Characterization

Characterization - informa Scandinavian Journal of...

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Unformatted text preview: informa Scandinavian Journal of Gastroenterology, 2008; 43: 1489—1496 healthcare ORIGINAL ARTICLE Characterization of a,a-trehalase released in the intestinal lumen by the probiotic Saccharomyces boulardii JEAN-PAUL BUTS', CATHERINE STILMANT‘, PAUL BERNASCONIZ, CHRISTIANE NEIRINCK‘ & NADINE DE KBYSER‘ 'Faculzy of Medicine, Universite' Caiholt'que de Lauriai'n, Laboratory of Paediatric Gasmenmmlogy and Nutrition, Cliniques St Luv, Brussels, Belgium, and zinbamwires Bibcodrx, Gentilly, France Abstract Objective. Trehalosc intolerance due to m,m-trehalase deficiency has scarcely been studied. The purpose of this study was to measure m,u-trehalase activity in intestinal biopsy samples from 200 consecutive patients over a period of 6 months, and to characterize a,u-trehalasc released by the probiotic Saccharamyces boulardii (S. baulardt'i). Material and methods. Enzyme activities were measured in human and rat intestinal mucosa] samples using the micromcthod of Messer & Dalqvist. d,d—trehalase from S. baubrdii was immunoptccipitated and Western blotted using an 136 purified antibody raised against a 23 amino acid peptide of m,n-trehaiasc of S. cerevisiae. Results. Among 200 patients, most of whom complained of abdominal symptoms and diarrhoea, l8 [9%) had total u,u»trchalase deficiency (0—12 Ut‘g mucosa) and 39 had partial deficiency (3712 Ulg mucosa). Only 4 patients (2%) presented selective ot,d—trehalsse deticimcy with otherwise normal disaccharidascs. Expressed per gram of powder, ct,n—treha1ase from S. boulardif delivered in viva an activity ITS times higher than that ofhuman trehalase per gram of intestinal mucosa. V”. (22 $0.43 umol) and Km (5 mM.) were close to that ofthe human enzyme, whereas Western blot revealed a signal of two subunits of 82 kDa. Finally, treatment of rats with S. batdardi'i' resulted. in increases in n,n.—trehalase activities of 25 to 45% ((2 <0.0 l) in endolominal fluid and intestinal mucosa compared with in controls. Conclusions. Our data suggest that u,u-trchalase deficiency is more common than is believed and that oral administration of S. boulara‘ix' could be beneficial in patients with digestive symptoms caused by trehaJose intolerance. Key Words: mar—Ticketing, human small intestine, pmbianc, rat small intestine, Saccharumyces baulardfi signs of trehalose intoleranCe in response to a ZS-g oral trebalose load test. Murray et al. [4] estimated that 2% of the Caucasian population has a very low activity of trehalase (below 4 Ulg protein) or has virtually no enzyme activity at all. Like sucrase- Introduction Trehalose is a disaccharide, the main dietary source of which is mushrooms. It has been approved as an additive in the preparation of dried foods. Isolated intestinal trehaiase deficiency is found in 8% of Greenlanders [1]. Although congenital trehalase deficiency is rare [1], secondary trehalase deficiency is more usual. Activity may be significantly reduced in untreated coeliac disease, in acute and chronic cnterocolopatbies and in patients with chronic ab— dominal symptoms of unknown origin. Arola et al. [2,3] showed that maldigestion of trehalose causes abdominal symptoms similar to those in lactose intolerance including flatus, hypermeteorism and loose stools or diarrhoea. Among 64 adult subjects with abdominal symptoms, 19 experienced clear isomaltase, human ot,u-trehalase is anchored to the intestinal microvillus membrane, and is a homodi- meric mayme and a glycoprotein with glycosidase activity. Sacchammyces boularrlii is a non—pathogenic yeast exhibiting therapeutic properties in acute and chronic enteropathies, irritable bowel syndrome, antibiotic-associated diarrhoea, and enterotoxigenic Closn't'dium di'flicile infections [5,6]. In human volun- tccrs [7] and in growing rats [8], lyophilized preparations of S. boulardi't' produce trophic intest- inal effects including increases in the specific and Correspondence: Jean»Paul Burs. MD PhD, Family of Medicine, Universite' Cathohqne de Louvain. Laboratory of Paediatric Gastroenterology and Nutrition, Um! of Paediatriu. 