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Biomedical subjects

B Onraed

Publications and source records attributed to B Onraed.

6 recordsLinked to original sources
PubMed2006

Predictive factors for rhabdomyolysis after bariatric surgery.

BACKGROUND: Prevalence of obesity is increasing internationally. Obesity is also incriminated in the development of postoperative rhabdomyolysis (RML). Its major risk is the development of renal failure which is associated with high mortality. The aim of this study was to determine the risk factors for RML in patients undergoing bariatric surgery. METHODS: Over a 12-month period, 49 consecutive patients were studied. They underwent gastric banding (n=32) or intestinal or gastric bypass (n=17) for morbid obesity (BMI >40 kg/m(2)). Surgery was performed in the supine position with a lumbar pad placed for intestinal shunt. The duration of surgery, persistent postoperative muscular pain, and pre- and postoperative creatine kinase (CK) were recorded. RML was defined as postoperative CK >1000 IU. L(-1) (5 times the normal value). Patients were retrospectively divided into 2 groups according to the presence or not of RML. In order to assess the role of BMI, it was decided to conduct an additional analysis in a group of consecutive non-obese patients who were matched for other risk characteristics. RESULTS: In the 49 patients included in the study 13 developed RML (26.5%). Surgery >4 hours, presence of diabetes and patient ASA physical status III or IV were identified as factors associated with higher risk of RML. In the matched group (9 patients), no one developed postoperative RML. CONCLUSIONS: After surgery for obesity, the risk of RML increases with prolonged surgery (>4 hours) and in diabetic obese patients with BMI >40 kg/m(2). In such patients, CK could be systematically measured to verify the presence of muscle injuries.

Adult↗
PubMed2004

CSF isoelectrofocusing in a large cohort of MS and other neurological diseases.

The present study was performed in order to confirm the diagnostic value of isoelectrofocusing (IEF) in a large multiple sclerosis (MS) cohort and to evaluate the various neurological diseases probably to present a similar IEF profile. The cerebrospinal fluid (CSF) of 1292 patients with neurological diseases was studied by IEF. After a follow-up of 2-36 months, we only included patients with a definite MS or confirmed diagnosis of other neurological diseases (OND). MS was diagnosed in 407 patients and OND in 593 patients. For patients in whom three or more oligoclonal bands (OCB) were detected, IEF results showed a sensitivity of 85% and a specificity of 92% for the diagnosis of MS. The positive and negative predictive values were 86.5 and 90%, respectively. Inflammatory and infectious disorders of the central nervous system represented the main affections associated with OCB, including human immunodeficiency virus encephalitis, Lyme disease and less frequently Sjogren syndrome. Furthermore, when OCB were observed, 10 or more bands were more frequently found in MS than in OND (P < 0.0001). IEF of the CSF is a reliable method for the diagnosis of MS. The absolute number of bands may help to discriminate between MS and OND.

Acquired Immunodeficiency Syndrome↗
PubMed1999

Identification of IgG-specific oligoclonal banding in serum and cerebrospinal fluid by isoelectric focusing: description of a simplified method for the diagnosis of neurological disorders.

Clinical laboratory procedures using cerebrospinal fluid (CSF) to assist in the diagnosis of multiple sclerosis (MS) are based essentially on the determination of oligoclonal bands (OB) in CSF and not in serum. To date, the techniques using isoelectric focusing (IEF) have represented one of the most efficient methods for detecting supernumerary bands in CSF but unfortunately were not always compatible with a routine use. Here, we describe a revised method of IEF suitable for the diagnosis of neurological disorders. The kit-based technique was simplified and the present procedure allowed an easier execution, reduced the overall analysis time and permitted an uncomplicated intepretation of oligoclonal profiles. Moreover, the technique developed was very sensitive and specific for the diagnosis of MS diagnosis. In conclusion, the IEF protocol described in this report is suitable for OB detection in any laboratory.

Central Nervous System Diseases↗
PubMedDate not supplied

[Difficulties with immunofixation interpretation].

Immunofixation is widely used for monoclonal gammapathies identification and Bence Jones proteinuria research. In more of cases, interpretation is easy, but some difficulties persist. Five examples are presented and their causes are analysed; in our first case, seric immunofixation shows the problem generated by additives. These components are added to optimize antigen- antibody reaction but they can induce interferences; three cases of urinary immunofixation showing Bence Jones proteinuria with/or without complete monoclonal immunoglobulin are presented. The variability of immunsera avidity is sometimes a problem; a case of light chain disease associated with monoclonal IgA illustrate difficulties of interpretation when precipitin bands have nearly the same migration. These examples underline the great importance of regular controls of immunologic reagents. The use of two antisera with the same specificity but different origin is recommended in order to resolve difficulties with interpretation of immunofixation.

Aged↗
PubMedDate not supplied

[HS CRP with Fumouze immunoturbidimetry and Dade Behring immunonephelemetry].

Increased concentrations of high sensitivity C-reactive protein are associated with increased risk for coronary heart disease. We report here a comparison of Fumouze hs-CRP turbidimetric method on Roche Diagnostics Hitachi 911 with Dade Behring BN II nephelemetric method. 134 samples were analysed. Within-run imprecision and between-run CV were good. Linearity was less satisfactory. Correlation study showed that without exceeding the maximum value of 6 mg/L, the hs-CRP method presented a good agreement with hs-CRP BN II method.

C-Reactive Protein↗