. 2020

IJMS

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Arginase is a widely known enzyme of the urea cycle that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. The action of arginase goes beyond the boundaries of hepatic ureogenic function, being widespread through most tissues. Two arginase isoforms coexist, the type I (Arg1) predominantly expressed in the liver and the type II (Arg2) expressed throughout extrahepatic tissues. By producing L-ornithine while competing with nitric oxide synthase (NOS) for the same substrate (L-arginine), arginase can influence the endogenous levels of polyamines, proline, and NO•. Several pathophysiological processes may deregulate arginase/NOS balance, disturbing the homeostasis and functionality of the organism. Upregulated arginase expression is associated with several pathological processes that can range from cardiovascular, immune-mediated, and tumorigenic conditions to neurodegenerative disorders. Thus, arginase is a potential biomarker of disease progression and severity and has recently been the subject of research studies regarding the therapeutic efficacy of arginase inhibitors. This review gives a comprehensive overview of the pathophysiological role of arginase and the current state of development of arginase inhibitors, discussing the potential of arginase as a molecular imaging biomarker and stimulating the development of novel specific and high-affinity arginase imaging probes.

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Section: Molecular Imaging Of Arginasementioning

confidence: 99%

Section: Development Of Arginase-targeted Radiotracers For Nuclear Imagingmentioning

confidence: 99%

Section: Development Of Arginase-targeted Radiotracers For Nuclear Imagingmentioning

confidence: 99%

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Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective

Clemente

Waarde

Antunes

et al. 2020

IJMS

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“…To characterize the transport mechanism of [ 99m Tc]TcO-MOPADTC, competitive inhibition studies were conducted with the S180 cell line according to a previously reported method [ 24 , 25 , 26 ]. A series of inhibitors was added to the cells in DMEM at a concentration of 20 mM.…”

Section: Methodsmentioning

confidence: 99%

Radiolabeling and Biological Evaluation of Novel 99mTc-Nitrido and 99mTc-Oxo Complexes with 4-Methoxy-L-Phenylalanine Dithiocarbamate for Tumor Imaging

et al. 2022

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To develop novel radiolabeled amino acid tumor imaging agents, 4-methoxy-L-phenylalanine dithiocarbamate (MOPADTC) was synthesized successfully, and two kinds of 99mTc-labeled complexes ([99mTc]TcN-MOPADTC and [99mTc]TcO-MOPADTC) with high radiochemical purities (RCP > 95%) were obtained. The in vitro stability and partition coefficient were determined, and the results show that both of these complexes have good in vitro stability; [99mTc]TcO-MOPADTC is hydrophilic, while [99mTc]TcN-MOPADTC is slightly lipophilic. The biodistribution of [99mTc]TcN-MOPADTC and [99mTc]TcO-MOPADTC in mice bearing S180 tumors shows that the tumor uptake and tumor/muscle ratio of [99mTc]TcO-MOPADTC were higher than the tumor uptake and tumor/muscle ratio of [99mTc]TcN-MOPADTC. In addition, the tumor retention of [99mTc]TcO-MOPADTC is better than the tumor retention of [99mTc]TcN-MOPADTC. A competitive inhibition assay was performed, and the results indicate that [99mTc]TcO-MOPADTC may enter cells primarily via the L-alanine/L-serine/L-cysteine (ASC) system. Single-photon emission computed tomography (SPECT) imaging of [99mTc]TcO-MOPADTC shows obvious accumulation in tumor sites, suggesting that [99mTc]TcO-MOPADTC is a novel potential tumor-imaging agent.

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“…18 F-FDG is the commonly used probe to detect glucose uptake for breast cancer imaging. Other probes include 18 F-FMISO (hypoxia condition detection) [73,74], 18 F-flortanidazole (hypoxia and radiotherapy-associated changes detection) [77], 18 F-4F-Gln (glutamine uptake detection) [55], 18 F-fluciclovine (leucine metabolism detection) [6], (2S,4S)4-18 F-FPArg (arginine metabolism detection) [87], 18 F-FASu (detecting levels of cystine/glutamate antiporter subunit xCT) [58,59], 18 F-FLT (thymidine metabolism) [60,61], 89 Zr-transferrin (interrogating MYC signaling pathway) [79], and so on. For breast cancer imaging, positron emission mammography (PEM) is being developed, which achieves a prone position to improve the spatial resolution and reclassify suspicious calcifications [88].…”

Section: Pet Imagingmentioning

confidence: 99%

Integrating metabolic reprogramming and metabolic imaging to predict breast cancer therapeutic responses

Liu

Zhou

Song

2021

Trends in Endocrinology & Metabolism

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Metabolic reprogramming is not only an emerging hallmark of cancer, but also an essential regulator of cancer cell adaptation to the microenvironment. Metabolic imaging targeting metabolic signatures has been widely used for breast cancer diagnosis. However, limited implications have been explored for monitoring breast cancer therapy response, although metabolic plasticity is notably associated with therapy resistance. In this review, we focus on the metabolic alterations upon breast cancer therapy and their potential for evaluating breast cancer therapeutic responses. We summarize the metabolic network and regulatory changes upon breast cancer therapy in terms of cancer pathological and genetic differences and discuss the implications of metabolic imaging with various probes in selecting target beneficiaries for precision treatment. Key metabolic reprogramming of breast cancer in response to therapyReprogramming of glucose metabolism upon breast cancer therapy Drug-resistant breast cancer cells are able to reprogram glucose metabolism to adapt to the stress induced by drug treatment (Figure 1). For example, breast cancer cells resistant to lapatinib, a dual inhibitor of dermal growth factor receptor (EGFR) and HER2, recover the Highlights Reprogramming of metabolic pathways is pivotal for the adaptation and resistance to antitumor treatments in breast cancer.Metabolic changes upon treatment are superior to single timepoint metabolic signals in monitoring breast cancer therapeutic response.Cancer genetic and metabolic heterogeneity need to be fully integrated to precisely predict breast cancer response to different treatments.Metabolic imaging guided usage of anticancer drugs is critical for precise treatment in breast cancer.

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Synthesis and biological evaluation of [18F](2S,4S)4-(3-fluoropropyl) arginine as a tumor imaging agent

Cited by 17 publications

References 49 publications

Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective

Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective

Radiolabeling and Biological Evaluation of Novel 99mTc-Nitrido and 99mTc-Oxo Complexes with 4-Methoxy-L-Phenylalanine Dithiocarbamate for Tumor Imaging

Integrating metabolic reprogramming and metabolic imaging to predict breast cancer therapeutic responses

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