Laparoscopic adenomectomy versus Eraser laser enucleation of the prostate.

PURPOSE: To evaluate functional outcomes and morbidity rates after laparoscopic adenomectomy (LA) and Eraser laser enucleation of the prostate (ELEP). MATERIALS AND METHODS: Forty patients with lower urinary tract symptoms suggesting bladder outlet obstruction, with a prostate heavier than 70 g on transrectal ultrasound, were selected to undergo laparoscopic adenomectomy or Eraser laser enucleation of the prostate. All patients were consecutively enrolled without randomization and assessed preoperatively, 3 and 6 months postoperatively. Baseline characteristics, perioperative data, and postoperative outcomes were compared. RESULTS: The total operating time was significantly longer in the LA group (138.8 ± 11.4 vs. 78.4 ± 10.0 min, p < 0.000001). Catheter removal was performed earlier (61.2 ± 21.3 vs. 174.0 ± 13.2 h, p < 0.000001) and the hospital stay was significantly shorter (62.4 ± 21.2 vs. 187.2 ± 12.6 h, p < 0.000001) in the ELEP group. The latter group experienced significantly less perioperative hemoglobin (Hb) loss (0.71 ± 0.25 vs. 2.15 ± 1.08 g/dl, p < 0.000001), and their postoperative Hb levels (14.1 ± 1.21 vs. 11.7 ± 1.31 g/dl, p < 0.000001) were significantly higher. The resected tissue was significantly greater in the LA group (58.5 ± 23.3 vs. 87.9 ± 22.4 g, p = 0.0002). Significant improvements in Qmax, Qol, and symptom scores from baseline to each follow-up time point were noted in both groups. No statistically significant difference in symptom scores or Qmax was registered between the LA and the ELEP group throughout the follow-up period. CONCLUSION: Laparoscopic adenomectomy and ELEP were equally effective for relieving bladder outflow obstruction and lower urinary tract symptoms. The advantages of ELEP include less blood loss, shorter catheterization times, and shorter hospital stays.

Tissue effects resulting from eraser laser enucleation of the prostate: in vivo investigation.

UNLABELLED: BACKGROUND/AIMS/OBJECTIVES: To describe the depth of the laser coagulation zone in vivo based on histological examinations and the functional outcome of a 1,318-nm diode laser for enucleation in benign prostatic enlargement (BPE). METHODS: A total of 20 patients with BPE were treated by laser Eraser® enucleation of the prostate (ELEP). Prostatic tissue wedges were evaluated to assess the depth of the ELEP coagulation zones. Additionally, patients were assessed preoperatively and 12 months postoperatively. RESULTS: The coagulation zones were 0.36 ± 0.17 mm in epithelial tissue, 0.28 ± 0.15 mm in stromal tissue, and 0.25 ± 0.12 mm in mixed tissue. The coagulation area at the cutting edge completely sealed capillary vessels, reaching a depth of 0.35 ± 0.15 mm. The diameter of the coagulated vessels measured 1.75 ± 0.83 mm. Mean blood loss was 115.54 ± 93.12 ml, catheter time 1.35 ± 0.33 days, and hospital stay 1.89 ± 0.52 days. The International Prostate Symptom Score, maximal flow rate, and quality of life significantly improved 12 months after the procedure. CONCLUSIONS: ELEP is safe and effective for BPE treatment and yields good results at a follow-up of 1 year. Because of the limited penetration depth, damage to the urinary sphincter is not expected.

Phosphorylation of period is influenced by cycling physical associations of double-time, period, and timeless in the Drosophila clock.

The clock gene double-time (dbt) encodes an ortholog of casein kinase Iepsilon that promotes phosphorylation and turnover of the PERIOD protein. Whereas the period (per), timeless (tim), and dClock (dClk) genes of Drosophila each contribute cycling mRNA and protein to a circadian clock, dbt RNA and DBT protein are constitutively expressed. Robust circadian changes in DBT subcellular localization are nevertheless observed in clock-containing cells of the fly head. These localization rhythms accompany formation of protein complexes that include PER, TIM, and DBT, and reflect periodic redistribution between the nucleus and the cytoplasm. Nuclear phosphorylation of PER is strongly enhanced when TIM is removed from PER/TIM/DBT complexes. The varying associations of PER, DBT and TIM appear to determine the onset and duration of nuclear PER function within the Drosophila clock.

double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation.

