Rosiglitazone in the assistance of metabolic control during olanzapine administration in schizophrenia: a pilot double-blind, placebo-controlled, 12-week trial.

INTRODUCTION: Excessive body weight gain (BWG), hyperglycemia and dyslipidemia are important side effects of olanzapine. We assessed the effects of rosiglitazone on BWG, the insulin resistance index (HOMA-IR), lipids, glycated hemoglobin and fibrinogen in olanzapine-treated schizophrenia patients. METHODS: Thirty patients taking olanzapine (10-20 mg daily for 8 months) were randomly allocated to rosiglitazone (n=15; 4 to 8 mg daily) or placebo (n=15) in a 12-week double-blind protocol. Anthropometric and biochemical variables were evaluated at baseline, weeks 6 and 12. RESULTS: The rosiglitazone and placebo groups gained 3.2+/-4.5 and 2.2+/-2.3 kg, respectively (p=0.65). Insulin and the HOMA-IR significantly decreased after rosiglitazone (p<0.05). Rosiglitazone did not improve the lipid profile, fibrinogen and Hb1c levels. DISCUSSION: The positive impact of rosiglitazone was limited to improved glycemic control. It cannot be recommended for metabolic control during olanzapine treatment.

Laparoscopic pancreatic surgery in patients with chronic pancreatitis.

BACKGROUND: In recent years, technological advances and technical refinements to laparoscopic instruments have encouraged some surgeons to explore the application of laparoscopic methods to benign disorders of the pancreas. The aim of this report was to evaluate the feasibility and outcome of laparoscopic pancreatic surgery in patients with chronic pancreatitis. METHODS: One group of five patients with disease of nonalcoholic origin localized in the body-tail of the pancreas underwent distal pancreatectomy with preservation of the splenic vessels; a second group of six patients with symptomatic pancreatic pseudocysts (alcoholic origin in four cases and idiopathic in two cases) underwent laparoscopic transgastric drainage. For distal pancreatectomy and spleen salvage, the patient's positioning was half-lateral decubitus with the left side up. Four ports were used. A comparison was made with 41 patients with chronic, pancreatitis who underwent conventional open distal pancreatectomy. For the patients with laparoscopic distal pancreatectomy, the mean operative time was 4 h (range 3-5). RESULTS: There were no pancreatic-related complications, but one patient was reoperated for perforation of duodenal ulcer. The mean hospital stay was 6 days and the mean time to resume normal daily activities was 3 weeks. Laparoscopic pseudocyst drainage was performed in four patients via laparoscopic anterior gastrostomy and two patients via laparoscopic intraluminal cystogastrostomy. The mean operative time was 100 min (range 60-160). There was no morbidity. The mean hospital stay was 5 days, and the mean time to resume normal daily activities was 2 weeks. CONCLUSION: This study provides information about the possibilities of performing laparoscopic surgery in patients with chronic pancreatitis. Laparoscopic distal pancreatectomy with preservation of the splenic vessels and laparoscopic transgastric drainage are feasible and safe techniques. They offer obvious advantages, such as reduction of the parietal damage to the abdomen, a shorter hospital stay, and an earlier postoperative recovery than can be obtained with conventional open pancreatic resection.

Substance use among resident doctors in Venezuela.

This study was aimed to develop a self-administered questionnaire to detect substance use disorders based on the Spanish version of the Diagnostic Interview Schedule (DIS) and to evaluate the frequency of substance abuse and/or dependence among resident physicians of a large university hospital in Venezuela. The questionnaire showed a high concordance with the clinical diagnoses. Frequency of substance abuse and dependence was evaluated among 191 resident doctors. The frequencies of lifetime diagnoses were: tobacco dependence: 20.9%; alcohol abuse: 11%; alcohol dependence: 0.5%; drug abuse: 1% and drug dependence: 1%; non-pathological use of drugs: 20.4%.

The 1,4-beta-D-glucan glucanohydrolases from Phanerochaete chrysosporium. Re-assessment of their significance in cellulose degradation mechanisms.

A physico-chemical, functional and structural characterization, including partial sequence data, of three major 1,4-beta-D-glucan glucanohydrolases (EC. 3.2.1.4) isolated from the culture filtrate of the white-rot fungus Phanerochaete chrysosporium, shows that all three enzymes belong to a single family of cellulases. EG44, pI 4.3, (named after its apparent molecular mass in kDa), shows a clear homology with Schizopyllum commune Endoglucanase I (EGI); whereas EG38, pI 4.9, (named in the same manner) is related more closely to Trichoderma reesei (Trichoderma longibrachiatum) Endoglucanase III (EGIII). EG36, pI 5.6-5.7, is probably an EG38 protein lacking its cellulose binding domain. Strong synergistic action is induced by the enzymes acting in concert with cellobiohydrolases (CBHI and CBHII) from the same organism, indicating a highly effective enzymatic system for cellulose degradation. Controlled proteolysis with papain has allowed a so far unique cleavage of endoglucanases EG44 and EG38 into two domains: a core protein, which virtually lacks the capacity to absorb onto microcrystal-line cellulose but retains full catalytic activity against carboxymethyl cellulose and low molecular weight soluble substrates; and a peptide fragment corresponding to the cellulose binding domain. The latter appears to be of paramount significance in the mechanisms involved in the hydrolysis of microcrystalline cellulose.

The 1,4-beta-D-glucan cellobiohydrolases from Phanerochaete chrysosporium. I. A system of synergistically acting enzymes homologous to Trichoderma reesei.

A physico-chemical and structural characterization of three 1,4-beta-D-glucan cellobiohydrolases (EC. 3.2.1.91), isolated from a culture filtrate of the white-rot fungus Phanerochaete chrysosporium, reveals that the cellulolytic enzyme secretion pattern and thus the general degradation strategy for P. chrysosporium is similar to that of Trichoderma reesei. Partial sequence data show that two of the isolated enzymes, i.e., CBHI, pI 3.82 and CBH62, pI 4.85, are homologous with CBHI and EGI from T. reesei; while, the third, i.e., CBH50, pI 4.87, is homologous to T. reesei CBHII. Limited proteolysis with papain cleaved each of the three enzymes into two domains: a core protein which retained full catalytic activity against low molecular weight substrates and a peptide fragment corresponding to the cellulose binding domain, in striking similarity to the structural organization of T. reesei. CBHI and CBH62 have their binding domain located at the C-terminus, whereas in CBH50 it is located at the N-terminus. It is evident that synergistically acting cellobiohydrolases is a general requirement for efficient hydrolysis of crystalline cellulose by cellulolytic fungi.

Cellobiose oxidase from Phanerochaete chrysosporium can be cleaved by papain into two domains.

Cellobiose oxidase from the white rot fungus Phanerochaete chrysosporium has been purified to homogeneity by a new method. The enzyme has been cleaved by papain into two fragments: one containing the heme group and one containing the flavin group. The flavin fragment can oxidize cellobiose and is reoxidized by oxygen. Cellobiose oxidase binds to cellulose to approximately the same extent as cellobiohydrolase I. The cellulose-binding site is located on the flavin domain. The enzyme cannot be totally displaced from cellulose by cellobiose, and it is still active when adsorbed to cellulose. The possible role of the enzyme in lignocellulose degradation is discussed.