Intrathoracic application of vacuum wound therapy following thoracic surgery.

OBJECTIVE: The VAC system (vacuum-assisted wound closure) is an established noninvasive active therapy to promote the healing of difficult wounds that fail to heal with conventional treatment after cardiac surgery. We report our initial experience of the intrathoracic application of the VAC system after extended thoracic surgery. METHODS: Thirteen patients (11 men, 2 women) with a median age of 60 years (range 41 to 82 years) with deep wound infections after thoracotomy (empyema = 3; lobectomy = 5; Pancoast = 1; pneumonectomy = 4) were treated primarily with the VAC system after initial surgical debridement. All patients had an increased risk for impaired wound healing (e.g., diabetes, obesity, empyema, steroids). The VAC system was removed when systemic signs of infection resolved and quantitative cultures were negative. RESULTS: After a mean period of 64 +/- 45 days (range 7 to 134 days) the VAC system was removed in all patients. It was used as a bridge to reconstructive surgery with a latissimus dorsi muscle flap in 2 patients (15 %), while surgical wound closure could be achieved in the remaining 11 patients (85 %). Complete healing without recurrence was achieved in 11/13 (85 %) patients to date. Hemodynamic or respiratory complications (e.g., air leakage) during VAC system application were not observed in any case. Survival was 100 % after 16 +/- 9 months. Duration of hospital stay varied from 16 to 110 days (mean 44 +/- 34 days). CONCLUSION: Intrathoracic vacuum therapy after extended thoracic surgery seems to be an effective and safe adjunct to conventional treatment modalities for the therapy of intrathoracic infections or deep wound infections.

[Investigations of stomatologic lighting equipment]. / Untersuchungen von stomatologischen Arbeitsfeldleuchten.

12 types of stomatologic lighting equipment were investigated with regard to their specific luminous intensity. The examination of the thermal radiation of the lighting equipment included subjective evaluations. Conclusions were drawn in order to improve the lighting.

Crystallization of rat cellular retinol binding protein II. Preliminary X-ray data obtained from the apoprotein expressed in Escherichia coli.

Rat cellular retinol-binding protein II (CRBP II) is a member of a family of cytoplasmic proteins which bind hydrophobic ligands. CRBP II is thought to participate in the intestinal absorption and intracellular metabolism of retinoids. We have previously described the crystallization of a homologous rat intestinal fatty acid-binding protein (I-FABP) isolated from Escherichia coli containing a suitably constructed prokaryotic expression vector (Sacchettini, J. C., Meininger, T. A., Lowe, J. B., Gordon, J. I., and Banaszak, L. J., J. Biol. Chem. 262, 5428-5430). We have now efficiently expressed rat CRBP II in E. coli. The E. coli-derived protein, which does not contain any bound retinoid, has been purified and crystals grown from solutions of polyethylene glycol 4000. Crystals of apo-CRBP II are triclinic, space group P1, a = 36.8 A, b = 64.0 A, c = 30.4 A; alpha = 92.8 degrees, beta = 113.5 degrees, gamma = 90.1 degrees. Each unit cell contains two molecules of the 134-residue apoprotein. X-ray diffraction data suggest that the unit cell parameters of crystalline apo-CRBP II resemble those of I-FABP. Comparison of the tertiary structures of E. coli-derived rat I-FABP and CRBP II should provide insights about how these proteins evolved to bind different hydrophobic ligands.

Association of the cyclic AMP chemotaxis receptor with the detergent-insoluble cytoskeleton of Dictyostelium discoideum.

Treatment of 6-h differentiated Dictyostelium discoideum cells with the nonionic detergent Triton X-100 dissolves away membranes and soluble components, as judged by marker enzyme distributions, leaving intact a cytoskeletal residue that contains approximately 10% of the cell protein and 50% of the actin. Nitrobenzooxadiazo-phallacidin staining for F-actin and electron microscopy of detergent-extracted whole-mounts indicate that the cytoskeletons retain the size and shape of intact cells and contain F-actin in cortical meshworks. The cytoskeletons contain little if any remaining membrane material by morphological criteria, and the plasma membrane enzymes cyclic nucleotide phosphodiesterase and alkaline phosphatase are absent from the insoluble residue, which retains only 15% of the membrane concanavalin A-binding glycoproteins. This detergent-insoluble residue retains a specific [3H]cAMP-binding site with the nucleotide specificity, rapid kinetics and approximate affinity of the cAMP receptor on intact cells. Upon detergent extraction of cells, the number of cAMP-binding sites increases 20-70%. The binding site is attached to the insoluble residue whether or not the cAMP receptor is occupied at the time of detergent addition. The pH dependence for recovery of the insoluble cAMP-binding site is much sharper than that on intact cells or membranes with an optimum at pH 6.1. Conditions of pH and ionic composition that lead to disruption of the cytoskeleton upon detergent treatment also result in the loss of cAMP binding. During differentiation, the detergent-insoluble cAMP binding increases in parallel with cell surface cAMP receptors and chemotaxis to cAMP.