Outpatient vs inpatient total laparoscopic hysterectomy: A randomized controlled trial.

INTRODUCTION: The objective of the study was to investigate whether outpatient total laparoscopic hysterectomy (TLH) could be performed as a routine without compromising patient satisfaction. The main outcomes were patient satisfaction with length of hospital stay, quality of life, complications and readmissions, and time to return to work. MATERIAL AND METHODS: A non-blinded prospective randomized controlled trial (Canadian Task Force classification I) performed in a single-center teaching hospital in Denmark. A total of 204 women scheduled for TLH on benign indication were randomized to same-day discharge or overnight stay after TLH. Visual analogue scales (VAS), a validated questionnaire EQ-5D, and a diary were filled in pre- and postoperatively. VAS scores on satisfaction with length of hospital stay and pain were administered taken with the EQ-5D and the diary during a follow up over 4 weeks. Student's t test, Chi-square and non-parametric statistics were used for analysis. The study was registered with ClinicalTrials.gov #NCT02933047. RESULTS: A total of 204 women gave informed consent and 203 underwent surgery (101 outpatient and 102 inpatient women). Complete data were available for 76 women in the outpatient group and 86 women in the inpatient group. There were no differences in baseline characteristics. No group differences were found in satisfaction with length of hospital stay (P = 0.35). The EQ-5D revealed no difference in patient satisfaction. However, one-third in the outpatient group chose overnight stay without medical indication. The groups were comparable in clinical outcomes. Sick leave was longer in the outpatient group regardless of the actual treatment (P = 0.015). CONCLUSIONS: Routine outpatient TLH implies that one-third of the patients stay overnight if this option is available without medical indication. Within this context the procedure can be performed with high patient satisfaction, but may lengthen the time to return to work.

Hysterectomy is not associated with de-novo urinary incontinence: A ten-year cohort study.

OBJECTIVE: To determine prevalence, incidence proportion, and changes of urinary incontinence (UI) 10-13 years after hysterectomy compared to two control groups. STUDY DESIGN: A longitudinal cohort study of 661 women with follow-up for ten years. Originally, 866 women answered a questionnaire on continence status preoperatively. Ten years postoperatively the queries were repeated in 371 with a hysterectomy, 89 with laparoscopic cholecystectomy (LC), and 201 with transcervical endometrial resection (TCRE). Significant incontinence was UI at least once a week. The main outcome measures were prevalence and incidence proportions of UI. RESULTS: The overall prevalence of stress UI ten years after surgery was 23% compared to 12% preoperatively. Urge UI was prevalent in 12% compared to 5% preoperatively. Incidence proportions of stress UI were in hysterectomies 21%, in LC 15%, and in TCRE 18%. Similarly, incidence proportions of urge UI were in hysterectomies 11%, in LC 11%, and in TCRE 8%. No significant differences between surgical procedures were found; however, we found substantial amount of changes in continence status from continent to incontinent and vice versa in all three groups. CONCLUSIONS: No significant difference was found after hysterectomy compared to controls in the prevalence or incidence proportions of UI after 10 years follow-up. Hysterectomy is not a risk factor of UI.

Successful desensitization to cetuximab in a patient with a positive skin test to cetuximab and specific IgE to alpha-gal

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KORRIGAN1 and its aspen homolog PttCel9A1 decrease cellulose crystallinity in Arabidopsis stems.

KORRIGAN1 (KOR1) is a membrane-bound cellulase implicated in cellulose biosynthesis. PttCel9A1 from hybrid aspen (Populus tremula L. x tremuloides Michx.) has high sequence similarity to KOR1 and we demonstrate here that it complements kor1-1 mutants, indicating that it is a KOR1 ortholog. We investigated the function of PttCel9A1/KOR1 in Arabidopsis secondary growth using transgenic lines expressing 35S::PttCel9A1 and the KOR1 mutant line irx2-2. The presence of elevated levels of PttCel9A1/KOR1 in secondary walls of 35S::PttCel9A1 lines was confirmed by in muro visualization of cellulase activity. Compared with the wild type, 35S::PttCel9A1 lines had higher trifluoroacetic acid (TFA)-hydrolyzable glucan contents, similar Updegraff cellulose contents and lower cellulose crystallinity indices, as determined by (13)C solid-state nuclear magnetic resonance (NMR) spectroscopy. irx2-2 mutants had wild-type TFA-hydrolyzable glucan contents, but reduced Updegraff cellulose contents and higher than wild-type cellulose crystallinity indices. The data support the hypothesis that PttCel9A1/KOR1 activity is present in cell walls, where it facilitates cellulose biosynthesis in a way that increases the amount of non-crystalline cellulose.

Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-beta-glucanases.

1H NMR spectroscopy has been used to analyze the product profiles arising from the hydrolysis of cellooligosaccharides by family GH9 cellulases. The product profiles obtained with the wild type and several active site mutants of a bacterial processive endoglucanase, TfCel9A, were compared with those obtained by a randomly acting plant endoglucanase, PttCel9A. PttCel9A is an orthologue of the Arabidopsis endocellulase, Korrigan, which is required for efficient cellulose biosynthesis. As expected, poplar PttCel9A was shown to catalyze the degradation of cellooligosaccharides by inversion of the configuration of the anomeric carbon. The product analyses showed that the number of interactions between the glucose units of the substrate and the aromatic residues in the enzyme active sites determines the point of cleavage in both enzymes.

[Clinical aspects and endoscopic management of gastrointestinal bleeding from Dieulafoy's lesion]. / Aspectos clínicos y tratamiento endoscópico de la hemorragia digestiva por lesión de Dieulafoy.

OBJECTIVE: the aim of the study was to assess the incidence, clinical presentation, location, and response to endoscopic therapy of gastrointestinal bleeding from Dieulafoy's lesion. MATERIAL AND METHOD: ALL consecutive episodes of gastrointestinal bleeding due to Dieulafoy's lesion seen between 2000 and 2006 were retrospectively reviewed. All main clinical and endoscopic data were collected: type and effectiveness of endoscopic therapy, rebleeding, complications, and mortality during hospitalization. RESULTS: WE found 41 patients, 26 males and 15 females, median age of 71.19 years. Dieulafoy's lesion accounted for 1.55% of all gastrointestinal bleeding episodes during the study period. The incidence of Dieulafoy's lesion was 2.2 cases/100.000 inhabitants/year. Active bleeding at endoscopy was present in 85.36%, and comorbidity in 92.68%. The stomach was the most frequent location (60.97%), followed by duodenum (29.26%). Endoscopic therapy achieved initial hemostasis in all cases. Three patients (7.31%) initially treated with epinephrine injection showed rebleeding and properly responded to a second session of endoscopic therapy. No surgery was needed. The mortality rate during hospitalization was 4.87%. CONCLUSIONS: Dieulafoy's lesion is an uncommon, but potentially severe cause of gastrointestinal bleeding. It may be found in any location within the gastrointestinal tract. Endoscopic therapy is effective and safe. Injected epinephrine alone is associated with a higher risk of rebleeding.

Recombinant expression and enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides.

PttCel9A is a membrane-bound, family 9 glycosyl hydrolase from Populus tremula x tremuloides that is upregulated during secondary cell wall synthesis. The catalytic domain of PttCel9A, Delta(1-105)PttCel9A, was purified, and its activity was compared to TfCel9A and TfCel9B from Thermobifida fusca. Since aromatic amino acids involved in substrate binding at subsites -4, -3, and -2 are missing in PttCel9A, the activity of TfCel9A mutant enzymes W256S, W209A, and W313G was also investigated. Delta(1-105)PttCel9A hydrolyzed a comparatively narrow range of polymeric substrates, and the preferred substrate was (carboxymethyl)cellulose 4M. Moreover, Delta(1-105)PttCel9A did not hydrolyze oligosaccharides shorter than cellopentaose, whereas TfCel9A and TfCel9B hydrolyzed cellotetraose and cellotriose, respectively. These data suggest that the preferred substrates of PttCel9A are long, low-substituted, soluble cellulosic polymers. At 30 degrees C and pH 6.0, the kcat for cellohexaose of Delta(1-105)PttCel9A, TfCel9A, and TfCel9B were 0.023 +/- 0.001, 16.9 +/- 2.0, and 1.3 +/- 0.2, respectively. The catalytic efficiency (kcat/Km) of TfCel9B was 39% of that of TfCel9A, whereas the catalytic efficiency of Delta(1-105)PttCel9A was 0.04% of that of TfCel9A. Removing tryptophan residues at subsites -4, -3, and -2 decreased the efficiency of cellohexaose hydrolysis by TfCel9A. Mutation of W313 to G had the most drastic effect, producing a mutant enzyme with 1% of the catalytic efficiency of TfCel9A. The apparent narrow substrate range and catalytic efficiency of PttCel9A are correlated with a lack of aromatic amino acids in the substrate binding cleft and may be necessary to prevent excessive hydrolysis of cell wall polysaccharides during cell wall formation.