Nuclear medicine and biology · 2020
Novel radiogallium-labeled pyridyl benzofuran derivative for detection of amylin aggregates in pancreas.
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Watanabe Hiroyuki, Kawano Kiyoshiro, Iikuni Shimpei, Shimizu Yoichi, Ono Masahiro
Аннотация
INTRODUCTION: The deposition of islet amyloid composed of amylin aggregates is related to β-cell mass dysfunction in type 2 diabetes mellitus (T2DM), and it may be involved in the development and progression of T2DM. In this study, we newly designed, synthesized, and evaluated a radiogallium-labeled pyridyl benzofuran derivative ([67/68Ga]GPBF) as an amylin imaging probe.
METHODS: An in vitro competitive inhibition assay was performed to determine the binding affinity for amylin aggregates. An in vitro autoradiographic study was carried out using pancreatic sections from a T2DM patient. A biodistribution of [67Ga]GPBF in normal mice was evaluated. Finally, we carried out ex vivo autoradiography using mouse transplanted with amylin aggregates.
RESULTS: GPBF exhibited binding affinity for amylin aggregates in vitro. In addition, [67Ga]GPBF clearly labeled islet amyloids in in vitro autoradiography of a T2DM pancreatic section. In a biodistribution study using normal mice, [67Ga]GPBF showed initial uptake into the pancreas, but non-specific accumulation in the liver, spleen, and pancreas was also observed. Furthermore, an ex vivo autoradiogram demonstrated that [67Ga]GPBF bound to amylin aggregates in the pancreas of the amylin aggregate-transplanted mice.
CONCLUSIONS: These results provide useful insights into the development of radiogallium labeled probes that target amylin aggregates in the T2DM pancreas.
METHODS: An in vitro competitive inhibition assay was performed to determine the binding affinity for amylin aggregates. An in vitro autoradiographic study was carried out using pancreatic sections from a T2DM patient. A biodistribution of [67Ga]GPBF in normal mice was evaluated. Finally, we carried out ex vivo autoradiography using mouse transplanted with amylin aggregates.
RESULTS: GPBF exhibited binding affinity for amylin aggregates in vitro. In addition, [67Ga]GPBF clearly labeled islet amyloids in in vitro autoradiography of a T2DM pancreatic section. In a biodistribution study using normal mice, [67Ga]GPBF showed initial uptake into the pancreas, but non-specific accumulation in the liver, spleen, and pancreas was also observed. Furthermore, an ex vivo autoradiogram demonstrated that [67Ga]GPBF bound to amylin aggregates in the pancreas of the amylin aggregate-transplanted mice.
CONCLUSIONS: These results provide useful insights into the development of radiogallium labeled probes that target amylin aggregates in the T2DM pancreas.