Errors in Medicine: perception of healthcare professionals in the Lazio Region.

INTRODUCTION: The error in medicine is always the subject of debate in the scientific debates. The purpose of this study is to evaluate the degree knowledge, attitudes and behaviors of health workers towards the error in the health sector. METHODS: A survey was carried out involving 435 health profes- sionals working in health facilities of the Lazio region, of which 312 females (71%) and 123 males (28%) with an age between 21 and 68 years. A structured questionnaire was administered for investigating the experiences and opinions about the errors found in medical prac- tice, the causes underlying them and the mistakes that should never be committed. Data were collected, stratified by sex, age, marital status, year of graduation, years of service and the workplace (medical or surgical). The statistical significance was set at p≤0.05. RESULTS: The 5 errors found more frequently in the clinical prac- tice by health professionals were as follows: errors related to the request for examination (60.9%); errors in the collection of samples (37.5%); errors relating to the delivery of the reports (35.2%); errors due to reporting of examinations (31.7%); errors of history (29.2%). The five cases considered to be the most frequently responsible for such errors were: disorganization (52%); fast (46.4%); tiredness due to excessive workloads, stress (44.6%); negligence and carelessness (41.6%); inattention (41.1). With regard to the errors that you should never commit they were more frequently: exchange of patient or misidentification of the patient (49.2%); administration errors of therapies or medications (47.6%); errors related to surgery (41.6%); errors of prescription therapies or medications (39.3); errors in the reporting of exams (33.6%). CONCLUSIONS: The results of this study shows the importance of a culture of error in medicine among healthcare professionals, those who have already gained practical experience in health care and therefore better able to perform a critical analysis and evaluation of the errors that occur every day. The continuous training of health professionals is fundamental for promoting patient safety and quality in the healthcare sector.

Infections in hospital departments. What is Hospital Responsibility?

Infections in hospitals still have a high incidence and many of them could be avoided through better welfare standards. To try to overcome them, a strategy based on prevention is needed, but cleaning, disinfection and sterilization procedures are also a key tool. It is important to provide for all healthcare professionals a constant update and the creation of protocols that take into account the technical, scientific and economic aspects, but also specific operational needs, so that the proposed solutions can be applied in daily routines. The authors outline the mandatory duties to the doctors and hospital and underline the need to document in the clinical record the treatments performed. In case of infections occurred in hospital environment, the patient must demonstrate the guilty nature of the hospital's conduct, the existence of a harm and the causal connection. The hospital must demonstrate that asepsis measures were adopted according to the actual scientific knowledge and they must cover not only the treatment but also the diagnosis, all the activities prior to surgery and the postoperative phase. The sentences examined show that hospitals can avoid being accused of negligence and imprudence only if they can prove that they have implemented all prophylaxis measures contained in the guidelines and protocols. They must demonstrate that the infection was caused by an unforeseeable event. While some initiatives to improve the quality of hospital care have already allowed a decrease in the incidence and cost of these infections, much remains to be done.

Iron and insulin resistance.

BACKGROUND: Preliminary clinical and experimental results suggest that iron can modify hepatocytes' insulin sensitivity by interfering with insulin receptor and intracellular insulin signalling. AIM: To evaluate in vivo the influence of iron on insulin resistance and insulin release in patients with non-alcoholic fatty liver disease and in vitro the interaction between iron and insulin sensitivity by analysing the effect of iron manipulation on insulin receptor expression in hepatoblastoma HepG2 cell line. RESULTS: Insulin resistance evaluated by homeostatis model assessment (HOMA)-insulin resistance significantly decreased after diet, and a further reduction was observed after phlebotomies. Iron depletion by desferrioxamine increased by twofold the 125I-insulin-specific binding, whereas iron addition reduced insulin binding, similarly to cells exposed to high glucose concentration. CONCLUSION: Iron status affects insulin sensitivity by modulating the transcription and membrane expression/affinity of insulin receptor expression in hepatocytes and influencing insulin-dependent gene expression suggesting that increased insulin clearance and decreased insulin resistance may contribute to the positive effect of iron depletion in patients with non-alcoholic fatty liver disease.

Analysis of the region between amino acids 30 and 42 of intact UmuD by a monocysteine approach.

