Analysis of risk factors for surgical site infection and postoperative recurrence following inguinal and femoral hernia surgery in adults.

Objective: We aimed to evaluate the causes of complications following surgery for inguinal and femoral hernia, using surgical site infection (SSI) and recurrence rate as indicators of outcomes to consider appropriate treatments.

Methods: We retrospectively assessed the medical histories of 1,098 patients with adult inguinal and femoral hernias who underwent herniorrhaphy between July 2010 and March 2019. Using SSI and recurrence rate as indicators of outcomes, we statistically assessed the influence of preoperative and operative conditions on surgical outcomes.

Expression of CXCR-4 and IDO in human colorectal cancer: An immunohistochemical approach.

C-X-C chemokine receptor type 4 (CXCR4), the receptor for the chemokine stromal cell-derived factor (SDF)-1 [also known as C-X-C motif chemokine 12 (CXCL12)], is involved in lymphocyte trafficking. Recent studies have demonstrated that, during pregnancy, a placental enzyme called indoleamine 2, 3-dioxygenase (IDO) exerts a key role in suppressing the maternal T-cell response against the fetus. In the present study, the significance of CXCR4 and IDO expression in human colorectal cancer (CRC) has been investigated by immunohistochemical assay, and their association with survival was analyzed.

Initial Report of Phase II Study on Bi-weekly SOX plus Cetuximab Treatment for Wild-type K-RAS Advanced and Recurrent Colorectal Cancer.

Aim: This prospective study was designed to evaluate the tolerability and the efficacy of bi-weekly SOX (S-1 and oxaliplatin)+cetuximab as first-line chemotherapy for wild-type K-RAS metastatic colorectal cancer.

Patients And Methods: We studied patients with previously untreated, unresectable, advanced or recurrent colorectal cancer who were treated in our hospital between October 2010 and March 2013. Their performance status (PS) was 0 to 1.

Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum.

Glutamate is industrially produced by fermentation using Corynebacterium glutamicum. The key factor for efficient glutamate production by this microorganism has been considered to be a metabolic change at the 2-oxoglutarate dehydrogenase (ODH) branch point caused by a decrease in ODH activity under glutamate-overproducing conditions. However, this change would be insufficient because the ODH branch is merely the final branch in the glutamate biosynthetic pathway, and efficient glutamate production requires a balanced supply of acetyl-CoA and oxaloacetate (OAA), which are condensed to form a precursor of glutamate, namely, citrate.