Journal of Pediatric Gastroenterology and NutritionVolume 39, Issue S1 p. S49-S50 ABSTRACTS: Oral Presentation Abstracts O0108 THE COMBINATION OF HELICOBACTER PYLORI STRAIN AND TNF ALPHA POLYMORPHISM OF THE HOST INCREASES THE RISK OF PEPTIC ULCER DISEASE IN CHILDREN M. Wilschanski, M. Wilschanski Pediatric Gastroenterology, Hadassah University Hospital, Jerusalem, IsraelSearch for more papers by this authorY. Schlesinger, Y. Schlesinger Pediatric Infectious Diseases, Jerusalem, IsraelSearch for more papers by this authorB. Rudensky, B. Rudensky Microbiology Laboratory, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this authorJ. Faber, J. Faber Pediatric Gastroenterology, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this authorF. Ohnona, F. Ohnona Pediatric Infectious Diseases, Jerusalem, IsraelSearch for more papers by this authorS. Refael, S. Refael Pediatric Gastroenterology, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this authorS. Freier, S. Freier Pediatric Gastroenterology, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this authorD. Branski, D. Branski Pediatric Gastroenterology, Hadassah University Hospital, Jerusalem, IsraelSearch for more papers by this authorD. Halle, D. Halle Pediatric Gastroenterology, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this author M. Wilschanski, M. Wilschanski Pediatric Gastroenterology, Hadassah University Hospital, Jerusalem, IsraelSearch for more papers by this authorY. Schlesinger, Y. Schlesinger Pediatric Infectious Diseases, Jerusalem, IsraelSearch for more papers by this authorB. Rudensky, B. Rudensky Microbiology Laboratory, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this authorJ. Faber, J. Faber Pediatric Gastroenterology, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this authorF. Ohnona, F. Ohnona Pediatric Infectious Diseases, Jerusalem, IsraelSearch for more papers by this authorS. Refael, S. Refael Pediatric Gastroenterology, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this authorS. Freier, S. Freier Pediatric Gastroenterology, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this authorD. Branski, D. Branski Pediatric Gastroenterology, Hadassah University Hospital, Jerusalem, IsraelSearch for more papers by this authorD. Halle, D. Halle Pediatric Gastroenterology, Shaare Zedek Medical Center, Jerusalem, IsraelSearch for more papers by this author First published: 01 June 2004 https://doi.org/10.1002/j.1536-4801.2004.tb12416.x Submitted by: [email protected] Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Reference(S): (1)J Pediatr Gastro Nutr 35: 680–684; 2002. 10.1097/00005176-200211000-00018 PubMedWeb of Science®Google Scholar Volume39, IssueS1June 2004Pages S49-S50 ReferencesRelatedInformation

BACKGROUND:Programmed cell death refers to the genetically determined processes by which cells die in response to physiologic extracellular and intracellular signals, morphologically described as apoptosis. In physiologic and pathologic circumstances this process may involve effector and target cells.METHODS:To identify serine esterase granules in intraepithelial lymphocytes, fresh-frozen human small intestine mucosal sections from normal and celiac-affected mucosa were incubated with substrate-specific N-alpha-benzyloxy-carbonyl-L-lysine thiobenzyl (BLT) and a chromogen (4 Benzoylamino-2,5-diethoxybenzene-dazonium chloride hemi [zinc chloride] salt as capture agent and were examined by light microscopy.RESULTS:Normal mucosa showed an occasional intraepithelial lymphocyte with BLT-positive intracytoplasmic granules. Some large mononuclear cells of the lamina propria were similarly stained. Many more intraepithelial lymphocytes were BLT-positive among the surface enterocytes of untreated celiac mucosa. Lamina propria mononuclear cells close to the basal layer of crypt cells also appeared to be increased.CONCLUSIONS:The histochemical identification of BLT-positive esters within intraepithelial lymphocytes suggests their involvement in enterocyte death under physiologic conditions. The increased BLT-positive intraepithelial lymphocytes found in the celiac mucosa may be related to the known increase in cytotoxic intraepithelial lymphocytes in untreated celiac disease.