10 Avenue Mounicr. Cliniques St. Luc, Brussels, EE-I 200 Belm'urn. E-mni]: [email protected] (Renewed 8 April 2003,- accepted :5 jun.- 2008) ISSN 0036-5521 prino'lSSN l502-77DS online I'- 2008 Informs UK Ltd. DOI: ID. [USO/00355520802308862 1490 1-1? Burs 21 of. total activities of brush—border membrane enzymes [7,8], enhanced secretion of s—IgA in intestinal fluid [9] and marked stimulation of sodium-dependent, D-glucose uptake with a corresponding increase in the sodium D-glucose co-transporter—l (SGLT—l) [8]. These effects are at least partly mediated by the endoluminal release of polyamines [10], as yeast cells contain substantial amounts of spermine and spermidine [11], and by the endoluminal release of yeast enzymes such as sucrose [7,12], leucine ami- nopeptidase [13] and a novel protein phosphatase that inhibits Escherichia 0011' endotoxin by depho- sphorylatiou [14,15]. To further study the trophic effects of the probio- n'c S. boulara'ii, we identified and characterized the properties (pH optimum, Km, me, mol weight) of a yeast, tz,nt-trehalase, isolated from S. buulardii cells, and measured its activity in the lumen and intestinal mucosa of rats treated with S. boulardii or with saline controls. We also measured the enzyme activity in the lyophilized preparation of S. baulardir' and in intestinal biopsy samples from 200 consecutive patients along with other disaccharidase activities. Material and methods Media and culture conditions S. baulardii cells were inoculated in YPD (yeast extract, 0.5%; peptone, 2%; glucose, 2%; DIFCO, Detroit, Mich, USA) media and were grown at 30”C with moderate shaking, as described [13]. To disrupt the external capsid, yeast cells were concentrated (1.45%.50 x 10m cellslml) and shaken with beads (diameter OAS-pm) under cold C02 flux by using an MSK pulse device (Braun, Paris, France) [13]. After stabilization in phosphate—buffer 0.01 M (pH =7), or maleate boiler 0.1 M (pH =65), particulate components were removed by centrifuga‘ don (500g) for 15 min at 0°C and the supernatants were stored at —70”C in liquid nitrogen until analysed. Animals and treatments The study was approved by the Animal Welfare Committee and the Human Ethics Committee of the Catholic University of Louvain, Faculty of Medicine. Litters of rats were reduced to six pups per lactating mother to equalize conditions of nursing and feed- ing. For ontogenic studies, pups were killed during the suckling, weaning and post-weaning periods. To determine whether, oral administration of lyophilized S. boulardi'z' can influence endoluminal ma-urehalase activity, growing rats were treated from day 15 to day 20 postpartum because at this time, t1,d-trehalase activity is low in the rat jejunum as well as in the ileum. S. boulardi'z' was prepared in lyophilized form (100 mg per flask, biologic activity 2.9 x 109 viable cellslml) by the manufacturer (Biocodex, Gentilly, France). As previously reported [7—10], we used a dose of 50 ug lyophilized yeast cells per gram body- weight (b.w.) per day. The appropriate dose was administered in 0.1 ml saline by nasogastric intuba- lion twice daily from day 15 to day 20. Control groups were treated according to the same schedule and received equal volumes of saline. Nine to 11 animals per group were studied during the weaning period of induction of the enzyme activity. Collection ofendoluminal fluid On day 20 postpartum, the rats were killed by decapitation, and the small intestine from the pylorus to the ileocaecal valve was immediately excised. The total length was measured and divided