Comparison of percutaneous ablation and hepatectomy for liver metastasis: A single center retrospective study.

AIM: To investigate the current treatment for liver metastasis and clarify the indications for percutaneous thermal ablation for liver metastasis. METHODS: Ninety-two patients were enrolled and retrospectively analyzed. The patients underwent hepatectomy and/or percutaneous thermal ablation for liver metastases between January 2012 and December 2018. Twenty-six patients who underwent ablation treatment and seven patients who underwent both ablation and hepatectomy were included in the ablation treatment group (group A). We compared these patients with 59 patients who underwent hepatectomy only (group H). Subgroup analyses were performed between ablation (group AC) for colorectal liver metastasis and hepatectomy (group HC) for colorectal liver metastasis in 17 and 53 patients, respectively. RESULTS: The percentage of liver metastases other than colorectal cancer in group A was higher than that in the group H. Maximum tumor size in group A was significantly smaller than that in group H. Similarly, the patients in group AC were significantly older and demonstrated higher total bilirubin, lower serum albumin, and lower platelet counts than those in group HC. Overall survival was poorer in the AC group than that in the HC group. However, no differences were observed at metastasis ≤2 cm in size. CONCLUSIONS: Percutaneous thermal ablation was performed for many cancer types than hepatectomy. It is performed in elderly patients. We suggested that ablation for colorectal liver metastasis sized ≤2 cm is a suitable indication.

Selective O-Acylation of Enol Silyl Ethers with Acyl Fluorides Catalyzed by Fluoride Ions Derived from Potassium Fluoride and 18-Crown-6.

The fluoride ion-catalyzed selective O-acylation of enol silyl ethers with acyl fluorides using KF and 18-Crown-6 is described herein. This catalytic system facilitated the practical and facile reaction of a variety of enol silyl ethers derived from aromatic/aliphatic ketones and aldehydes with acyl fluorides to afford useful and valuable enol esters.

[A case of pancreatic pseudocyst associated with pancreatic cancer successfully treated with endoscopic pseudocyst drainage, which allowed continuation of chemotherapy].

We report a case of pancreatic pseudocyst associated with pancreatic cancer that was successfully treated with endoscopic pseudocyst drainage, which allowed continuation of chemotherapy. A 74-year-old woman complaining of jaundice was diagnosed with locally advanced cancer in the head of the pancreas, and she underwent chemotherapy with gemcitabine. One month later, she was admitted to our hospital for severe epigastralgia, and she diagnosed with a pancreatic pseudocyst that was 14 cm in diameter. Endoscopic ultrasonography-guided pseudocyst drainage was successfully performed. The amylase concentration of pseudocyst fluid was 13,320 U/L, and bacterial culture was negative. The epigastralgia soon resolved, but 1 week later, the size of the pseudocyst was 12 cm in diameter. Endoscopic retrograde pancreatography revealed communication of the pancreatic duct with the pseudocyst. A pancreatic stent was placed. The patient again underwent chemotherapy for 3 months, without major complications. The pseudocyst was no longer visible 3 months after stent placement. The patient died of pancreatic cancer with peritonitis carcinomatosa, 6 months after the initial diagnosis.

Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk.

H(+)-transporting ATP synthase is a multi-subunit enzyme involved in the production of ATP, which is an essential molecule for living organisms as a source of energy. Archaeal A-type ATPase (A-ATPase) is thought to act as a functional ATP synthase in archaea and is thought to have chimeric properties of F-ATPase and V-ATPase. Previous structural studies of F-ATPase indicated that the major nucleotide-binding subunits alpha and beta consist of three domains. The catalytic nucleotide-binding subunit A of V/A-ATPase contains an insertion of about 90 residues which is absent from the F(1)-ATPase beta subunit. Here, the first X-ray structure of the catalytic nucleotide-binding subunit A of an A(1)-ATPase is described, determined at 2.55 A resolution. A(1)-ATPase subunit A from Pyrococcus horikoshii consists of four domains. A novel domain, including part of the insertion, corresponds to the 'knob-like structure' observed in electron microscopy of A(1)-ATPase. Based on the structure, it is highly likely that this inserted domain is related to the peripheral stalk common to the A- and V-ATPases. The arrangement of this inserted domain suggests that this region plays an important role in A-ATPase as well as in V-ATPase.

Crystallization and preliminary X-ray diffraction study of the catalytic subunit of archaeal H+ -transporting ATP synthase from Pyrococcus horikoshii OT3.

H+ -transporting ATP synthase (H+ -ATPase) is a multi-subunit complex which acts to produce ATP molecules. The catalytic subunit A of the archaeal-type H+ -ATPase from Pyrococcus horikoshii OT3 was cloned, expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method with MPD as a precipitant. X-ray intensity data were collected to 2.55 A resolution at beamline BL41XU of SPring-8. The crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 128.0, c = 104.7 A, and contain one molecule per asymmetric unit.