We have isolated three alleles of a novel Drosophila clock gene, double-time (dbt). Short- (dbtS) and long-period (dbtL) mutants alter both behavioral rhythmicity and molecular oscillations from previously identified clock genes, period and timeless. A third allele, dbtP, causes pupal lethality and eliminates circadian cycling of per and tim gene products in larvae. In dbtP mutants, PER proteins constitutively accumulate, remain hypophosphorylated, and no longer depend on TIM proteins for their accumulation. We propose that the normal function of DOUBLETIME protein is to reduce the stability and thus the level of accumulation of monomeric PER proteins. This would promote a delay between per/tim transcription and PER/TIM complex function, which is essential for molecular rhythmicity.

The Drosophila clock gene double-time encodes a protein closely related to human casein kinase Iepsilon.

The cloning of double-time (dbt) is reported. DOUBLETIME protein (DBT) is most closely related to human casein kinase Iepsilon. dbtS and dbtL mutations, which alter period length of Drosophila circadian rhythms, produce single amino acid changes in conserved regions of the predicted kinase. dbtP mutants, which eliminate rhythms of per and tim expression and constitutively overproduce hypophosphorylated PER proteins, abolish most dbt expression. dbt mRNA appears to be expressed in the same cell types as are per and tim and shows no evident oscillation in wild-type heads. DBT is capable of binding to PER in vitro and in Drosophila cells, suggesting that a physical association of PER and DBT regulates PER phosphorylation and accumulation in vivo.

An alternatively spliced Pit-1 isoform altered in its ability to trans-activate.

Although alternative splicing has been shown to give rise to isoforms of a number of transcription factors, such isoforms have not previously been detected for the POU homeodomain protein Pit-1. Screening of a rat pituitary GH3 cell cDNA expression library yielded a clone, termed pCMVPit-1a, encoding a 35.8 kD protein (Pit-1a) containing a 26 amino acid insert in the Pit-1 trans-activation domain. The position of the insert, plus Southern blot analysis, implied that Pit-1a mRNA arises by alternative splicing of the Pit-1 gene transcript. Pit-1a mRNA was detected in GH3 rat pituitary tumor cells at levels about 1/7 that of Pit-1 mRNA. Pit-1a mRNA-specific sequences were also detected in rat and mouse pituitary, and in mouse thyrotropic tumor TtT cells. DNA mobility shift assays showed that Pit-1a binds specifically to Pit-1 binding sites in the proximal prolactin promoter, but produces DNA-protein complexes of markedly different mobilities than Pit-1. In stably transfected CHO cells which accumulated approximately equal levels of either of the two proteins, Pit-1 trans-activated a prolactin promoter-driven CAT construct, while Pit-1a yielded no detectable transactivation, implying a trans-activation ratio for Pit-1a/Pit-1 of less than 0.05. Thus, the insertion of 26 amino acids of similar composition into the activation domain of Pit-1 has at once affected both the mode of binding of this protein and its ability to function as a trans-activator.

Elevated plasma cortisol levels during interferon-gamma treatment.

We investigated plasma levels of cortisol and ACTH in 9 patients with advanced metastatic tumors before and during treatment with interferon-gamma (IFN-gamma), 2-4 h after administration of IFN-gamma there was a sharp rise in plasma cortisol levels. The rise coincided with the onset of fever. Highest cortisol levels were reached 4-6 h after IFN-gamma injections, whereas IFN-gamma serum levels peaked 6-10 h after the IFN-gamma injections. Elevated cortisol levels during IFN-gamma treatment may be part of a homeostatic response of the neuroendocrine system to the immunological stimulus induced by IFN-gamma. On the other hand, the increased plasma levels of cortisol in response to pharmacological doses of IFN-gamma may dampen the in vivo effectiveness of IFN-gamma.