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PubMed1990

Role of fructose-sorbitol malabsorption in the irritable bowel syndrome.

Because even after low doses of fructose and sorbitol, fructose-sorbitol malabsorption has been found in a high number of patients with the irritable bowel syndrome, an etiological role of fructose-sorbitol malabsorption in the irritable bowel syndrome has been suggested. However, these studies have been uncontrolled. Therefore, a controlled study of fructose-sorbitol malabsorption in the irritable bowel syndrome compared with healthy controls was performed. Seventy-three patients, 23 men and 50 women with a mean age 43.1 +/- 1.7 years (range, 18-66 years) with the irritable bowel syndrome were compared with 87 age- and sex-matched control subjects. Fructose-sorbitol malabsorption was determined by a breath-hydrogen test (Lactoscreen, Hoek Loos, Schiedam, The Netherlands) following an oral load of 25 g fructose and 5 g sorbitol after a 10-hour fast. Fructose-sorbitol malabsorption, as shown by an H2 peak of 20 ppm over basal values, was found in 22 (30.1%) of the patients and 35 (40.2%) of the control subjects. With a lower peak level of 10 ppm over basal values, these percentages were 45.2% and 57.5%, respectively. Also, the highest H2 peak values (15.2 +/- 2.3 ppm vs. 21.5 +/- 2.6 ppm), time to reach peak levels (110.7 +/- 5.4 min vs. 107.1 +/- 5.9 min), and area under the H2 curve (1310 +/- 219 ppm.min vs. 1812 +/- 255 ppm.min) did not discriminate between patients and controls. During the test, symptoms developed in 31 of 70 patients and in 3 of 85 control subjects (P less than 0.0001). Symptomatic patients did not differ from asymptomatic patients regarding the presence or absence of fructose-sorbitol malabsorption, H2 peak values, and area under the curve. No differences could be identified between male and female patients or controls. In conclusion, fructose-sorbitol malabsorption is frequently seen in patients with irritable bowel syndrome, but this is not different from observations in healthy volunteers. Therefore, fructose-sorbitol malabsorption does not seem to play an important role in the etiology of irritable bowel syndrome.

Adult↗
PubMedDate not supplied

Effects of fructose on D-[6-3H]-glucose uptake and sorbitol metabolism of bovine retina in vitro.

In order to study the influence of fructose on sorbitol formation, bovine retinal tissue was incubated with different concentrations of glucose and fructose, and supplemented with tracer amounts of D-[6-3H]-glucose. Combining high-performance liquid chromatography (HPLC) with radioactivity determinations allowed detection of sorbitol and fructose derived from glucose in the incubation medium. In addition, the total amount of sorbitol was measured with a sensitive bioluminescence method. In this way, it was possible to distinguish between sorbitol formation from glucose and fructose. High concentrations of glucose in the medium increased the formation of sorbitol and fructose from glucose. Addition of fructose to the incubation medium diminished the sorbitol and fructose formation from glucose although the total amount of sorbitol increased significantly. Incubating retinal tissue with an aldose reductase inhibitor decreased sorbitol formation from glucose but did not influence the formation of sorbitol from fructose. Thus, the present findings clearly demonstrate the important influence exerted by fructose on sorbitol formation. The possible significance of the present finding is discussed with respect to diabetes retinopathy and retinal osmoregulation.

Animals↗
PubMed1997

Sensitive, selective gas chromatographic-mass spectrometric analysis with trifluoroacetyl derivatives and a stable isotope for studying tissue sorbitol-producing activity.

One of the major mechanisms involved in diabetic microangiopathy is considered to be an altered polyol pathway. However, clarifying the pathophysiology is difficult due to the lack of a sensitive method for measuring the reduction of glucose to sorbitol in tissue. Here we report a sensitive and selective method for polyol measurement using trifluoroacetyl (TFA) derivatives of polyols and stable isotope-labeled D-sorbitol (U-[13C]sorbitol, 13C6H14O6, 98.7%) as an internal standard. Gas chromatography-mass spectrometry (GC-MS) using an SE-30 capillary column gave elution of TFA derivatives of sugars, polyols and U-[13C]sorbitol within 8 min, with clear separation of sorbitol. In the calibration study, the coefficients of correlation between the amount of sorbitol added and that determined in standard solutions containing 0.1-8.0 nmol sorbitol, erythrocyte mixture and liver cytosol mixture were r = 0.999, r = 0.997 and r = 0.997, respectively. The precision of the GC-MS measurement of standard solution was C.V. = 4.3%. Because glucose is used as a substrate, the method can clarify the polyol pathway under physiological conditions. With this method, Km and Vmax values of the reductase in erythrocytes were 115 +/- 19 mmol/l and 4.42 +/- nmol/min/g of hemoglobin. In human liver, on the other hand, they were 755 +/- 132 mmol/l and 0.773 +/- 0.090 nmol/min/mg of protein, respectively. This difference of Km values suggested that aldehyde reductase rather than aldose reductase is mainly responsible for reducing glucose to sorbitol in the liver. In conclusion, this newly developed method offers a highly sensitive and selective procedure for measuring low concentrations of sorbitol in various tissues and cells and should enable clarification of the kinetics of glucose reduction to sorbitol, which in turn can be used to evaluate the role of an altered polyol pathway in the pathophysiology of diabetic microangiopathy.