Journal of Pediatric Gastroenterology and NutritionVolume 13, Issue 3 p. 332-332 Abstracts from: PDF Only ANDERSON'S DISEASE NO LINKAGE TO THE apo B LOCUS D. Strich, D. Strich Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorR. Goldstein, R. Goldstein Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorR. Shemer, R. Shemer Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorA. Phillips, A. Phillips Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorY. Goldberg, Y. Goldberg Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorA. Razin, A. Razin Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorS. Freier, S. Freier Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this author D. Strich, D. Strich Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorR. Goldstein, R. Goldstein Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorR. Shemer, R. Shemer Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorA. Phillips, A. Phillips Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorY. Goldberg, Y. Goldberg Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorA. Razin, A. Razin Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this authorS. Freier, S. Freier Department of Paediatrics, Gastroenterological Laboratory, Shaare Zedek Med. Cent., Department of Cellular BiochemistrySearch for more papers by this author First published: 01 October 1991 https://doi.org/10.1002/j.1536-4801.1991.tb10446.xAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume13, Issue3October 1991Pages 332-332 RelatedInformation

Acta PaediatricaVolume 80, Issue 10 p. 958-960 Intolerance to Casein Hydrolysate Formula:Clinical Aspects E. Rosenthal, E. Rosenthal Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorY. Schlesinger, Y. Schlesinger Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorY. Birnbaum, Y. Birnbaum Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorR. Goldstein, R. Goldstein Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorA. Benderly, A. Benderly Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorS. Freier, Corresponding Author S. Freier Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, Jerusalem(S. F.) Department of Pediatrics, Inst of Gastroenterology, Shaare Zedek Medical Center, P. O. Box 3235, Jerusalem 91-031, IsraelSearch for more papers by this author E. Rosenthal, E. Rosenthal Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorY. Schlesinger, Y. Schlesinger Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorY. Birnbaum, Y. Birnbaum Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorR. Goldstein, R. Goldstein Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorA. Benderly, A. Benderly Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, JerusalemSearch for more papers by this authorS. Freier, Corresponding Author S. Freier Department of Pediatrics ‘A’, Rambam Medical Center, Haifa and Department of Pediatrics and Laboratory of the Institute of Gastroenterology, Shaare Zedek Medical Center, Jerusalem(S. F.) Department of Pediatrics, Inst of Gastroenterology, Shaare Zedek Medical Center, P. O. Box 3235, Jerusalem 91-031, IsraelSearch for more papers by this author First published: October 1991 https://doi.org/10.1111/j.1651-2227.1991.tb11760.xCitations: 31AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume80, Issue10October 1991Pages 958-960 RelatedInformation

In a family in which the father was the mother's uncle, 3 of the 7 children were affected by a syndrome of malabsorption with various clinical symptoms. Diarrhea appeared in 2 of the children at birth, and in the third child at six months. The diarrhea led to failure-to-thrive, muscular wasting and abdominal swelling. However, the children improved spontaneously over the years. During childhood all 3 had manifest steatorrhea. Serum cholesterol was between 39 and 100 mg/dl, while triglycerides were normal to high. Reevaluation during the past year revealed areflexia, deficiency of vitamins A and E and of apoproteins A and B, and prolonged PT time in 2 of the children. Electron and light microscopy of small intestinal biopsies revealed vacuoles in the enterocytes. Electrophysiological tests revealed major disturbances in sensory conduction and brain-stem function. These cases differ from those described in the literature. Although in hypobetalipoproteinemia, 1 of the parents would be expected to be heterozygous and have low serum levels of APO B, in this family the parents had normal levels. Their children had low levels of serum APO A, while in patients with hypobetalipoproteinemia the levels are normal. There is a report of a case of deficiencies of both apolipoproteins, but the patient was asymptomatic, had chylomicronemia after a prolonged fast, and lower cholesterol levels than our patients. 8 other cases of apolipoprotein deficiency have been reported with biochemical characteristics similar to those of our patients, but with retention of chylomicrons in the small intestine.

Our previous studies have shown that cholecystokinin and pilocarpine are known to be extracellular messengers promoting the release of immunoglobulins A and G antibody activity in the lumen of the rat intestine. In the present study, which was also performed in rats, we show that CCK also promotes the translocation of albumin, electrolytes, and water into the lumen of the intestine. The effect of CCK on the translocation of immunoglobulins, albumin, and electrolytes is reduced by the prior injection of the calcium-channel blocker verapamil and the chloride-channel blocker furosemide. Taken together, the above observations suggest that the translocation of immunoglobulins, albumin, and electrolytes in the intestine appears to be stimulated by identical mechanisms and to proceed simultaneously.

