International Journal of Molecular Sciences

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The Role of Nuclear Medicine in Cancer Diagnosis and Therapy

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Dear Colleagues,

Nuclear Medicine with positron emission tomography (PET) and single-photon emission computed tomography (SPECT) is an important tool for the diagnosis of various diseases and the radionuclide therapy of cancers. It also has translational potential, from preclinical to clinical studies, in personalized medicine for many diseases. Multimodal imaging and/or therapy including nuclear medicine, magnetic resonance imaging, ultrasonography, near-infrared imaging, etc., may create further progress in personalized medicine. In addition, advanced PET and SPECT imaging technologies emphasize the usefulness of nuclear medicine.

This Special Issue focuses on the synthesis and evaluation of novel radiopharmaceuticals, the other applications of radiopharmaceuticals for clinical use, and the combination of radionuclides with other imaging modalities. Advanced PET and SPECT scanners and imaging technologies are also target topics. However, the areas of interest are not limited to these keywords. This Special Issue will focus on fundamental cellular/molecular studies, and papers that contain only clinical trials/data will not be accepted.

Dr. Masato Kobayashi
Guest Editor

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14 pages, 1448 KiB

Open AccessArticle

Potential Application of the Myocardial Scintigraphy Agent [¹²³I]BMIPP in Colon Cancer Cell Imaging

by Kakeru Sato, Yuka Hirayama, Asuka Mizutani, Jianwei Yao, Jinya Higashino, Yuto Kamitaka, Yuka Muranaka, Kana Yamazaki, Ryuichi Nishii, Masato Kobayashi and Keiichi Kawai

Int. J. Mol. Sci. 2024, 25(14), 7747; https://doi.org/10.3390/ijms25147747 - 15 Jul 2024

Viewed by 796

Abstract

[¹²³I]β-methyl-p-iodophenyl-pentadecanoic acid ([¹²³I]BMIPP), which is used for nuclear medicine imaging of myocardial fatty acid metabolism, accumulates in cancer cells. However, the mechanism of accumulation remains unknown. Therefore, this study aimed to elucidate the accumulation and accumulation mechanism of [¹²³I]BMIPP in cancer cells. We compared the accumulation of [¹²³I]BMIPP in cancer cells with that of [¹⁸F]FDG and found that [¹²³I]BMIPP was a much higher accumulation than [¹⁸F]FDG. The accumulation of [¹²³I]BMIPP was evaluated in the presence of sulfosuccinimidyl oleate (SSO), a CD36 inhibitor, and lipofermata, a fatty acid transport protein (FATP) inhibitor, under low-temperature conditions and in the presence of etomoxir, a carnitine palmitoyl transferase I (CPT1) inhibitor. The results showed that [¹²³I]BMIPP accumulation was decreased in the presence of SSO and lipofermata in H441, LS180, and DLD-1 cells, suggesting that FATPs and CD36 are involved in [¹²³I]BMIPP uptake in cancer cells. [¹²³I]BMIPP accumulation in all cancer cell lines was significantly decreased at 4 °C compared to that at 37 °C and increased in the presence of etomoxir in all cancer cell lines, suggesting that the accumulation of [¹²³I]BMIPP in cancer cells is metabolically dependent. In a biological distribution study conducted using tumor-bearing mice transplanted with LS180 cells, [¹²³I]BMIPP highly accumulated in not only LS180 cells but also normal tissues and organs (including blood and muscle). The tumor-to-intestine or large intestine ratios of [¹²³I]BMIPP were similar to those of [¹⁸F]FDG, and the tumor-to-large-intestine ratios exceeded 1.0 during 30 min after [¹²³I]BMIPP administration in the in vivo study. [¹²³I]BMIPP is taken up by cancer cells via CD36 and FATP and incorporated into mitochondria via CPT1. Therefore, [¹²³I]BMIPP may be useful for imaging cancers with activated fatty acid metabolism, such as colon cancer. However, the development of novel imaging radiotracers based on the chemical structure analog of [¹²³I]BMIPP is needed. Full article

(This article belongs to the Special Issue The Role of Nuclear Medicine in Cancer Diagnosis and Therapy)

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17 pages, 2191 KiB

Open AccessArticle

Preclinical Evaluation of HER2-Targeting DARPin G3: Impact of Albumin-Binding Domain (ABD) Fusion

by Sergey M. Deyev, Maryam Oroujeni, Javad Garousi, Torbjörn Gräslund, Ruonan Li, Alia Hani Binti Rosly, Anna Orlova, Elena Konovalova, Alexey Schulga, Anzhelika Vorobyeva and Vladimir Tolmachev

Int. J. Mol. Sci. 2024, 25(8), 4246; https://doi.org/10.3390/ijms25084246 - 11 Apr 2024

Cited by 1 | Viewed by 1935

Abstract

Designed ankyrin repeat protein (DARPin) G3 is an engineered scaffold protein. This small (14.5 kDa) targeting protein binds with high affinity to human epidermal growth factor receptor 2 (HER2). HER2 is overexpressed in several cancers. The use of the DARPin G3 for radionuclide therapy is complicated by its high renal reabsorption after clearance via the glomeruli. We tested the hypothesis that a fusion of the DARPin G3 with an albumin-binding domain (ABD) would prevent rapid renal excretion and high renal reabsorption resulting in better tumour targeting. Two fusion proteins were produced, one with the ABD at the C-terminus (G3-ABD) and another at the N-terminus (ABD-G3). Both variants were labelled with ¹⁷⁷Lu. The binding properties of the novel constructs were evaluated in vitro and their biodistribution was compared in mice with implanted human HER2-expressing tumours. Fusion with the ABD increased the retention time of both constructs in blood compared with the non-ABD-fused control. The effect of fusion with the ABD depended strongly on the order of the domains in the constructs, resulting in appreciably better targeting properties of [¹⁷⁷Lu]Lu-G3-ABD. Our data suggest that the order of domains is critical for the design of targeting constructs based on scaffold proteins. Full article

(This article belongs to the Special Issue The Role of Nuclear Medicine in Cancer Diagnosis and Therapy)

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