Comparison of quick point-of-care test for small-bowel hypolactasia with biochemical lactase assay in children.

Aim: The aim of the present study was to compare the Biohit Lactose Intolerance Quick Test (BLIQT) to the criterion standard biochemical duodenal lactase (DL) activity assay in the paediatric population using standard statistical comparative tests.

Methods: Using standard Olympus endoscopes, 2 postbulbar duodenal biopsies were taken from 38 prospective children (0-16 years) from June 2008-May 2009 at a single tertiary paediatric gastroenterology unit. The biopsies were used for the BLIQT and for biochemical disaccharides assay.

Lectins: from basic science to clinical application in cancer prevention.

Many physiological functions are attributable to lectin-carbohydrate interactions. Lectins are currently being studied for their ability to destroy tumour growth by binding to specific carbohydrate motifs on cancer cells. Cell-surface molecules, including growth factor receptors are often glycosylated, and lectins may act by binding to these.

Comparison of the effects of concanavalin-A and epidermal growth factor on epithelial cell proliferation in the rat intestine.

Background: Concanavalin-A, the lectin present in Jack beans, binds to mannose- and glucose-containing residues and can interact with the epidermal growth factor receptor and moderate cell proliferation in vitro.

Aim: To compare the actions of concanavalin-A and epidermal growth factor on the gastrointestinal tract in vivo.

Methods: Rats maintained on total parenteral nutrition were given intragastric concanavalin-A, intravenous epidermal growth factor or concanavalin-A and epidermal growth factor.

Proglucagon-derived peptides in intestinal epithelial proliferation: glucagon-like peptide-2 is a major mediator of intestinal epithelial proliferation in rats.

Proglucagon-derived peptides have been implicated in the control of intestinal mucosal cell division. To investigate the actions of these peptides on intestinal cell proliferation, different doses of enteroglucagon, oxyntomodulin, glucagon-like peptide-1 (GLP-1) and glucagon-like peptide-2 (GLP-2) were tested in male Wistar rats maintained on total parenteral nutrition. Crypt cell proliferation was assessed by the analysis of arrested metaphases in microdissected crypts.

Elevated plasma cholecystokinin at high altitude: metabolic implications for the anorexia of acute mountain sickness.

The aims of the present study were to measure the satiety neuropeptide cholecystokinin (CCK) in humans at terrestrial high altitude to investigate its possible role in the pathophysiology of anorexia, cachexia, and acute mountain sickness (AMS). Nineteen male mountaineers aged 38 +/- 12 years participated in a 20 +/- 5 day trek to Mt. Kanchenjunga basecamp (BC) located at 5,100 m, where they remained for 7 +/- 5 days.

Systemic effect of peanut agglutinin following intravenous infusion into rats.

Background: Ingested peanut agglutinin stimulates colonic proliferation in humans. In rats, ingested peanut agglutinin stimulates hormone release and proliferation in the small and large intestines. Peanut agglutinin is absorbed into the circulation but little is known about the systemic effect of this lectin.

Characterization of the E-cadherin-catenin complexes in pancreatic carcinoma cell lines.

E-cadherin and its associated cytoplasmic proteins alpha-, beta-, and gamma-catenins play important roles in cell adhesion and signal transduction, as well as in maintenance of the structural and functional organization of polarized epithelial cells. In this study, the expression, distribution, and complex assembly of catenins with E-cadherin was analysed at the steady state in a panel of human pancreatic adenocarcinoma cell lines (BxPc3, HPAF, T3M4, and PaTuII cell lines). The expression and subcellular distribution were determined by western blotting and immunocytochemistry.

Gastrointestinal responses to a panel of lectins in rats maintained on total parenteral nutrition.

Total parenteral nutrition (TPN) causes atrophy of gastrointestinal epithelia, so we asked whether lectins that stimulate epithelial proliferation can reverse this effect of TPN. Two lectins stimulate pancreatic proliferation by releasing CCK, so we asked whether lectins that stimulate gastrointestinal proliferation also release hormones that might mediate their effects. Six rats per group received continuous infusion of TPN and a once daily bolus dose of purified lectin (25 mg.

Vicia faba agglutinin, the lectin present in broad beans, stimulates differentiation of undifferentiated colon cancer cells.

Background: Dietary lectins can alter the proliferation of colonic cells. Differentiation is regulated by adhesion molecules which, being glycosylated, are targets for lectin binding.

Aims: To examine the effects of dietary lectins on differentiation, adhesion, and proliferation of colorectal cancer cells.

Soybean agglutinin stimulated cholecystokinin release from cultured rabbit jejunal cells requires calcium influx via L-type calcium channels.

We have studied the mechanism of soybean agglutinin (SBA) mediated cholecystokinin (CCK) release in enriched cultured cholecystokinin-secreting cells. 12-O-Tetradecanoylphorbol-13-acetate 1 mM significantly stimulated release of CCK-like-immunoreactivity (CCK-LI) by 55%+/-17% (p < 0.05), which was blocked by the protein kinase C inhibitor staurosporine 100 nM.

Effects of a panel of dietary lectins on cholecystokinin release in rats.

We previously showed that soybean lectin (SBL) releases cholecystokinin (CCK) and have now asked whether other dietary lectins have this effect and if extracellular calcium is involved. Lectins and vehicle were first infused into the duodenum of anesthetized rats. The CCK response to vehicle was 3.

Soybean lectin stimulates pancreatic exocrine secretion via CCK-A receptors in rats.

Rats fed raw soy flour (RSF) show pancreatic growth due to excessive cholecystokinin (CCK) release. Soybean trypsin inhibitors are implicated, but rats fed soybean lectin also showed pancreatic growth. Therefore, we studied the effect of soybean lectin on pancreatic protein secretion in anesthetized rats.