28 research outputs found
Transurethral resection for botryoid bladder rhabdomyosarcoma
The outcome of multimodal therapy for localized bladder rhabdomyosarcoma is quite good in terms of morbidity, and conservative surgery is generally recommended. However, in cases originating in the bladder neck, tumorectomy or partial cystectomy has adverse effects on bladder function. A 2-year-old girl underwent transurethral resection of a bladder tumor (TUR-BT), chemotherapy consisting of vincristine, actinomycin-D, and cyclophosphamide, and radiotherapy. She was in remission for 3 years when frequent urination became evident. Her bladder capacity and compliance were low; however, her urinary symptom was controlled using anticholinergic medication. Accordingly, TUR-BT could be an optional approach for bladder rhabdomyosarcoma
2-Arachidonoyl glycerol potently induces cholecystokinin secretion in murine enteroendocrine STC-1 cells via cannabinoid receptor CB1
Cholecystokinin (CCK) is a peptide hormone secreted from enteroendocrine cells and regulates the exocrine pancreas, gastric motility, and appetite. Dietary triacylglycerols are hydrolyzed to fatty acids (FA) and 2-monoacylglycerols (2-MAG) in the small intestine. Although it is well known that FA stimulate CCK secretion, whether 2-MAG have the CCK-releasing activity remains unclear. We examined the CCK-releasing activity of four commercially available 2-MAG in a murine CCK-producing cell line, STC-1, and the molecular mechanism underlying 2-MAG-induced CCK secretion. CCK released from the cells was measured using ELISA. Among four 2-MAG (2-palmitoyl, 2-oleoyl, 2-linoleoyl, and 2-arachidonoyl monoacylglycerols) examined, 2-arachidonoyl glycerol (2-AG) potently stimulated CCK secretion in a dose-dependent manner. Structurally related compounds, such as 2-arachidonoyl glycerol ether and 1-arachidonoyl glycerol, did not stimulate CCK secretion. Both arachidonic acid and 2-AG stimulated CCK secretion at 100 mu M, but only 2-AG did at 50 mu M. 2-AG-induced CCK secretion but not arachidonic acid-induced CCK secretion was attenuated by treatment with a cannabinoid receptor 1 (CB1) antagonist. These results indicate that a specific 2-MAG, 2-AG, directly stimulates CCK secretion via CB1
2-Arachidonoyl glycerol suppresses gastric emptying via the cannabinoid receptor 1-cholecystokinin signaling pathway in mice
2-Monoacylglycerol (2-MAG) is one of the digestion products of dietary lipids. We recently demonstrated that a 2-MAG, 2-arachidonoyl glycerol (2-AG) potently stimulated cholecystokinin (CCK) secretion via cannabinoid receptor 1 (CB1) in a murine CCK-producing cell line, STC-1. CCK plays a crucial role in suppressing postprandial gastric emptying. To examine the effect of 2-AG on gastric emptying, we performed acetaminophen and phenol red recovery tests under oral or intraperitoneal administration of 2-AG in mice. Orally administered 2-AG (25 mg/kg) suppressed the gastric emptying rate in mice, as determined by the acetaminophen absorption test and phenol red recovery test. Intraperitoneal administration of a cholecystokinin A receptor antagonist (0.5 mg/kg) attenuated the gastric inhibitory emptying effect. In addition, both oral (10 mg/kg) and intraperitoneal (0.5 mg/kg) administration of a CB1 antagonist counteracted the 2-AG-induced gastric inhibitory effect. Furthermore, intraperitoneal 2-AG (25 mg/kg) suppressed gastric emptying. These results indicate that 2-AG exhibits an inhibitory effect on gastric emptying in mice, possibly mediated by stimulating both CCK secretion via CB1 expressed in CCK-producing cells and acting on CB1 expressed in the peripheral nerves. Our findings provide novel insights into the 2-MAG-sensing mechanism in enteroendocrine cells and the physiological role of 2-MAG
2-Arachidonoyl glycerol potently induces cholecystokinin secretion in murine enteroendocrine STC-1 cells via cannabinoid receptor CB1
Correction: Identification and Characterization of Sulfated Carbohydrate-Binding Protein from Lactobacillus reuteri.
[This corrects the article DOI: 10.1371/journal.pone.0083703.]