into two equal segments. The proximal half was considered the jejunum and the distal half the ileum. For collection of intestinal endoluminal fluid, jejunal and ileal segments were flushed with 2 ml cold 0.9% saline. The collected fluid was centrifuged (500:, 5 min) and the supernatants were pooled and filtered through a 02-pin membrane filter (Millipore Corp., Bedford, Mass, USA) to discard yeast cells in suspension. As a result, the enzyme activity mea- sured was the total endoluminal enzyme activity delivered both by oral S. boulardii and by intestinal cells extruded from the villi. Intestinal mucosa! biopsy samples a,u-Trehalase activity was also assayed on hot-now genates of duodenojeiunal biopsy samples from 200 children and adult patients who underwent an upper gastrointesnnal (GI) tract endoscopy for digestive symptoms. Activity of the other disaccharidases (lactase, maltase and saccharase—isomaltase) was also assayed. Lyophilized prepay-emu: of S. boulardx'z' ago—trebalase activity was also measured on lyophi- lized preparations of S. boulardii, freshly prepared by the manufacturer (Biocodex) on cells having a biological activity of 2.9 x 10° viable cells. Enzyme assays mat—trehalase activity was measured on suspensions of S. boulam‘ii cells, intestinal fluid, purification buffers and intestinal mucosa! samples using ttehalose as o,ot—1'i'ehalase released from S. boulardi'i 1491 Table 1. Among 20 species of microorganisms (bacteria, fungi) matching with the sequence Chosen of 23 amino acids ('DPHRVEAEYGNQGADFKGAATEGZ‘) 11,:1-Irchalasc or Samhamnrycer muons on Blast search, “3‘ 7‘" the most representative matching sequences are listed below. Enzyme (EC 3-2-1-28) Species Identities Match 1. u,a~irehalase neutral Saxhamrryao cerwiriae 23123 [00% 2. mn-trchalase neutral Enemarhw'um gntsypa'i 21/23 91% 3. u,a-trchalsse neutral Kiuyommyce: Ian-o 21/23 91% 4. n,m—trehslase neutral Candida glabmm strain (335138 21123 91% 5. at,a-u‘ehalise neutral Candida albicaru strain SC5314 19f22 86% 6. m,n-rrehalase neutral Aspergfll'm nidulans 19/23 82% 7. at,u—erehalase neuu'al Schizomcchnmfigmes pombe 18/23 78% (fission yeast) substrate in maleate buffer (0.56 M, pH 6.0) using the micromethod of Mcsser & Dahlqvist [16]. Unless otherwise indicated, assays were performed at 37"C for 60 min. One unit equals 1 tunol of glucose formed per minute and per gram of protein. Protein content was determined by the method used by Lowry er a]. [17]. By convention, total enzyme deficiency was considered for activities ranging from 0 to 2 Ulg protein- 1, while activifies raging from 3 to 12 U/g protein'1 were considered as a partial deficiency. Immunaprecipimtion and immunoblom'ng To demonstrate the production by S. boulardii‘ of an enzyme protein with md-trehalase activity, a peptide (‘DPHRVEAEYGNQGADFKGAATEGZo corre- sponding to a highly conserved sequence of mo:- trehalasc of 8. “resulting was synthesized (see Table). This peptide matched with ot,ot-trehalase of 20 species of microorganisms (bacteria and fungi) including Schizasaccharamyces pombe (78% identities with the above sequence). The Table presents a list of the most representative microorganisms (match 78—] 00%) whose u,a—trehalasc has identities in common (18/23 to 23/23) with the sequence synthe- sized. Rabbits were immunized with the above peptide corresponding to a 23 amino acid sequence of S. czrem‘st'ae. A polyclonal antiserum was gener— ated and IgG were purified. Fresh samples of viable S. baulardif were suspended in phosphate buffer (0.01 M, pH 7) containing antiproteases (lenpep- tine, pcpstan'n, PMSF). The samples were ultraCen- trifuged at 102.000g at 4°C for 80 min. The supemates were collected and again centrifuged 20.0003 at 4°C for 25 min. The collected supemates were frozen in liquid nitrogen at — [70°C until use. Protein concentrations were measured in samples of the supernates (~47 