On the basis of characterizations of a set of UmuD monocysteine derivatives, we had suggested that positions 24, 34, and 44 are closer to the intact UmuD homodimer interface than other positions tested (M. H. Lee, T. Ohta, and G. C. Walker, J. Bacteriol. 176:4825-4837, 1994). Because this region of UmuD also appeared to be important for interactions with RecA, we followed up on our previous study by constructing a second set of monocysteine UmuD derivatives with single cysteine substitutions at positions 30 to 42. We found that like the VC34 mutant, UmuD derivatives with monocysteine substitutions at positions 32 and 35 showed deficiencies in in vivo and in vitro RecA-mediated cleavage as well as in UV mutagenesis, suggesting that the position 32 to 35 region may be important for RecA-mediated cleavage of UmuD. Interestingly, UmuD with monocysteine substitutions at residues 33 and 40 showed a reduction in UV mutagenesis while retaining the ability to be cleaved by RecA in vivo, suggesting a deficiency in the subsequent role of the UmuD' derivatives in mutagenesis. All of the UmuD monocysteine derivatives in the position 30 to 42 series purified indistinguishably from the wild-type protein. The observations that purified proteins of the UmuD derivatives RC37 and IC38 could be disulfide cross-linked quantitatively upon addition of iodine and yet were poorly modified with iodoacetate led us to suggest that the pairs of residues at positions 37 and 38 are extremely close to the UmuD2 homodimer interface. These observations indicate that the structure of the UmuD2 homodimer in solution is very different from the crystal structure of the UmuD'2 homodimer reported by Peat et al. (T. S. Peat, E. G. Frank, J. P. McDonald, A. S. Levine, R. Woodgate, and W. A. Hendrickson, Nature [London] 380:727-730, 1996).

Inhibition of RecA-mediated cleavage in covalent dimers of UmuD.

Disulfide-cross-linked UmuD2 derivatives were cleaved poorly upon incubation with activated RecA. Reducing the disulfide bonds prior to incubating the derivatives with RecA dramatically increased their extent of cleavage. These observations suggest that the UmuD monomer is a better substrate for the RecA-mediated cleavage reaction than the dimer.

Metallothionein-II and ferritin H mRNA levels are increased in arsenite-exposed HeLa cells.

Arsenite is extremely toxic and, though non-mutagenic, is a carcinogen. To determine the effects of arsenite on changes in cell physiology, we searched for genes in HeLa cells whose mRNAs are more abundant after cellular exposure to arsenite. A cDNA subtraction was performed between cDNA synthesized from HeLa cells grown in the absence and presence of 5 microM sodium arsenite. Isolation and sequencing of three clones that showed a higher hybridization signal to RNA from arsenite-exposed cells, versus unexposed cells, revealed that two of the cDNAs coded for human ferritin H chain and the other coded for metallothionein-II. These results suggest the possibility that arsenite exposure may lead to increased levels of oxygen radicals, which augmented metallothionein and ferritin can act to detoxify.

A luxAB transcriptional fusion to the cryptic celF gene of Escherichia coli displays increased luminescence in the presence of nickel.

From a library of 3000 Escherichia coli clones, each containing a single, chromosomally located luxAB transcriptional gene fusion, one clone was found in which luminescence increased in the presence of 1 to 50 ppm of NiSO4. A molecular analysis revealed that the insertion occurred within the celF gene of E. coli. This gene encodes the phospho-beta-glucosidase involved in cleavage of the sugars cellobiose, salicin and arbutin. Cloning and sequencing of DNA downstream of the celF gene revealed three open reading frames (potentially encoding polypeptides of 9.9, 14.1 and 28.5 kDa) that could be co-expressed with the celF gene and that may underlie the observed induction of the celF gene by nickel. A polypeptide of 26 kDa was produced when this region was placed under the control of the Ptac promoter. Moreover, this region was found to be directly adjacent to, and transcribed in the opposite orientation from, the katE gene of E. coli.

Characterization of the effects of aluminum on luciferase biosensors for the detection of ecotoxicity.

Luciferase-based biosensors are becoming increasingly used for environmental monitoring. A transcriptional fusion of the Vibrio harveyi luxAB genes (encoding bacterial luciferase) to the fliC gene of Escherichia coli was constructed and luminescence shown to be induced (in liquid media) in the presence of 1-10 micrograms/ml aluminum, but not copper, iron or nickel. Moreover, luminescence is markedly increased at pH 5.5, where aluminum is more soluble than at pH 7.0. However, aluminum also stimulated luciferase activity when the luxAB genes were located in the xyl operon. This suggests that aluminum stimulates luciferase enzyme activity in vivo. These results are specific to E. coli, as no such aluminum stimulation was observed in the luminescent bacterium V. harveyi. These results have important implications in the generalized use of these clones for environmental monitoring, where aluminum can be present at elevated concentrations.