The surged faradic stimulation to the pelvic floor muscles as an adjunct to the medical management in children with rectal prolapse

<p>Abstract</p> <p>Background</p> <p>To assess the role of the surged faradic stimulation to the pelvic floor muscles as an adjunct to the conservative management in the children of idiopathic rectal prolapse</p> <p>Methods</p> <p><it>Study design</it>: Prospective</p> <p><it>Setting</it>: Pediatric Surgery Department, Pt BD Sharma, Post Graduate Institute of Medical Sciences, Rohtak</p> <p><it>Subjects</it>: 47 consecutive children with idiopathic rectal prolapse attending the Pediatric Surgery out patient department from July 2005 to June 2006</p> <p><it>Methodology</it>: The information pertaining to duration and the extent of rectal prolapse, predisposing or associated medical conditions, results of local clinical examination were noted. Surged faradic stimulation using modified intraluminal rectal probe, was given on the alternate days. The conventional conservative medical management was also continued. The extent of relief and the number of the sittings of faradic stimulation required were noted at various stages of follow-ups</p> <p><it>Statistical Methods</it>: Mean values between those completely cured and others; poor responders and others were compared with t-test and proportions were compared with Chi square test. The p-value < 0.05 was considered statistically significant.</p> <p>Results</p> <p>The mean number of sittings in the completely cured group (n = <b>28</b>(64%)) was (12.4 ± 7.8) and was comparable with very poor responder (n = 6(13%). There was higher percentage of relief (76%) at the first follow up (at 15 days) in completely cured Vs other (37%) and also the poor responders showed (20%) Vs other (68%) and was statistically significant.</p> <p>Conclusion</p> <p>With use of faradic stimulation, even the long-standing rectal prolapse can be fully cured. The follow up visit at 2 weeks is very important to gauge the likely success of this modality in treatment of the patients with rectal prolapse. Those showing poor response at this stage may require alternative treatment or take a long time to get cured</p

Single-point single-molecule FRAP distinguishes inner and outer nuclear membrane protein distribution

The normal distribution of nuclear envelope transmembrane proteins (NETs) is disrupted in several human diseases. NETs are synthesized on the endoplasmic reticulum and then transported from the outer nuclear membrane (ONM) to the inner nuclear membrane (INM). Quantitative determination of the distribution of NETs on the ONM and INM is limited in available approaches, which moreover provide no information about translocation rates in the two membranes. Here we demonstrate a single-point single-molecule FRAP microscopy technique that enables determination of distribution and translocation rates for NETs in vivo

Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor

The metazoan nuclear envelope breaks down in early mitosis and does not reform until late anaphase. Phosphorylation of lamin B receptor by Cdk1 not only prevents premature nuclear envelope assembly, but also facilitates complete dissociation of the nuclear envelope from the chromatin during nuclear envelope breakdown

Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin.

During division of metazoan cells, the nucleus disassembles to allow chromosome segregation, and then reforms in each daughter cell. Reformation of the nucleus involves chromatin decondensation and assembly of the double-membrane nuclear envelope around the chromatin; however, regulation of the process is still poorly understood. In vitro, nucleus formation requires p97 (ref. 3), a hexameric ATPase implicated in membrane fusion and ubiquitin-dependent processes. However, the role and relevance of p97 in nucleus formation have remained controversial. Here we show that p97 stimulates nucleus reformation by inactivating the chromatin-associated kinase Aurora B. During mitosis, Aurora B inhibits nucleus reformation by preventing chromosome decondensation and formation of the nuclear envelope membrane. During exit from mitosis, p97 binds to Aurora B after its ubiquitylation and extracts it from chromatin. This leads to inactivation of Aurora B on chromatin, thus allowing chromatin decondensation and nuclear envelope formation. These data reveal an essential pathway that regulates reformation of the nucleus after mitosis and defines ubiquitin-dependent protein extraction as a common mechanism of Cdc48/p97 activity also during nucleus formation