Congenital chest wall deformities: a modified surgical technique.

BACKGROUND: Congenital chest wall deformities are the most common disorders among the other congenital diseases in thoracic surgery. Standard surgical techniques seem to be sufficient, but to prevent recurrence and complications other surgical approaches have to be chosen, such as freeing the sternum from the second rib cartilage to the costal arch, completely and bilaterally, and external application of Kirschner wire for stabilization. PATIENTS AND METHODS: Between 1996 and 2005, 47 patients with congenital chest wall deformities were examined. The surgical method consists of resecting rib cartilages from the second rib up to the costal arch bilaterally and the application of Kirschner wire for the stabilization of the chest wall. RESULTS: No mortality occurred. Three patients had complications, such as wound infection and pneumothorax. Kirschner wire was removed on the 15th day (between 10-21 days). Mean hospital stay was 16.5 days (10-23 days). Patients were followed up between 2 months and 6 years. No recurrence was observed. CONCLUSION: To prevent recurrence and complications for cosmetic surgery is quite important. For this reason, the surgical technique has to be carried out carefully. Kirschner wire is useful for the stabilization of the chest wall with no risk of infection, foreign body reaction, or the need for a second operation for removal.

Diaphragmatic hydatid disease.

Hydatid disease caused by echinococcus granulosus is still a serious problem in both underdeveloped and developing countries. Clinical signs of the disease are not specific. Most patients have no symptom or sign when a hydatid cyst is discovered. Symptoms depend on its complications, location and size. Parasite can settle in every organ and tissue in the human body. We report two cases with diaphragmatic hydatid disease with no other cyst present.

Cardiac contractile dysfunction in Lep/Lep obesity is accompanied by NADPH oxidase activation, oxidative modification of sarco(endo)plasmic reticulum Ca2+-ATPase and myosin heavy chain isozyme switch.

AIMS/HYPOTHESIS: Obesity is an independent risk factor for heart diseases but the underlying mechanism is not clear. This study examined cardiac contraction, oxidative stress, oxidative modification of sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) and the myosin heavy chain (MHC) isoform switch in obese mice. METHODS: Mechanical properties were evaluated in ventricular myocytes from C57BL/6J lean and Lep/Lep obese mice (formerly known as ob/ob mice), including peak shortening (PS), time to 50 or 90% PS, time to 50 or 90% relengthening (TR50, TR90), maximal velocity of shortening/relengthening (+/-dL/dt), intracellular Ca2+ and its decay (tau). Oxidative stress, lipid peroxidation, protein damage and SERCA activity were assessed by glutathione/glutathione disulfide, malondialdehyde, protein carbonyl and 45Ca2+ uptake, respectively. NADPH oxidase was determined by immunoblotting. RESULTS: Myocytes from Lep/Lep mice displayed depressed PS and +/- dL/dt, prolonged TR50, TR90, elevated resting [Ca2+]i, prolonged tau, reduced contractile capacity at high stimulus frequencies and diminished responsiveness to extracellular Ca2+ compared with lean controls. Cardiac glutathione/glutathione disulfide was decreased whereas malondialdehyde, protein carbonyl, membrane p47(phox) and membrane gp91(phox) were increased in the Lep/Lep group. SERCA isoenzyme 2a was markedly modified by oxidation in Lep/Lep hearts and associated with decreased 45Ca2+ uptake. The MHC isozyme displayed a shift from the alpha to the beta isoform in Lep/Lep hearts. Short-term incubation of angiotensin II with myocytes mimicked the mechanical defects, SERCA oxidation and 45Ca2+ uptake seen in Lep/Lep myocytes. Incubation of the NADPH oxidase inhibitor apocynin with Lep/Lep myocytes alleviated contractile defects without reversing SERCA oxidation or activity. CONCLUSIONS/INTERPRETATION: These data indicate that obesity-related cardiac defects may be related to NADPH oxidase activation, oxidative damage to SERCA and the MHC isozyme switch.