Deep-learning image reconstruction for 80-kVp pancreatic CT protocol: Comparison of image quality and pancreatic ductal adenocarcinoma visibility with hybrid-iterative reconstruction.

PURPOSE: To evaluate the image quality and visibility of pancreatic ductal adenocarcinoma (PDAC) in 80-kVp pancreatic CT protocol and compare them between hybrid-iterative reconstruction (IR) and deep-learning image reconstruction (DLIR) algorithms. METHOD: A total of 56 patients who underwent 80-kVp pancreatic protocol CT for pancreatic disease evaluation from January 2022 to July 2022 were included in this retrospective study. Among them, 20 PDACs were observed. The CT raw data were reconstructed using 40% adaptive statistical IR-Veo (hybrid-IR group) and DLIR at medium- and high-strength levels (DLIR-M and DLIR-H groups, respectively). The CT attenuation of the abdominal aorta, pancreas, and PDAC (if present) at the pancreatic phase and those of the portal vein and liver at the portal venous phase; background noise; signal-to-noise ratio (SNR) of these anatomical structures; and tumor-to-pancreas contrast-to-noise ratio (CNR) were calculated. The confidence scores for the image noise, overall image quality, and visibility of PDAC were qualitatively assigned using a five-point scale. Quantitative and qualitative parameters were compared among the three groups using Friedman test. RESULTS: The CT attenuation of all anatomical structures were comparable among the three groups (P = .26-.86), except that of the pancreas (P = .001). Background noise was lower (P <.001) and SNRs (P <.001) and tumor-to-pancreas CNR (P <.001) were higher in the DLIR-H group than those in the other two groups. The image noise, overall image quality, and visibility of PDAC were better in the DLIR-H group than in the other two groups (P <.001-.003). CONCLUSION: In 80-kVp pancreatic CT protocol, DLIR at a high-strength level improved image quality and visibility of PDAC.

NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers.

A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported to serve as an E3-type SUMO ligase for tumor suppressor p53 and its own. It also was proposed that the N-terminal domain of PIAS1 interacts with DNA as well as p53. Extensive biochemical studies have been devoted recently to understand sumoylations and its biological implications, whereas the structural aspects of the PIAS family and the mechanism of its interactions with various factors are less well known to date. In this study, the three-dimensional structure of the N-terminal domain (residues 1-65) of SUMO ligase PIAS1 was determined by NMR spectroscopy. The structure revealed a unique four-helix bundle with a topology of an up-down-extended loop-down-up, a part of which the helix-extended loop-helix represented the SAP (SAF-A/B, Acinus, and PIAS) motif. Thus, this N-terminal domain may be referred to as a four-helix SAP domain. The glutathione S-transferase pull-down assay demonstrated that this domain possesses a binding ability to tumor suppressor p53, a target protein for sumoylation by PIAS1, whereas gel mobility assays showed that it has a strong affinity toward A/T-rich DNA. An NMR analysis of the four-helix SAP domain complexed with the 16-bp-long DNA demonstrated that one end of the four-helix bundle is the binding site and may fit into the minor groove of DNA. The three-dimensional structure and its binding duality are discussed in conjunction with the biological functions of PIAS1 as a SUMO ligase.