Total uterine prolapse complicated with vesicovaginal fistula: A case report.

RATIONALE: Vesicovaginal fistula (VVF) most commonly occurs due to iatrogenic injury during surgery or obstructed labor. We report a rare case of a patient with severe pelvic organ prolapse who developed VVF even though pessary had not been used. PATIENT CONCERNS: A 63-year-old postmenopausal woman, para 3 (all spontaneous vaginal deliveries), complained of vaginal bulging sensation and involuntary urinary leakage for 3 years. DIAGNOSIS: Stage IV uterine prolapse with VVF. INTERVENTIONS: She underwent transvaginal VVF repair combined with total vaginal hysterectomy and sacrospinous ligament fixation. The postoperative course was uncomplicated. OUTCOMES: The patient remained free of complications during the 1-year follow-up. LESSONS: This case illustrates the point that patients with pelvic organ prolapse (POP) should be treated promptly and careful follow-up should be conducted. Clinicians should be aware of the symptoms of VVF to ensure its early diagnosis and treatment.

USP11 regulates p53 stability by deubiquitinating p53.

The p53 tumor suppressor protein coordinates the cellular responses to a broad range of cellular stresses, leading to DNA repair, cell cycle arrest or apoptosis. The stability of p53 is essential for its tumor suppressor function, which is tightly controlled by ubiquitin-dependent degradation primarily through its negative regulator murine double minute 2 (Mdm2). To better understand the regulation of p53, we tested the interaction between p53 and USP11 using co-immunoprecipitation. The results show that USP11, an ubiquitin-specific protease, forms specific complexes with p53 and stabilizes p53 by deubiquitinating it. Moreover, down-regulation of USP11 dramatically attenuated p53 induction in response to DNA damage stress. These findings reveal that USP11 is a novel regulator of p53, which is required for p53 activation in response to DNA damage.

[Purification and characterization of hemolymph lectin from Tegillarca granosa Linnaeus].

Agglutinin with hemagglutinating activity was found in hemolymph of Tegillarca granosa Linnaeus. By extraction, fraction with saturated ammonium sulfate precipitation, gel filtration on Sephadex G-100 and followed by affinity chromatography on Sepharose 4B, an agglutinin was purified from the hemolymph of T. granosa. The purified lectin contains 5.02% neutral saccharide. The molecular weights is about 123 KDa, which showed 2 bands on SDS-PAGE, and the relative molecular weights of these subunits were 15 KDa and 16 KDa, respectively. In its amino acid composition, Asp has the highest content, followed by Glu and His, but there is a lack of Met. Assays for erythrocyte agglutination and sugar inhibition were done in microtiter plates. The result indicared that TGL-hemolymph could agglutinate erythrocytes from the natural and enzyme-treated erythrocytes of human and animals, and the highest activity was found in the agglutination with rabbit erythrocytes. The agglutinic activity of TGL-hemolymph was inhibited by lactose and D-galactose. The hemagglutination activity of TGL-hemolymph depended on Ca2+, and it showed the highest hemagglutination activity in pH 7.0. Thermostability was not high. The agglutinating activities changed from 2(5) to 2(1) between 30-70 degrees C, and was completely destroyed beyond 80 degrees C.