Following previous observations that medium chain triglycerides (MCT) are absorbed from the stomach of suckling rats, this study was devoted to studying absorption of MCTs in human infants. Four groups of patients were studied: (a) infants suffering from pyloric stenosis, (b) premature infants, (c) children suffering from cystic fibrosis, (d) infants with miscellaneous conditions. Infant formulae with known amounts of MCT were introduced by gastric tube and samples were removed at 0, 20, 40, and 60 min. In patients with pyloric stenosis there was an 18.1% decrease in MCT during the first 20 min. No significant changes in MCT took place during the subsequent 40 min. A similar response was observed in the group of premature infants. Older infants with miscellaneous diagnoses and children with cystic fibrosis showed an even rate of disappearance of MCT during the 60-min test period, and approximately 30% of the original MCTs present disappeared during this period. We conclude that MCTs are absorbed in the stomach of infants and children. Absorption appears to improve with age. Because MCT are an important constituent of formulae for premature infants and children with defects of small intestinal digestion and absorption of fat, these observations have practical implications.

Chronic neuropathic intestinal pseudoobstruction is a rare entity, characterized by recurrent episodes of bowel obstruction without a mechanical obstructive cause. We report five members of two Jewish-Iranian families in whom chronic neuropathic intestinal pseudoobstruction was associated with an identical and unique progressive severe neuronal disease. It appeared within the first two decades of life. The disease consisted of external ophthalmoplegia, ptosis, and severe sensory and motor peripheral neuropathy. Three patients also had neuronal hearing loss. There was no evidence of central nervous system involvement and all patients were mentally intact. The combined disease was confirmed by radiologic, electrophysiologic, and histologic studies. Specific nutritional deficiencies, toxic elements, and systemic diseases affecting both the gastrointestinal tract and the nervous system were ruled out. It seems that these patients suffer from an autosomal recessive, presently unrecognized variant, of chronic neuropathic intestinal pseudoobstruction. In a patient with severe peripheral neuropathy of unknown etiology associated with symptoms suggestive of intestinal obstruction, the possibility of chronic neuropathic intestinal pseudoobstruction has to be considered.

The object of this study was to ascertain the frequency of postinfectious cow's milk protein hypersensitivity (CMPH). Twenty-four infants less than 3 months old were included in the study. Following hospitalization for acute gastroenteritis, the infants were given a protein hydrolysate formula for a period of 6 weeks, after which an intestinal biopsy was performed. Thereafter, a milk challenge was given. The existence of CMPH was defined as a postchallenge reduction of one or more of the mucosal disaccharidases below the normal levels for our laboratory. A bacterial etiology of the gastroenteritis was found in 10. Nineteen infants had no adverse reaction to cow's milk after 6 weeks on a hypoallergenic formula. Only two could be confidently diagnosed as having developed secondary CMPH; both had been infected by Escherichia coli 0 111. One infant had primary CMPH and one extra-intestinal CMPH. The incidence of secondary CMPH with gastrointestinal manifestations in this series was considerably less than described elsewhere.

We have shown previously that MCT are hydrolysed and absorbed from the stomach of suckling rats. We now report evidence that MCT are absorbed from the stomach of infants. Three groups of infants were chosen: 5 suffering from pyloric stenosis (P.S.), 7 from prematurity and 5 from miscellaneous problems. Infants with P.S. were chosen because of the delayed gastric emptying inherent to this condition so that the more rapid disappearance of MCT as compared to LCT must be due to absorption rather than to possibly more rapid gastric emptying of MCT. To each infant 10 ml/kg of formula were administered by gastric tube. Prematures received Enfalac (50% of fat as MCT) while the other groups received Pregestimil (40% MCT) (Mead-Johnson Co, Evansville, 111). Aliquots of 3 ml. were removed at 0, 20, 40 and 60 minutes. We found that in the P.S. group 35% of Total MCT were absorbed in the first hour. Corresponding figures for the prematures and the miscellaneous groups were 22.8% and 58.5% respecticely.C8 was absorbed more rapidly than C10. These results show that MCT are absorbed from the gastric mucosa of infants. In view of the presence of MCT in breast milk and in infant formulas, this may be of physiological importance.

A 4 year old girl with congenital nerve deafness and pancreatic insufficiency had incapacitating ataxia. Electrophysiological studies of the median nerve and the brain stem evoked response were abnormal. Serum vitamin E concentration was low. After intramuscular injections of vitamin E the ataxia disappeared and electrophysiological variables reverted to normal.

A 10-month-old infant is described who suffered from extensive atopic dermatitis, failure to thrive, hypoalbuminaemia and oedema. Large amounts of sticky exudate were lost through the skin and were shown to be rich in albumin. As renal and intestinal loss of protein was excluded, the patient's condition was ascribed to the loss of albumin through the skin at a rate that out-stripped the synthesis of this protein. Treatment with steroids resulted in dramatic clearing of his dermatitis, and subsequent rapid correction of his hypoalbuminaemia, oedema and anaemia.

