Improvement in sentinel node biopsy results in a teaching community hospital: results of a multidisciplinary quality improvement program.

BACKGROUND: In 2001 we reported poor results for sentinel node biopsy and marked variability among surgeons. Subsequently, we initiated a multidisciplinary protocol involving standardized radiocolloid injection, physician education, and surgeon proctoring. METHODS: The current study presents follow-up data (2004-2006) after this quality improvement initiative. Data recorded included technical details and patient factors, related to each surgeon. Results were compared with our previously published data. RESULTS: The overall identification rate was improved markedly from 2001 (92% vs 66%). Eleven general surgeons performed 151 sentinel node biopsies. Seven surgeons had a 100% identification rate, the others had identification rates of 84% (N = 44), 86% (N = 29), 92% (N = 12), and 0% (N = 1). Differences still persist among surgeons, including number of sentinel nodes sampled, performance of axillary dissections, and breast conservation. CONCLUSIONS: A multidisciplinary protocol improved sentinel node biopsy performance in a community teaching hospital. However, further work is needed to standardize and improve overall breast surgery results.

How can trauma surgeons maintain their operative skills?

BACKGROUND: The operative experience of the dedicated trauma surgeon is declining. Much attention has focused on the operative workload of trauma surgeons as it is critical in both maintaining operative skills and promoting the interest of surgical residents in trauma careers. We examined the operative experience of our surgical service which includes trauma, emergency general surgery, and elective general surgery to analyze changes occurring over the past decade. METHODS: A retrospective study was performed by extracting data from the operative database at our Level I trauma center from January 1995 to December 2005. The cases were classified as trauma, emergency general surgery, or elective general surgery. Data were analyzed using weighted linear regression to analyze statistical significance. RESULTS: Although the total number of cases performed by the trauma service remained constant, the proportion of initial operative trauma cases (<24 hours from arrival to operation) decreased from 14% to 8% (r2 = 0.91, p < 0.001) over the study period. In contrast, emergency general surgery cases increased over this time period (r2 = 0.57, p < 0.01). Elective case volume was unchanged. The majority of the waning of trauma cases was due to decreased surgery on the liver and spleen and fewer neck explorations. CONCLUSIONS: Trauma operative experience decreased but emergency general surgery increased over a decade at our trauma center. It appears possible to maintain a busy operative trauma service by the inclusion of emergency general surgery consultations.

PDZ domains facilitate binding of high temperature requirement protease A (HtrA) and tail-specific protease (Tsp) to heterologous substrates through recognition of the small stable RNA A (ssrA)-encoded peptide.

The Escherichia coli protease HtrA has two PDZ domains, and sequence alignments predict that the E. coli protease Tsp has a single PDZ domain. PDZ domains are composed of short sequences (80-100 amino acids) that have been implicated in a range of protein:protein interactions. The PDZ-like domain of Tsp may be involved in binding to the extreme COOH-terminal sequence of its substrate, whereas the HtrA PDZ domains are involved in subunit assembly and are predicted to be responsible for substrate binding and subsequent translocation into the active site. E. coli has a system of protein quality control surveillance mediated by the ssrA-encoded peptide tagging system. This system tags misfolded proteins or protein fragments with an 11-amino acid peptide that is recognized by a battery of cytoplasmic and periplasmic proteases as a degradation signal. Here we show that both HtrA and Tsp are able to recognize the ssrA-encoded peptide tag with apparent K(D) values of approximately 5 and 390 nm, respectively, and that their PDZ-like domains mediate this recognition. Fusion of the ssrA-encoded peptide tag to the COOH terminus of a heterologous protein (glutathione S-transferase) renders it sensitive to digestion by Tsp but not HtrA. These observations support the prediction that the HtrA PDZ domains facilitate substrate binding and the differential proteolytic responses of HtrA and Tsp to SsrA-tagged glutathione S-transferase are interpreted in terms of the structure of HtrA.