Adolescent↗
PubMed1983

The metabolic fate of exogenous sorbitol in the rat.

Dietary sorbitol is rapidly converted to fructose and other carbohydrates in the liver, but its metabolic fate has not been studied rigorously. Twenty-four rats were given 20.4 muCi [14C]sorbitol with 100 mg of sorbitol, and groups of six were killed at 1, 3, 6, and 24 hours after sorbitol administration. Rats were also fed 6.9 muCi [14C]sorbitol for 7 or 14 days. Serum, liver, and lens were analyzed for 14C-labeled sorbitol, fructose, and glucose by using high-performance liquid chromatography. Negligible radioactivity (1.1%) was found in the gastrointestinal content at 24 hours indicating virtually complete absorption. Most of the radioactivity was recovered in the glucose fraction in serum, liver and lens. Glucose and fructose concentrations showed some decline by day 14 compared with day 7 in serum and liver. However, in the lens, sorbitol showed a peak value at the end of the 14th day (37.5 +/- 9.9 micrograms/pair). These findings suggest that: 1) after oral administration, sorbitol is completely absorbed, and 2) that there is a finite accumulation of sorbitol and fructose in the lens in 14 days. Although the radioactive label indicated the exogenous origin of these carbohydrates, it is not certain whether the sorbitol is converted to glucose before entering and accumulating in the lens.

Administration, Oral↗
PubMed2003

Cloning, expression, and characterization of sorbitol transporters from developing sour cherry fruit and leaf sink tissues.

The acyclic polyol sorbitol is a primary photosynthetic product and the principal photosynthetic transport substance in many economically important members of the family Rosaceace (e.g. almond [Prunus dulcis (P. Mill.) D.A. Webber], apple [Malus pumila P. Mill.], cherry [Prunus spp.], peach [Prunus persica L. Batsch], and pear [Pyrus communis]). To understand key steps in long-distance transport and particularly partitioning and accumulation of sorbitol in sink tissues, we have cloned two sorbitol transporter genes (PcSOT1 and PcSOT2) from sour cherry (Prunus cerasus) fruit tissues that accumulate large quantities of sorbitol. Sorbitol uptake activities and other characteristics were measured by heterologous expression of PcSOT1 and PcSOT2 in yeast (Saccharomyces cerevisiae). Both genes encode proton-dependent, sorbitol-specific transporters with similar affinities (K(m) sorbitol of 0.81 mM for PcSOT1 and 0.64 mM for PcSOT2). Analyses of gene expression of these transporters, however, suggest different roles during leaf and fruit development. PcSOT1 is expressed throughout fruit development, but especially when growth and sorbitol accumulation rates are highest. In leaves, PcSOT1 expression is highest in young, expanding tissues, but substantially less in mature leaves. In contrast, PcSOT2 is mainly expressed only early in fruit development and not in leaves. Compositional analyses suggest that transport mediated by PcSOT1 and PcSOT2 plays a major role in sorbitol and dry matter accumulation in sour cherry fruits. Presence of these transporters and the high fruit sorbitol concentrations suggest that there is an apoplastic step during phloem unloading and accumulation in these sink tissues. Expression of PcSOT1 in young leaves before completion of the transition from sink to source is further evidence for a role in determining sink activity.

Amino Acid Sequence↗
PubMed2000

Regulation of sorbitol efflux in different renal medullary cells: similarities and diversities.

It is well accepted that organic osmolytes, including sorbitol, play a major role in the volume regulation of renal medullary cells. The signal leading to an activation of release channels during RVD is, however, poorly understood. Hypotonicity induced sorbitol efflux was investigated in freshly isolated rat inner medullary collecting duct (IMCD) cells and in rabbit medullary thick ascending limb of Henle's loop (TALH) cells biochemically or using labeled sorbitol. The time course of release was compared with changes in cell volume, measured by confocal microscopy, and alterations in cell calcium (Ca(i)) determined by Fura 2 technology. In IMCD cells sorbitol release, volume decrease and Ca(i) transients show a close temporal correlation. In addition increases in Ca(i) without volume changes stimulate sorbitol efflux. In TALH cells sorbitol release starts after a significant lag time and reaches a maximum when cell volume is already partially restored. The same discrepancy is observed with regard to changes in Ca(i) and sorbitol efflux. These studies suggest that in IMCD cells changes in Ca(i) are the main regulator for the sorbitol permeability of the plasma membrane. The sorbitol channel present in TALH cells seems to operate predominantly independently of Ca(i). Despite this diversity in signal transduction the sorbitol channels in both renal cell types appear, however, not to be stretch-activated.