We have previously shown that preduodenal lipases account for 50% of the lipolytic capacity of 14-day-old rats. The present investigation was designed to study the kinetics of and optimal conditions for absorption of fat in the stomach of suckling rats and its subsequent distribution in the body. After the simultaneous instillation of medium-chain triglycerides (MCT) containing 1.25 microCi 2,3-[3H]trioctanoate and of long-chain triglycerides containing 1.25 microCi 1-[14C]glycerol trioleate into the stomach ligated at the pylorus, we were able to show that gastric absorption of fat is limited to MCT. Two and a half minutes after injection, 88.6% of the radioactivity in the wall of the stomach was associated with free fatty acids, proving that lipolysis had preceded the absorption of the majority of the MCT. The remainder of the radioactivity was found in mono-, di-, and triglycerides as well as with cholesterol ester and phospholipids. In the plasma, peak radioactivity was attained within 2.5 min and a steady state ensued which lasted at least 30 min. Over this time period, specific radioactivity continued to rise in the liver, suggesting that hepatic uptake proceeded at the same rate as gastric absorption. Uptake could also be demonstrated in the three other organs tested, the lungs, the heart, and the kidneys. Absorption of MCT at pH 3 was only 20% of absorption at pH 6, which is the physiological pH in the suckling rat stomach within the first 10 min after a feed. Both at pH 3 and at pH 6, the addition of sodium taurocholate increased absorption of MCT over threefold. It is likely that the absorption of MCT by the stomach is a physiological event in the suckling rat.

In view of the technical difficulties inherent in using stool fat estimations as a parameter of malabsorption, we used a fatty meal absorption test. Children under investigation for failure to thrive were divided into two groups, those having a normal stool fat output (less than 3.2 g/day) constituting the control group, and those having steatorrhea. After a fatty meal containing 25 g of margarine and 25 g of butter fat, we measured the rise of serum triglycerides and chylomicrons hourly for 5 h. Serum triglyceride rise of less than 100 mg/dl or less than 100% above basal values and the appearance of less than 7% of chylomicrons were considered pathological. Of our control group 95% had a normal rise of triglycerides, and 96% of our patients with steatorrhea had an abnormal rise. This test was more reliable than the two-point triglyceride test previously described for the diagnosis of fat malabsorption. The fatty meal test as described here is considered to be a useful test of absorptive function.

Summary: A substantial portion of rat milk triglycerides was hydrolyzed in the ligated stomach of suckling rats with excised lingual gland and pancreas, due to the action of gastric lipase. Free fatty acids were the main lipolytic products. There were some diglycerides and traces of monoglycerides. Medium chain length (C8-C12) fatty acids were predominantly recovered in the free fatty acid fraction, whereas the remaining tri- and diglycerides became richer in long chain (≥C14) fatty acids suggesting a preferential lipolysis of medium chain fatty acid ester bonds. The lipase activity in extracts of stomach wall and sublingual gland tissue was more stable at acid pH and more resistant to the action of pepsin than the activity of pancreatic lipase. Trypsin strongly affected lingual lipase activity but only moderately reduced gastric and pancreatic lipase activity. Presence of sodium taurocholate made the lingual and gastric lipases less sensitive to proteolytic attack. It was also found that the activity of gastric lipase, related to the tissue protein content, decreased with the age of rats, whereas that of lingual lipase increased. The joint capacity of the stomach and lingual gland lipases amounted to about 50% of the total digestive lipolytic capacity 6 days after rat birth but decreased to about 20% at 60 days of life. This was due mainly to the considerable increase in the pancreatic gland size. Speculation: Lingual and gastric lipases are distinct enzymes with a mildly acidic pH optimum. They are stable in acid medium, resistant to peptic proteolysis and able to split all three ester bonds on the glycerol molecule. These properties enable them to efficiently digest milk triglycerides in the stomach of the newborn. There is a carry-over of digestive activity by lingual and gastric lipases into the upper intestine where they supplement the action of pancreatic lipase and complement it with respect to lipid emulsification. Gastric lipase seems important in intestinal lipolysis because since it is activated by bile salts, the presence of which protects the enzyme against tryptic proteolysis. Although the relative contribution of gastric and lingual lipases to the overall lipolytic capacity falls short of that of pancreatic lipase, it is likely that the extrapancreatic lipases are compensatory in conditions of pancreatic lipase deficiency.

A lipase activity of gastric origin was demonstrated by in vivo cleavage of medium and long-chain triacylglycerol substrates in the stomach of newborn rats with ligated pylorus and oesophagus and excised pancreas and lingual glands. The release of lipase activity from stomach tissue slices was also shown on in vitro incubation with histamine or pentagastrin.