Single-incision laparoscopic right hemicolectomy: inferior-to-superior approach with intracorporeal anastomosis.

BACKGROUND: Single-incision laparoscopic right hemicolectomy has been shown to be safe and feasible; however, it remains technically demanding. We present a single-incision laparoscopic right hemicolectomy with an inferior-to-superior approach with intracorporeal anastomosis. This approach may help overcome some of the technical challenges of the conventional technique. TECHNIQUE: With the patient in steep Trendelenburg and right-side elevated, a single-incision device is placed at the umbilicus. The small bowel is mobilized out of the pelvis, exposing the ileocolic peritoneal attachments. The peritoneum is divided and the retroperitoneal plane is established in a cranial and medial fashion until the duodenum is exposed. The ileocolic pedicle is readily identified and divided. Further exposure of the retroperitoneal plane is developed and the right branch of the middle colic vessel is isolated and divided. Attention is drawn to the remaining attachments of the hepatic flexure, which is then taken down. The resection margins of the transverse colon and terminal ileum are identified and a side-to-side intracorporeal anastomosis using a double-stapled technique is performed. CONCLUSIONS: Technical challenges of the single-incision laparoscopic right hemicolectomy may be overcome utilizing an inferior-to-superior approach with intracorporeal anastomosis by affording optimal exposure, retraction, and dissection of the tissue planes.

Alzheimer's disease skin fibroblasts selectively express a bradykinin signaling pathway mediating tau protein Ser phosphorylation.

Increased Ser phosphorylation of tau microtubule-associated protein in the brain is an early feature of Alzheimer's disease (AD) that precedes progression of the disease to frank neuronal disruption. We demonstrate that bradykinin (BK) B2 receptor activation leads to selective Ser phosphorylation of tau in skin fibroblasts from persons who have or will develop AD due to Presenilin 1 mutations or Trisomy 21, but not in skin fibroblasts from normal individuals at any age. The increased signal transduction in AD fibroblasts that culminates in tau Ser phosphorylation reflects modification of the G protein-coupled BK B2 receptors themselves. Both the BK B2 receptor modification and BK-mediated tau Ser phosphorylation are dependent on activation of protein kinase C and can be detected in fibroblasts from persons with Trisomy 21 two decades before the characteristic onset of AD. This dysregulated signaling cascade in AD may thus be expressed throughout life as an aberrant pathway in peripheral tissues more accessible than brain for molecular analysis. The sites of greatest BK B2 receptor expression in brain overlap with those areas displaying the earliest pathology in the course of AD, suggesting that BK receptor pathway dysfunction may be a molecular signature yielding information about the pathogenesis of AD.