Minimally invasive video-assisted thyroidectomy: a retrospective study over two years of experience.

OBJECTIVE: The minimally invasive video-assisted thyroidectomy technique has slowly gained acceptance. Previous studies have reported advantages of better cosmetic results and faster postoperative recovery. We report preliminary results from our single assistant technique over the initial two years of inception at an academic training center. METHODS: This study consists of a retrospective chart review of 172 cases between May 2005 and September 2007. All cases started as video-assisted thyroidectomy were included. Demographic, pre- and postoperative clinical data, imaging results, and hospital stay were collected. RESULTS: Acceptable data were available for 24 male and 148 female patients who underwent the video-assisted procedure. Five cases were converted to the conventional thyroidectomy. Of the 172 cases, 60 total thyroidectomies and 112 hemithyroidectomies were performed, with 37 cases of malignancy. The average hospitalization was 1.43 days with mean incision length was 3.51 cm, mean surgical time of 91.37 minutes, and mean blood loss of 31 cc. Transient voice problems were noted in 10 patients. CONCLUSION: We found statistically improved operative times, hospital stay, and blood loss the first 2 years with a low rate of temporary complications. It appears that minimally invasive video-assisted thyroidectomy is a safe and feasible option to standard thyroidectomy in selected patients.

Substrate specificity of streptomyces transglutaminases.

Transglutaminase (TGase) is a multifunctional enzyme vital for many physiologic processes, such as cell differentiation, tissue regeneration, and plant pathogenicity. The acyl transfer function of the enzyme can activate primary amines and, consequently, attach them onto a peptidyl glutamine, a reaction important for various in vivo and in vitro protein crosslinking and modification processes. To understand better the structure-function relationship of the enzyme and to develop it further as an industrial biocatalyst, we studied TGase secreted by several Streptomyces species and Phytophthora cactorum. We purified the enzyme from S. lydicus, S. platensis, S. nigrescens, S. cinnamoneus, and S. hachijoensis. The pH and temperature profiles of S. lydicus, S. platensis, and S. nigrescens TGases were determined. The specificity of S. lydicus TGase toward its acyl-accepting amine substrates was characterized. Correlation of the electronic and steric features of the substrates with their reactivity supported the mechanism previously proposed for Streptomyces mobaraensis TGase.