mg/ml). On the day of the experiment, S. baulardii super- natcs were diluted, respectively, 4—, 10—, 16— and 40— fold with radioimmunoprecipitation assay (RIPA) buffer (TRIS 0.025 M, Triton X100 0.5%, Non-Ide P40 0.5%) containing antiproteases (10 til) pepsta- tin, leupeptinc and PMSF. To S. boulardii suspen— sions, 100 “.1 protein A Sepharose 4B, diluted in RIPA buffer (III), was added to each sample and mixed by rotation for 4 h at 4"C. Thereafter, the samples were centrifuged at 24.000; for 5 min at 49C. The pre—cleared supcmates were collected and mixed with 10 [.11 IgG purified anti-a,ot—trehalasc antibodies by rotation overnight at 4°C. Thereafter, 100 pl protein A sepharose 4B was added to the samples and mixed by rotation for 4 h at 4°C. The sepharose beads were then washed twice with RIPA buffer and once with TRIS 10 mM buffer. After the last wash, 5 pl bromophenol blue (lnvitrogen, Carlsbad, Calif., USA) diluted in 10 p] aqua milliQ was added to the heads, the supemates having been discarded. Immunoprecipitation and immunoblot— ting were carried out using the one-step complete IP-Western ltit (Genescript Corporation, Piscataway, N.J., USA). This novel procedure allows the detec- tion of nanograms of antigen by chemolurninescence (ECL) without showing co-immunoprecipitation of the heavy and light chains of the lgG antibody. CORRELATION TREHALASE (n = 74 ) LACTASE (n = 74: Figure 1. Correlation between n-chalase activity (n=74) and lactasc activity (n :74) in patients with low lactlse activities. The correlation (r=0.56) is positive and is highly significant. (p<0.0001). I492 1—]? Bun et :1]. Calculation: and statistics Statistical analyses were carried out using ANOVA followed by a multiple comparison test (Newman— Keuls) using GraphPad prisms? (GraphPad Soft— ware, San Diego,Calif., USA). Differences between means were considered to be statically significant when the p—value was less than 0.05. All units represent means fiSD, unless otherwiso indicated. Results Patient: From October 2006 to April 2007, biopsy samples collected from the distal duodenum (3rd and 4th segments) of l 44 adults (mean age 43 :17 years) and 56 children (mean age 5:2 years) were analysed specifically for the activity of disaccharidases including the activities of amt—trehalase, neutral iactase—phloridzin hydralase, sucrase—isomaltase and maltase—glucoamylase. Adults underwent biopsies mainly for lactase deficiency and abdominal symp- toms due to lactose intolerance, irritable bowel syndrome and digestive complaints of unknown aetiology including abdominal distension, cramps and diarrhoea. Children underwent biopsies mainly because of suspected coeliac disease, food intolerance, lactase deficiency and chronic entcropa- thies with diarrhoea. Among the 200 biopsy samples (105 F, 95 M), 18 patients (9%) had total deficiency in r1,rt-trehalase (0—2 U/g protein), 39 895%) had partial deficiency (3‘12 U/g protein) while the remainder of the group (143) had normal 11,11- trehalase activity (13—96 U/g protein) (71.5%). Thus, 57 patients (30 adults and 27 children) had total or partial trehalase deficiency which in this series represents 28.5%. Considering patients with ct,a—trehalase deficiency with otherwise normal disaccharidases activities, 4 patients on 200 (2%) were found to have an isolated total at,ot—trehalase deficiency (0—2 Ulg protein) while 14 patients among 200 (7%) had alactasia (0—2 Ui'g) with an otherwise normal enzyme pattern. In Figure 1 it is shown that, for otot TREHALASE S.buu lard“ 22 20 18 16 ...n h N Activity (Units.g protein -1l 6 m 2 4 6 I NO EDTA 16 E! EDTA[20mM] u 12 .é a) § 8 3.