Animals↗
PubMed1978

Conversion of glucose to sorbitol and fructose by liver-derived cells in culture.

Conversion of glucose to fructose and sorbitol is documented in rat hepatoma-derived cultured cells (HTC cells). After addition of 5.5 mM [U-14C]glucose to incubation medium, labeled sorbitol and fructose accumulated intracellularly at a linear rate over a period of 60 min. The sugars were isolated, identified, and quantitated by paper chromatography, gas-liquid chromatography, and enzymatic phosphorylation of fructose. Primary culture of adult rat hepatocytes was analyzed similarly and demonstrated no significant accumulation of labeled fructose or sorbitol. The basis for this difference between HTC cells and primary hepatocyte culture was examined both in terms of enzyme activities that mediate the formation of sorbitol and fructose and in terms of the catabolism of these sugars. Both types of culture (as well as extracts of intact rat liver) exhibited enzymatic activities catalyzing the conversion of glucose to sorbitol (aldose reductase) and sorbitol to fructose (sorbitol dehydrogenase). However, the cultures differed strikingly with regard to the catabolism of sorbitol and fructose. The conversion of labeled sorbitol to metabolites in HTC cells was negligible; by contrast, hepatocytes in primary culture utilized the sugars at rates comparable to that of glucose, which may account for the lack of their accumulation in primary culture. The findings suggest that the conversion of glucose to sorbitol and fructose by HTC cells may represent a retained normal liver function, one which is amplified by the inability of HTC cells to dispose of these sugars.

Aldehyde Reductase↗
PubMed1984

Interaction between xylitol and sorbitol in plaque metabolism.

Xylitol and sorbitol, when metabolized by microorganisms, are transported through the cell membrane and phosphorylated by membrane-bound phosphoenolpyruvate-dependent phosphotransferase systems. Sorbitol-6-phosphate may be oxidized by a sorbitol-6-phosphate dehydrogenase to fructose-6-phosphate and further decomposed in the Embden-Meyerhof pathway. Xylitol-5-phosphate - if not metabolized - may be toxic to the cell. There are few specific pathways known for xylitol metabolism in microorganisms. Due to structural resemblance between the xylitol and the sorbitol molecules interaction between xylitol and sorbitol metabolism is likely to occur. Xylitol - although only slowly taken up by plaque and oral microorganisms - may reduce plaque formation and cause an increase in plaque pH. Evidence for a phosphotransferase system for xylitol has recently been demonstrated in Strep. mutans, which may cause accumulation of xylitol-5-phosphate in the cell. Some studies carried out by the author and associates on acid production in the oral cavity from cell. Some studies carried out by the author and associates on acid production in the oral cavity from sorbitol in the presence of xylitol in chewing gum containing sorbitol reduces acid production from sorbitol. This may be explained by the following effects of xylitol: Reduction of plaque and the number of microorganisms on the teeth. This is thought to be a consequence of the toxic effect of xylitol-5-phosphate. Inhibition of acid production from sorbitol. This is believed to be a consequence of competitive blocking of the phosphotransferase system due to structural similarities between xylitol and sorbitol.

Acids↗
PubMed1981

Effect of sorbitol on psychomotor function: its use in alcoholic cirrhosis.

Sorbitol solution has been used to a control substance of evaluating the efficacy of lactulose therapy for hepatic encephalopathy (HE). However, recent in vitro studies suggested that sorbitol may be an inert placebo and may have therapeutic relevance. We evaluated in vivo metabolism of sorbitol in healthy volunteers and alcoholic cirrhotic patients and found that sorbitol was metabolized by gut bacteria in a similar manner to lactulose. We next evaluated the effect of sorbitol treatment on five psychomotor performances tests in cirrhotic patients. Patients receiving sorbitol demonstrated improvement in all psychomotor tests, whereas similar patients not receiving sorbitol showed no improvement. We conclude the following: sorbitol is metabolized by gut bacteria in man, sorbitol therapy improved psychomotor performance in cirrhotic patients, and previous studies using sorbitol as a control underestimated the beneficial effects of lactulose.

Humans↗
PubMed1982

Sorbitol metabolism and sink-source interconversions in developing apple leaves.

