ABSTRACT
PURPOSE: To evaluate the urodynamic characteristics of a series of women with stress urinary incontinence presenting various rates of vaginal prolapse. METHODS: 92 female patients were included in this study, mean age was 48 years (range 29-75). All patients underwent urogynecologic physical examination (vaginal prolapse was graded) and complete urodynamic study in order to detect the presence of detrusor overactivity. Urodynamic terminology and measurements comply with the ICS (International Continence Society) standards. Statistical significance was established below 0.05. RESULTS: 65 women (70.6%) presented anterior vaginal prolapse and 31 (33.6%) posterior vaginal prolapse. Involuntary contractions of the detrusor muscle appeared in 13 patients (20%) who had an anterior vaginal prolapse and 6 women (19.3%) who had a posterior vaginal prolapse. The existence of involuntary contractions was not associated with the diagnosis of vaginal prolapse. CONCLUSION: Our study did not show any correlation between existence of vaginal prolapse and detrusor overactivity.
Subject(s)
Urinary Incontinence, Stress/complications , Urinary Incontinence, Stress/physiopathology , Uterine Prolapse/etiology , Adult , Aged , Female , Humans , Middle Aged , Prospective Studies , UrodynamicsABSTRACT
Two peptides with kinin-like biological properties were isolated by chromatography on a Sephadex G-10 column followed by high-performance liquid chromatography, from the venom of the spider Scaptocosa raptoria. The isolated peptides (peptide-S and peptide-R) were shown to cause contraction on the isolated guinea-pig ileum at amounts equivalent to those shown by bradykinin. Both peptides relaxed the isolated rat duodenum, increased the capillary permeability, caused decreasing and biphasic effect of the arterial blood pressure in conscious rats and induced oedema in the rat paw. The peptides had activity and structural similarities to other peptides (kinin-like) isolated from venoms. The complete amino acid analysis gave peptide-S a structure with 36 amino acid residues and peptide-R 22 amino acid residues. The mol. wts were estimated to be in the range of 4000 and 2870, respectively.