- DJ 2 4 (n=11)(n=9) [pH]=6 3 1O 12pH Figure 2. Variations in u,o—trehalase activity measured on suspensions of S. baubrdil' cells in relationship with variations of the pH buffer. The enzyme activity peaked between pH4 and pH 6 and required the presence of cofaetors, since addition of EDTA (2031M) significantly lowered the enlyme activity. SUBSTRATE VELOCITY as Vmu=22 umul 40.43 = 5 20 Km mM 15 1|] V [ll/9} I 0102030105030 (5) ml SUBSTRATE CONCENTRATION Llnewoavor—Burk '01:: (1.25 can 0.15 1.00 1.25 "Km “(5, Figure 3. V...“ of the partial punfied enzyme was 22 itmoles $0.43 (SD) when using u,a-trehalose as substrate while Km was estimated to be 5111M. the whole group, there was a significant (p<0.001 R=O.56) correlation between the activity of 01,0!- trehalase and that of neutral lactose, which suggests that moi-Whale“ is readily denatured, like neutral lactase. However, for 74 patients with partial or totaI, mot— txehalase audior neutral lactase deficiency, the ratio of trehalase/lactase was 2.56 1-5.69 (SD) with a range of O to 37.7, while for the same patients the ratio of trehalase/sucraso was 0.40 10.16 (SD) with a range of 0 to 1.13, indicating that the ratio of trehalaselsucrase is a much better parameter in confirming ct,ot-trehalase deficiency because of much closer values than the ratio trehalasellactase, which has a very wide scatter of values. u,o{-1'i-ehalase released from S. boulardi'i 1493 2,1-trehalasefmm S. baulardt'i snot-trehalase activity and protein content were first measured in suspensions of S. baulardiz' viable cells. S. boulardi'i supplied about 700 units per gram of lyophilized powder, whereas the human small intes- tine exhibited an activity of only 4 units per gram of mucosa. Figure 2 shows variations in oi,oi-trehalase activity measured on suspensions of S. boulardii' cells in relationship to variations of the pH buffer. The enzyme activity peaked between pH4 and 6, and required the presence of eo-factors (Ca2+, Ki) since the addition of EDTA (20 mM) significantly lowered the enzyme activity Because we used a homogenate of whole cells, it is likely that the enzyme activity measured reflected both neutral soluble and acid vacuolar (Lot-trehalase [13,19], with a resulting pH of 5. As shown in Figure 3, V"...K was 22 nmol:0.43, while the Km was estimated to be 5 mM. These values are close to those measured for at,u—ttehalase of S. cerwinhe [18]. Figure 4 shows an immunobiot with 4 lines (A, B, C, D) of immunoprecipitated u,u—trehalase either with the whole antisera (A, B, C) resulting in a weak signal or with the purified IgG fraction (D) resulting in a stronger signal of two subunits of 80—82 kDa. This mol mass is close to the molecular mass estimated for the neutral a,a—trehalasc monomer of S. cerevisiae (86 kDa) [19,20]. Animal treatment Ontogenie changes of ot,ot—trehalase activity in the jejunum and ileum of growing rats (Figure 5) revealed that the enzyme activity is virtually absent during the suckiing period, as is sucrase [ll], and is triggered mainly in the jejunum by day 16 postpartum. In consequence, we treated weaning growing rats with lyophilized S. boulardi't' (50 pg/g b.w.) given by nasogastric intubation of 0.1 ml twice daily from day 15 to day 20. Control rats were treated with equivalent volumes of saline 0.9%, twice 5.3. PURIFIED ALPHAALPHA TREHALASE A A.B,C. I WHOLE AN'I'lBERUIl o - Ice PURIFIED B C D '9 Figure 4. lmtnunoblotting of immunoprecipitated mix-neiulne either with whole antigen (lanes ABC) orwith lgG purified (lane D) {mm precleared S. baulurdz'i cells. Each lane reveals a signal of 2 subiunim of 80 ~82 kDa. 1494 5-1? Butt et (21. 