Correction: Identification and Characterization of Sulfated Carbohydrate-Binding Protein from Lactobacillus reuteri
Identification and Characterization of Sulfated Carbohydrate-Binding Protein from <i>Lactobacillus reuteri</i>
<div><p>We previously purified a putative sulfated-galactosylceramide (sulfatide)-binding protein with a molecular weight of 47 kDa from the cell surface of <i>Lactobacillus reuteri</i> JCM1081. The aim of this study was to identify the 47-kDa protein, examine its binding to sulfated glycolipids and mucins, and evaluate its role in bacterial adhesion to mucosal surfaces. By cloning and sequencing analysis, the 47-kDa protein was identified as elongation factor-Tu (EF-Tu). Adhesion properties were examined using 6×Histidine-fused EF-Tu (His<sub>6</sub>-EF-Tu). Surface plasmon resonance analysis demonstrated pH-dependent binding of His<sub>6</sub>-EF-Tu to sulfated glycolipids, but not to neutral or sialylated glycolipids, suggesting that a sulfated galactose residue was responsible for EF-Tu binding. Furthermore, His<sub>6</sub>-EF-Tu was found to bind to porcine gastric mucin (PGM) by enzyme-linked immunosorbent assay. Binding was markedly reduced by sulfatase treatment of PGM and in the presence of acidic and desialylated oligosaccharide fractions containing sulfated carbohydrate residues prepared from PGM, demonstrating that sulfated carbohydrate moieties mediated binding. Histochemical staining revealed similar localization of His<sub>6</sub>-EF-Tu and high iron diamine staining in porcine mucosa. These results indicated that EF-Tu bound PGM via sulfated carbohydrate moieties. To characterize the contribution of EF-Tu to the interaction between bacterial cells and PGM, we tested whether anti-EF-Tu antibodies could inhibit the interaction. Binding of <i>L. reuteri</i> JCM1081 to PGM was significantly blocked in a concentration-dependent matter, demonstrating the involvement of EF-Tu in bacterial adhesion. In conclusion, the present results demonstrated, for the first time, that EF-Tu bound sulfated carbohydrate moieties of sulfated glycolipids and sulfomucin, thereby promoting adhesion of <i>L. reuteri</i> to mucosal surfaces.</p></div
Glucagon-Like Peptide-1 Is Involved in the Thermic Effects of Dietary Proteins in Male Rodents
Protein intake potently increases body temperature and energy expenditure, but the underlying mechanism thereof remains incompletely understood. Simultaneously, protein intake potently stimulates glucagon-like peptide-1 (GLP-1) secretion. Here, we examined the involvement of GLP-1 in the thermic effects of dietary proteins in rodents by measuring rectal temperature and energy expenditure and modulating GLP-1 signaling. Rectal temperature of rats or mice fasted for 4 or 5 hours were measured using a thermocouple thermometer before and after an oral administration of nutrients. Oxygen consumption after oral protein administration was also measured in rats. Rectal temperature measurements in rats confirmed an increase in core body temperature after refeeding, and the thermic effect of the oral administration of protein was greater than that of a representative carbohydrate or lipid. Among the five dietary proteins examined (casein, whey, rice, egg, and soy), soy protein had the highest thermic effect. The thermic effect of soy protein was also demonstrated by increased oxygen consumption. Studies using a nonselective beta-adrenergic receptor antagonist and thermal camera suggested that brown adipose tissue did not contribute to soy protein-induced increase in rectal temperature. Furthermore, the thermic effect of soy protein was completely abolished by antagonism and knockout of the GLP-1 receptor, yet potentiated via augmentation of intact GLP-1 levels through inhibition of dipeptidyl peptidase-4 activity. These results indicate that GLP-1 signaling is essential for the thermic effects of dietary proteins in rats and mice, and extend the metabolic actions of GLP-1 ensuing from nutrient ingestion to encompass the thermic response to ingested protein
Binding of His<sub>6</sub>-EF-Tu to sulfated glycolipids assessed by SPR analysis.
<p>(A) Binding of His<sub>6</sub>-EF-Tu to sulfatide (SO<sub>3</sub>-3Galβ1Cer) at different pH values (pH 4.0, 5.0, 6.0, and 7.2). (B) Binding of His<sub>6</sub>-EF-Tu to various glycolipids: sulfatide, sulfated-lactosylceramide (SO<sub>3</sub>-3Galβ4Glcβ1Cer), galactosylceramide (Galβ1Cer), lactosylceramide (Galβ4Glcβ1Cer), and GM3 (NeuAcα3Galβ4Glcβ1Cer) at pH 5.0 and 7.2. Resonance units were measured at the start of dissociation. Error bars indicate standard deviations (n<i> = </i>5). (C) Sensorgrams of the interaction of His<sub>6</sub>-EF-Tu with sulfatide at pH 5.0. Concentrations of His<sub>6</sub>-EF-Tu (from top to bottom) are as follows: 350, 300, 250, 200, and 150 nM. The K<sub>D</sub> value is described in the text.</p