The authors believe that the open approach with a blunt trocar is most important in helping to avoid complications in pediatric laparoscopy.
The hospital records of patients who underwent splenectomy during the last 2 years were reviewed to compare the advantages of the laparoscopic approach with traditional open splenectomy (OS). Between March 1994 and March 1996, 16 children underwent splenectomy, in 8 using an open approach and 8 by a laparoscopic procedure. Of the patients who underwent laparoscopic splenectomy (LS), 2 had a concomitant cholecystectomy. Ages ranged between 4 and 11 years (mean 6.4 years); there were 9 girls and 7 boys. The indications for splenectomy were: hereditary spherocytosis (7 cases); idiopathic thrombocytopenic purpura (4); sickle-cell disease (3); and beta-thalassemia (2). The average operating time for OS was 100 min (range, 50-155), for LS 170 min (range 125-240). The hospital stay for patients who had OS ranged from 3 to 9 days (mean 4.7), for those who had LS from 2 to 5 days (mean 3). One OS patient developed a wound infection. In 3 of the LS patients, the spleen was removed via a 7-cm Pfannenstiel minilaparotomy in the suprapubic region; in 5 cases the spleen was captured into an extraction bag, crushed, and removed through the umbilical orifice. The authors believe that LS must be performed only when it is possible to use the extraction bag to remove the spleen from the umbilical orifice (spleens weighing less than 700 g) and when a concomitant procedure such as cholecystectomy is indicated; in other cases OS is preferable.
Our case shows that an intestinal invagination due to Bean syndrome is extremely rare in pediatric patients but possible. In the emergency, laparoscopy seems to be a safe and effective procedure to confirm the diagnosis and to perform the disinvagination mini-invasivally. In addition, laparoscopy permits to have a clear picture of other intra-abdominal lesions linked to Bean syndrome.
One-trocar laparoscopic surgery can be considered as the ideal procedure in case of abdominal complications of VPS in children with hydrocephalus.
In this work, we sought to determine whether the components of the murine polyomavirus capsid establish specific interactions with the minichromosome encapsidated into the mature viral particles by using the cis-diamminedichloroplatinum(II) cross-linking reagent. Our data indicated that VP1, but not minor capsid proteins, interacts with the viral genome in vivo. In addition, semiquantitative PCR assays performed on cross-linked DNA complexes revealed that VP1 binds to all regions of the viral genome but significantly more to the regulatory region. The implications of such an interaction for viral infectivity are discussed.The murine polyomavirus (Py) genome is organized into a minichromosome that is formed from a supercoiled circular double-stranded 5.3-kb DNA molecule with which cellular histones are associated (15). This chromatin is encapsidated into an icosahedral capsid composed of 72 pentamers of the major capsid protein VP1, with each pentamer being associated with minor capsid protein VP2 or VP3 (15). Several functions in the lytic life cycle, other than the structural one, have been assigned to the capsid proteins. The VP1 protein mediates the initial attachment and entry into host cells through interaction with sialic acids and integrins (2,8,20,42,43), and VP2 has been proposed to participate in viral cell entry (11,28,39). In addition, previous characterizations of Py mutants of the VP1 DE loop have also suggested a role for VP1 in viral growth control (22,29,38). Indeed, at early times postinfection, VP1 appears to colocalize with the infecting viral minichromosome in the cell nucleus and, in particular, at the nuclear matrix (NM), where viral transcription and replication take place (5,10,14). The finding that VP1 interacts with the NM regulatory protein YY1 early after infection suggests that VP1 may be required to anchor viral genomes to the NM for the formation of protein complexes that are necessary for early transcription (35). In accordance with this hypothesis, previous reports aimed at studying the potential interactions between capsid proteins and DNA have demonstrated that VP1, but not the minor coat proteins, is able to bind DNA through a DNAbinding domain (DBD) mapped within its first seven N-terminal residues (9, 31). These experiments were performed with an in vitro method and thus did not allow the attribution of any DNA sequence specificity to the DBD of VP1, as VP1 binds all Py and non-Py DNA sequences with equivalent high affinities (9, 31). The aim of the present work was to determine whether the components of the Py capsid establish interactions with the minichromosome encapsidated into the mature viral particles and, if so, with what specificity. For this purpose, we decided to treat mature Py virions with the cis-diamminedichloroplatinum(II) (cis-DDP) reagent, a molecule that produces inter-and intra-DNA strand cross-links independently of the sequence (6, 25, 37) and preferentially induces cross-links between DNA and nonhistone proteins located within a distance of 4 Å (16,27...
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