0:0: TREHALASE 160 I?!) ENZYME SPECEFlC ACI' MTV Unltst;l ptotem 1 40 ON'I'DGENV JEJUN-UM AGE: DAYS FOSTAPARTUM. Figure 5. Ontogenic changes of a,a-trehalasc activity in the iciunum and ileum of growing rats. Enzyme activity is virtually absent during the suckling period and is triggered by day to post-partum weaning). daily during the same period. We found no differ- ence between the two groups in body-weight gain, intestinal length, mucosal mass and intestinal pro- tein content. The results of ot,at-trehalase activity measured in the endolurninal fluid and in the intestinal mucosa, expressed in milliunits per milli- gram protein and in milliunits per millilitre endo— lutninal fluid, are depicted in Figure 6. In the endoluminal fluid, filtered to discard S. baulardt'i cells, the enzyme activity was significantly (p <0.01) increased by 25% and 40% compared with the activity measured in control rats, while in the intestinal mucosa, the activity Was at least two times higher in treated rats than in controls. Discussion When given orally as a lyophilized preparation, S. boulardt't’supplies a high level of at,tt-trehalase activity in the small—intestinal lumen that represents an activity 175 times higher than that of at,nt-trehalase measured in the human small intestine, when data are expressed per gram of powder and per gram of intestinal mucosa. This massive supply in cut- trehalase by S. baulardt‘z' is further confirmed by the significant increases in enzyme activity in the in- testinal lumen and intestinal mucosa of rats treated with S. boulara‘t't' compared with saline—treated con- trols (Figure 6). In practice, our data suggest that trehalase defi- ciency is more common than believed and that in patients with u,ot—treha1ase deficiency oral treatment with lyophilized S. boulara’t't' could increase intestinal trehalase activity and could be beneficial in improv- ing their symptoms related to trehalose intolerance. A similar situation has been observed and pub- lished [21] for pan‘eno‘. with sucrase-isomaltase deficiency because the yeast supplies around 800 units sucrase per gram of lyophilized preparation [7]. Although isolated primary or congenital 01,0:- trehalase deficiency (0—2. U/g protein) appears to be rare [4], the true incidence of secondary forms of ot,ot—t:rehalase deficiency and partial deficiency re- mains unknown but could be more frequent than an: TREHALASE [D 20) N III In tat 3 L2 ENDOWMNN atth mum pm -I S Wlemgmi ll 1 C T C mucosa. WV mu mg mud punt-t S 9 l 8 I C Figure 5. Changes in ct,tt-trel'talase activity measured in the endoluminal fluid (per ml and per mg protein) and in the intestinal mucosa of growing rats treated with oral S. bodardi'i (full dark bars are n-eated rats), Results were significantly (p <0.0l) higher in treated rats (25 to 40%] than control rats. expected, especially in patients with dyspepsia caused by smoking [2]], food intolerance, coeliac disease [2,3], irritable bowel syndrome or chronic enterocolopathies [2,3]. It is noteworthy that u,tt-trehalase from S. bouiar— a’iz' exhibits sequences highly conserved between species such as the sequence from neutral S. cerevisiae which was used in the present study. Partial purification of the enzyme of S. boulardii exhibited a Va,” and 3 Km close to neutral mm-trehalase of S. cerevirme. The same similarity was noticed for the two subunits evidenced on SDS gels of ~82 kDa of mo] mass. The mol weight of the unprocessed precursor of neutral a,ot-treha1ase of S. cerevisiae is 89,675 kDa [18,19] while the unprocessed precursor of human at,u-trehalase monomer is 66,595 kDa with a pI of 5.34 [23,24]. Huang et al. [18] have shown that in many organisms Lrehalase has a critical function in preser— ving membrane structure and fluidity during dehy- dration/rehydration. In S. cerwuiae, hydrolysis of trehalose depends on both neutral trehalase and acid trehalase (Athl). Athl resides and functions in the vacuole and appears to catalyse the hydrolysis of extracellular trehalose [18,19]. In a recent study of 64 subjects that were submitted to an oral load test of 25 g trehalase, Arola et al. [2] found that [9 of them experienced clear symptoms of dyspepsia and Were considered as trehalose-intolerant subjects. Subjects with poor tolerance were best differentiated from tolerant subjects by changes in breath gases (hydrogen and methane) and by the duodenal ratio of trehalase