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BACKGROUND Stoma prolapse is the full-thickness protrusion of bowel through a stoma, which occurs in 2% to 26% of colostomies. However, stoma prolapse complicated by small bowel incarceration is very rare, reported in only 3 cases thus far. To our knowledge, the present case is the first reported case of surgical treatment after preoperative manual reduction for small bowel incarceration. CASE REPORT A 74-year-old male who had undergone sigmoid end colostomy in the right lower abdomen by Hartmann's operation for rectal cancer visited our emergency room complaining of severe stoma prolapse. The prolapse was about 20×15×15 cm in size and showed edematous change. Enhanced computed tomography revealed a loop of the small bowel incarcerated within the prolapsed colostomy. After the severe prolapse was reduced to 15×10×10 cm in size with manual compression for small bowel incarceration, an emergency laparotomy made via a circumferential incision revealed a partially necrotic prolapsed sigmoid colon and 15-cm-long reddish small bowel loop in the abdominal cavity that needed to be preserved. A new sigmoid end colostomy was constructed in the right lower abdomen at the same site as the preoperative stoma. CONCLUSIONS It is important to remember that small bowel can herniate into a stoma prolapse, and when encountering the acute presentation of a large stoma prolapse, manual reduction of the incarcerated small bowel may help in selecting elective versus emergency surgery.

Background: Inferior mesenteric arterioportal fistula (APF) is rare as only 35 case reports in the literature. We herein presented a case of simultaneously double cancer in the rectum and stomach with inferior mesenteric APF, which is the first case report by searching using PubMed. Combination of interventional embolization and surgical operation seemed to be optimal treatment for avoiding postoperative complications and the curability., Case Presentation: A 66-year-old male with epigastric pain was admitted to a practitioner. He underwent a gastroscopy with biopsy, and cancer located in the lesser curvature of the gastric cardia was found. Enhanced CT did not reveal wall thickening of the stomach and distant metastases, but several swollen lymph nodes were observed in the right cardia. In the arterial phase, dilation of inferior mesenteric vein (IMV) and superior rectal artery (SRA) were noted, which raised suspicions of an arterioportal communication. Colonoscopy revealed a type 2 rectal tumor located 12 cm from the anal verge. The histological diagnosis of well-differentiated tubular adenocarcinoma was confirmed by biopsy. At a first step, we planned to perform a radiological embolization of inflow vessels to APFs except for SRA. Additionally, we determined the interval time of 1 month between the first low anterior rectal resection and the sequential gastrectomy for the purpose of decreasing portal pressure. The postoperative course was uneventful without hemorrhagic complications, and S-1 was taken internally 1 year as adjuvant chemotherapy for gastric cancer. The patient still lives without recurrence of this cancer with APF and portal vein thrombosis 2.5 years after the aforementioned surgeries., Conclusion: Inferior mesenteric APF and/or arteriovenous fistula (AVF) would be consisted of the several inflow arteries as superior rectal, internal iliac, and median sacral arteries, and outflow veins as inferior mesenteric, internal iliac, and median sacral veins. To determine the therapeutic strategy for left-sided colorectal cancers with abnormal vessel communications of the pelvis, it is significant to comprehend distribution and component vessels of APF and/or AVF.

Mitochondrial sterol 27-hydroxylase (EC 1.14.13.15) is an important enzyme, not only in the formation of bile acids from cholesterol intermediates in the liver but also in the removal of cholesterol by side chain hydroxylation in extrahepatic tissues. The enzyme has been assayed by complicated methods using radiolabeled substrates or deuterium-labeled tracers. These methods may be inaccurate for measuring enzyme activity, because the amount of electron-transferring proteins may be insufficient for maximal velocity. To solve this problem, after solubilization of the enzyme from rat liver mitochondria with n-octyl-beta-d-glucopyranoside (OGP), we measured the enzyme activity by incubating the solubilized enzyme with saturated amounts of electron-transferring proteins. In our assay system, using 7alpha-hydroxy-4-cholesten-3-one (HCO) as a substrate, we could easily measure the product, 7alpha,27-dihydroxy-4-cholesten-3-one, with HPLC monitoring absorbance at 240 nm. The product formation was proportionate to the time up to 5 min and the protein concentration up to 0.5 mg of protein/ml. The maximal velocity of the enzyme was 1.1 nmol/min/mg of protein, which was 4- to 16-fold higher than previously reported values. A simple and accurate assay method for sterol 27-hydroxylase in rat liver mitochondria is herein described.

An accurate assay method of 25-hydroxyvitamin D3 24-hydroxylase (24-hydroxylase) was established. Kidney mitochondria prepared from vitamin D-replete rats were treated with polyoxyethylenesorbitan monolaurate. The solubilized suspension was ultracentrifuged at 100,000g for 60 minutes and an aliquot of the supernatant was incubated under the saturating concentrations of substrate NADPH and the mitochondrial-type electron transferring proteins, adrenodoxin and NADPH-adrenodoxin reductase. Products were analyzed by high-performance liquid chromatography (HPLC) monitoring effluents at a wavelength of 265 nm. The maximal velocity of the enzyme in vitamin D-replete rats was 400 pmol/minute per mg of protein, which was considerably higher than those reported by previous authors who used intact kidney mitochondria as the enzyme source. In applying the new assay method, an interesting property was found; Michaelis constant of 24-hydroxylase for 25-hydroxyvitamin D3 [25(OH)D3] was 0.6 microM, which was 35-fold lower than that for 1alpha,25-dihydroxyvitamin D3 [1alpha,25(OH)2D3] which was 20.9 microM. This fact indicates that affinity of the enzyme to 25(OH)D3 is 35-fold higher than that to 1alpha,25(OH)2D3. These data suggest that 25(OH)D3 is the preferred substrate to 1alpha,25(OH)2D3.

We purified extensively 25-hydroxyvitamin D3 1alpha-hydroxylase (calcidiol, NADPH: oxygen oxidoreductase (1-hydroxylating), EC 1.14.13.13) from kidney mitochondria of rachitic rats and disclosed its peculiar properties as a P450. The final preparation was identified as a 55 kDa protein having an intense absorption at 417 nm characteristic of P450. The specific activity was 4.8 nmol/min/mg of protein indicating a 350-fold purification. Specific content of P450 was 1.1 nmol/mg of protein and turnover number was 4.4 min-1.