We report herein on the follow-up of ten consecutive patients who underwent perineal rectosigmoidectomy, and discuss the indications, surgical technique, and outcomes of this procedure. The median age of the patients was 79 years, with a range of 26 to 85 years, and eight patients had complicating medical conditions. Of five patients who underwent this procedure for a recurrent prolapse after another type of perineal procedure, four had previously undergone the Thiersch operation combined with the Gant-Miwa technique. The mean length of the excised rectum and sigmoid colon was 22.1 cm. Pain was minimal or absent in all patients and oral intake was commenced after 2 days. There were no mortalities, but anastomotic leakage occurred in one patient. The mean follow-up period was 3.5 years. Only one patient developed recurrent rectal prolapse 24 months after the operation. Of seven patients who underwent concomitant levatoroplasty for incontinence, five became fully continent within 3 weeks after the operation, while the remaining two improved after 2 months. We propose that perineal rectosigmoidectomy is indicated for patients who have suffered an early recurrence of prolapse after another transperineal repair; elderly or high-risk patients with incontinence; male patients; and patients with an incarcerated or gangrenous prolapsed rectal segment.

We carried out a prospective clinical trial of colon preparation with a regimen of oral antibiotics starting on the day before surgery. The patients were assigned to one of two groups consisting of either a mechanical preparation alone group (group 1, 45 cases) or a mechanical bowel preparation with oral antibiotics group (group 2, 38 cases). Group 2 received kanamycin and metronidazole three times on the day before surgery. Cefmetazole was administered for 3 consecutive days as prophylaxis in both groups. In a study using intraoperative mucosal swabs, the rates of group 2 patients with cultures yielding anaerobes or Gram-negative bacteria were significantly lower than those of group 1. There were no significant differences in the rates of patients with cultures yielding fungi or Gram-positive organisms. The positive culture rate in the peritoneal fluid of group 1 was also higher than that of group 2 (40%, 16%, P < 0.05). The surgical site infection rate was 18% in group 1 and 13% in group 2. Organisms isolated from the sites of postoperative infections were not identical with those from the peritoneal fluid. This relatively brief course preparation minimized the emergence of resistant strains. However, in spite of the colonic bacterial burden and the intraoperative inoculation in the patients with mechanical cleansing alone, their incidence of subsequent infections was comparable to that of patients who were administered oral antibiotics provided that the prophylactic antibiotic was administered for 3 days after surgery.

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ABSTRACT. A panel of chicken monoclonal antibodies (mAbs) was developed against prion protein (PrP), the sequence of which is a highly conserved molecule among mammals. A portion of the splenocytes from chickens immunized with recombinant mouse PrP was fused with the chicken B cell line, MuH1. The remaining splenocytes were used to generate the recombinant mAbs by phage display. A t otal of 36 anti-PrP mAbs, 2 from cell fusion and 34 from phage display were established. The specificity of these mAbs was determined by Western blot and ELISA using various PrP antigens including recombinant PrPs, synthetic PrP peptides and PrPs from brains or scr apieinfected neuroblastoma cell line. These mAbs were classified into three main groups, protease K (PK)-sensitive (Group I), PK cl eavage site proximal (Group II) and PK-resistant (Group III), based on their abilities to recognize PrP following PK-treatment. Some mAbs were found to selectively recognize different glycoforms of PrP as well as the metabolic fragments of PrP. Furthermore, we found that PrP recognition by chickens differed from that by PrP-knockout mouse. These results indicate that these newly generated PrP ant ibodies from chickens will help to research the PrP and to establish the diagnosis of prion disease. KEY WORDS: avian, panel mAb, prion protein.

Four monoclonal antibodies (MAbs) specific for prion protein (PrP) were generated by using PrP-knockout mice immunized with a scrapie-infected mouse neuroblastoma cell line (N2a/22L). The MAbs reacted with both the cellular form (PrP(C)) and the protease K-treated form (PrP(Sc)) on Western blotting. Of the four MAbs, three recognized mouse and hamster PrP, while the remaining MAb recognized mouse, sheep, and bovine PrPs. In addition, these MAbs were shown to react only with the unglycosylated and monoglycoslated forms of PrP(Sc) in N2a/22L, but reacted with all glycosylated forms of PrP(C) and PrP(Sc) from mouse brain. This study was the first to report the development of anti-PrP MAbs using scrapie-infected cells as an immunogen and provides one approach for the generation of PrP-specific MAbs.