to sucrose activity. Our data are in agreement with this and show that the ratio of trehalase/sucrase is a much better indicator of trehalase deficiency becauSe sucrase activity tends to be stable while lactase activity is variable. Thus, the lower the ratio of n‘elalase/sucrase, the greater the likelihood that ot,ot-trehalase is severely deficient. The correlation between serum and duodenal trehalase activities was in the order of 0.6. Two subiects out of 64 were found to present total selective trehalase deficiency (3). Arola et al. {2] concluded that it is obvious that trehalose maldigestion can cause digestive symptoms similar to those of lactose maldigesnon and intolerance. We also found a low incidence of total selective trehalase deficiency (4 cases, 2%) but 57 patients in 200 presented total or partial trehalase deficiency. Three factors conn'ol the genesis of symptoms: 1) the low activity of small-bowel treha- lase; 2) the maldigested trehalose that causes osmo— tic flow into the colon; 3) the ability of the colonic microflora to produce gases that result in abdominal distension, flatus and eruetation. (1,11- Trehalase remixed from S. baulardl't' 1495 Further studies are warranted in the Caucasian population to record the incidence of subjects with trehalase deficiency, their related symptoms of trehalose intolerance and to determine whether in these patients oral treatment with S. boulardt't' could be beneficial for the relief of symptoms caused by trehalose intolerance. Acknowledgements We thank Bernard Hublot for helpful comments on the manuscript and the Laboratories Biocodex for financial support. Declaration of interest: The authors report no conflicts of interest. The authors alone are respon- sible for the content and writing of the paper. References [1] Gudmand‘Hoyer E, Fenger HI, Skovbierg H, Kemiflansen P, Madam PR. Trehalase deficiency in Greenland. Scand I Gastroenterol 1988;23:775—8. [2] Arola H, Koivula T, Kamnen AL, Iokcla H, Ahqu T, lsokoski M. Low mhalase activity is associated with abdom- inal symptoms caused by edible mushrooms. Scand I Gasn'oenterol 1999;34:398—903. [3] Arola H. Trehalose intolerance can be behind the abdominal symptoms caused by mushrooms. Duodecim 1999;115: 1309710. [4] Murray IA, Coupland K, Smith IA, Ansell D, Long RG. Intestinal Irehalase activity in a UK population: establishing a normal range and the efiect of disease. Br] Nut: 2000;83: 24l-5. [5] Surawicz CM, McFarland LV, Elmer G. Treatment of recurrent Clumidium dlfiiclze colitis with vmcomycin Ind Surchame haulandit'. Am J Gastroenterol 1989;84: 1255v7. [61 Burs JP, Corthier G, Deli-nee M. Sacchammyoet boulam‘ii for Claim'dium difi‘iriie—associated enreroparhies in infants. J Pediatr Gastroenterol Nuu' 1993;16:4l9e25. [7} Bets 11’, Bemasconj P, Van Craynest MP, Maldague 1’, De Meyer R. Response of human and rat small intestinal mucosa to oral administration of Sanchammynzs boulardit'. Pediatr Res 198652011924). [B] Buts 1?, De Keyser N, Marandi S, Hemms D, 50km EM. Chae YH, et al. Sacchammym buulardr'f upgrades cellular adaptation afier proximal enterectomy in rats. Gut 1999;45: 59—96. [9) Bots JP, chasconi P, Veer-man IF, Dive C. Stimulation of secretory IgA and secretory component of immunoglobulins in small intestine of rats treated with Saschammym boulardt'i. Dig Dis Sci 1990;35:25lfi. [ID] Huts JP, De Keyser N, De Raedemaeker L. Smhamnyee: bonkndi'n‘ enhances rat intestinal enzyme expression by endoluminal release of polyamines. Pedian' Res 1994;36: 522-77. [I I] Burs IF, De Keyser N, Kolanowski J, Sokal E, Van Hoof F. Maturation of villus and cry-pt cell functions in rat small intestine. Role of dietary polynmines. Dig Dis Sci 1993;38: 109l£. [l2] Jahn HU, Ullrich R, Schneider T, Licbr RM, Schieferdecker l-IL, Holst H, et al. Immunological and trophies] efl'ects of ...
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