CPR after CMT for rectal cancer is associated with improved local and distal control as well as better OS and DFS.

No abstract

Perivenular hepatocytes are the first cells within the liver lobule to display signs of toxicity following long-term alcohol use. In an attempt to explain this phenomenon, we have examined the hepatic intralobular distribution in rats and man of P450IIE1, a P-450 isozyme that not only oxidizes ethanol but is also inducible by this agent. Frozen liver sections and microsomes were prepared from male Sprague-Dawley rats pair-fed liquid diets containing 36% of total calories as either ethanol or carbohydrate (control) for 10 to 21 days. Frozen sections or microsomes were also prepared from liver biopsy samples obtained from 17 male patients with diverse drinking histories. Immunohistochemical staining was performed using the peroxidase-antiperoxidase method after liver sections were reacted with monospecific antibody (IgG) directed against human P450IIE1. Immunoreaction intensity was blindly rated in order to provide a semiquantitative assessment of P450IIE1 levels in perivenular, midzonal and periportal hepatocytes. At low applied anti-P450IIE1 IgG concentrations (2.5 micrograms per ml), P450IIE1 immunostaining was observed exclusively within the perivenular area in sections from all ethanol-treated rats, whereas no visible immunoreaction was found in sections from their pair-fed controls. At higher applied antibody concentrations (15 micrograms per ml), panlobular antigen immunostaining was observed in five of the six ethanol-treated animals, and P450IIE1 could now also be detected in perivenular hepatocytes from the control rats. In accordance with these immunohistochemical findings, protein blotting with anti-P450IIE1 IgG revealed a 7.5-fold increase in liver microsomal P450IIE1 content in ethanol-treated animals when compared to their pair-fed controls. With human liver, perivenular P450IIE1 immunostaining was observed only in biopsy sections obtained from recently drinking alcoholics (abstinence period of 1 day) when limiting concentrations (5 micrograms per ml) of the primary antibody were used. Increasing the applied anti-P450IIE1 IgG concentration to 15 micrograms per ml resulted in perivenular staining of the immunogen in liver sections from abstinent alcoholics (abstinence period of 4 to 8 days) and nondrinkers as well. Immunoblot analysis of human liver microsomes disclosed that the hepatic microsomal P450IIE1 content in recently drinking alcoholics was 4-fold higher than that found in nondrinkers. Our results show that, in both rats and in man, P450IIE1 is normally localized within the perivenular region, or zone 3, of the liver lobule, and that induction of P450IIE1 by prolonged alcohol consumption occurs primarily within the same acinar regi

The MIDP procedure is feasible, safe, and associated with less blood loss and overall complications, shorter time to oral intake, and shorter postoperative hospital stay. Furthermore, the minimally invasive approach reduces the rate of pancreatic leaks and surgical-site infections after ODP.

Laparoscopic surgery for Crohn's disease is feasible, safe, and associated with shorter duration of ileus and a shorter hospital stay.

No abstract

No abstract

Serum ferritin protein is an acute phase reactant. We hypothesized that serum ferritin protein generated in response to an inflammatory process would have much less iron (Fe) in it than would "normal" ferritin protein, and therefore measuring serum ferritin iron would assess human body iron status unconfounded by inflammation.Basic Methods. We measured serum ferritin iron in 140 clinical samples obtained from the serum banks of Bronx VA Medical Center Hematology and Nutrition Laboratory (Bronx, NY), the CDC Nutritional Biochemistry serum sample bank (Atlanta, GA), and the sample bank from patients with thalassemia and iron overload treated at New York Hospital (New York, NY). Each was analyzed for three conventional criteria of iron status: serum iron, percentage of transferrin saturation and ferritin protein. In addition, tests for inflammation were also performed: C-reactive protein, WBC and transaminases. Seventy-seven patients' sera from 140 screened met each of three consistent criteria for stages of iron status. Serum ferritin was immobilized by immunoprecipitation with rabbit antihuman polyclonal antibody bound to agarose and separated from other iron-containing proteins, digested with 0.2 ml of 3N nitric acid and analyzed for iron content by atomic absorption spectroscopy.Results. Serum ferritin iron ranged in normal controls from 10 ng to 35 ng Fe/ml. The patients with iron deficiency (4/4) and those in negative iron balance (5/6) had values ≤10 ng. Positive iron balance (8/9) and iron overload (22/22) values were >35 ng/ml, in contrast to 11/19 with inflammation. Seventeen of twenty-two with overload had values >100 ng/ml while only 1/19 with inflammation had such a value. Ferritin iron in ferritin protein was >15% by weight in 14/22 with iron overload but in 0/19 with inflammation.Implications of the Work. Serum ferritin iron is a simple, direct measure of iron stores that we propose, in conjunction with measuring serum ferritin protein, as a minimally invasive screening procedure for accurately assessing the whole range of human body iron status, unconfounded by inflammation.