Defining Voiding Dysfunction in Women: Bladder Outflow Obstruction Versus Detrusor Underactivity.

Purpose: We aimed to develop urodynamic criteria to improve the accuracy of the diagnosis of bladder outlet obstruction (BOO) and detrusor underactivity (DU) in women with lower urinary tract symptoms (LUTS).

Methods: Initially, in a group of 68 consecutive women with LUTS and increased postvoid residual (PVR) who had undergone urodynamic investigations, we examined the level of agreement between the operating physician's diagnosis of BOO or DU and the diagnosis according to urodynamic nomograms/indices, including the Blaivas-Groutz (B-G) nomogram, urethral resistance factor (URA), bladder outlet obstruction index (BOOI), and bladder contractility index (BCI). Based on the initial results, we categorized 160 women into 4 groups using the B-G nomogram and URA (group 1, severe-moderate BOO; group 2, mild BOO and URA≥20; group 3, mild BOO and URA<20; group 4, nonobstructed) and compared the urodynamic parameters.

Characterization of VP22 in herpes simplex virus-infected cells.

We examine biochemical characteristics of the herpes simplex virus (HSV) tegument protein VP22 by gel filtration, glycerol sedimentation, and chemical cross-linking experiments and use time course radiolabeling and immunoprecipitation assays to analyze its synthesis and interaction with other infected-cell proteins. VP22 was expressed as a delayed early protein with optimal synthesis requiring DNA replication. In immunoprecipitation assays, VP22 was found in association with several additional proteins including VP16 and a kinase activity likely to be that of UL13.

VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells.

In addition to its function as a powerful transactivator of viral immediate-early transcription, VP16 is an essential component of the herpes simplex virus (HSV) virion. As such, VP16 is introduced into cells, to effect its function in transactivation, as part of the virus tegument. Here we examine the potential for VP16 protein-protein interactions specific to virus-infected cells and show that VP16 copurifies in a highly enriched fraction with a single major polypeptide which we identify as the virus-encoded structural protein VP22.