In apple (Malus domestica Borkh.) sorbitol is the primary product of photosynthesis, the major translocated form of carbon, and a common fruit constituent and storage compound. Previous work on sorbitol metabolism has revealed a NADPH-dependent aldose 6-phosphate reductase (A6PR) in green tissues, and a NAD-dependent sorbitol dehydrogenase in nongreen tissues. Results here show a decrease in sorbitol dehydrogenase activity and an increase in A6PR activity as leaves developing in the spring undergo the transition from sink to source. Sorbitol dehydrogenase activity reached a minimum as A6PR peaked. These changes were related to increases in leaf carbohydrate levels, especially sorbitol, and to increases in rates of net photosynthesis. Studies conducted in the autumn on senescing leaves also showed changes in enzyme activites, leaf carbohydrate levels, and photosynthesis. At this time, however, sorbitol dehydrogenase increased in specific activity, whereas A6PR activity, leaf carbohydrates, and photosynthetic rates all decreased substantially. Other experiments showed differences in the ability of young and mature leaves to metabolize sorbitol and in the distribution of sorbitol enzymes in leaves at transitional developmental stages. The results suggest that sorbitol metabolism in apple is tightly controlled and may be related to mechanisms regulating partitioning or source and sink activity.

Journal Article↗
PubMed1971

Sorbitol metabolism in Aerobacter aerogenes.

Sorbitol (d-glucitol) metabolism in Aerobacter aerogenes PRL-R3 is shown to proceed via the pathway: sorbitol --> sorbitol 6-phosphate --> d-fructose 6-phosphate. Sorbitol phosphorylation is mediated by a phosphoenolpyruvate (PEP):sorbitol 6-phosphotransferase system, and sorbitol 6-phosphate oxidation by a pyridine-nucleotide-linked dehydrogenase. Mutants deficient in sorbitol 6-phosphate dehydrogenase or a component (enzyme I) of the phosphotransferase system did not grow on sorbitol, whereas revertants which had regained these enzymatic activities grew normally. Extracts of the enzyme I-deficient mutant failed to catalyze the phosphorylation of sorbitol in the presence of PEP, and adenosine 5'-triphosphate could not replace the PEP requirement for sorbitol phosphorylation in extracts of the wild-type strain.

Adenosine Triphosphate↗
PubMedDate not supplied

Plasma and red cell sorbitol assay in diabetic subjects.

Plasma and red cell sorbitol concentrations, fasting plasma glucose, glycosylated hemoglobin (GHb) were evaluated in 30 diabetic patients and 42 normal subjects. Red cell sorbitol levels were evaluated in hemolysate and non-hemolyzed samples. Mean red cell sorbitol concentrations evaluated after hemolysis were 21.5 +/- 5 nmol/ml in diabetics and 12.2 +/- 4 nmol/ml in controls (p less than 0.001). Mean values of red cell sorbitol determined in non-hemolyzed samples were 13.9 +/- 3 nmol/ml in diabetics and 8.1 +/- 3 nmol/ml in controls (p less than 0.001). Mean plasma sorbitol concentrations were 8.4 +/- 3 nmol/ml in diabetics and 5.2 +/- 1 nmol/ml in controls (p less than 0.001). The within and between run reproducibilities evaluated in plasma, hemolysate and non-hemolyzed red cells gave the lowest values for hemolyzed red cell samples. The studies on stability showed that samples neutralized and stored at -20 degrees C gave reproducible values if assayed within 3 days. A positive correlation was found between red cell hemolysate sorbitol concentrations and fasting plasma levels in both diabetics (r = 0.56; p less than 0.001) and controls (r = 0.62; p less than 0.001). Red cell hemolysate sorbitol concentrations were also positively correlated to GHb in both diabetics (r = 0.64; p less than 0.001) and controls (r = 0.36; p less than 0.05). We believe the most effective sorbitol assay to be that obtained in hemolyzed red cells and that these values related to glycemic levels could be a useful index of metabolic control and an indicator of tissue sorbitol levels in humans.

Adult↗
PubMed1993

Prevalence of sorbitol in multiple-dose activated charcoal regimens in emergency departments.

STUDY OBJECTIVES: To determine the availability and use of premixed activated charcoal in sorbitol preparations during multiple-dose activated charcoal therapy in the emergency department. DESIGN AND SETTING: A prospective telephone survey of all 911 receiving hospitals within the catchment area of one poison center. TYPE OF PARTICIPANTS: Hospital pharmacy supervisors and ED charge nurses. INTERVENTION: Hospital pharmacy supervisors were surveyed about the available preparations of activated charcoal on their hospital's formulary, and ED charge nurses in these same hospitals were surveyed about the prevalence of sorbitol use in multiple-dose activated charcoal regimens. MEASUREMENTS AND MAIN RESULTS: Eleven hospitals (16%) stocked only activated charcoal in sorbitol preparations. Twenty-one hospitals (31%) had both activated charcoal in sorbitol preparations and activated charcoal without sorbitol preparations, and 35 hospitals (52%) had only activated charcoal without sorbitol preparations. Repeat dosing of sorbitol during multiple-dose activated charcoal therapy occurred in 33 of 67 (49%) of the EDs surveyed. CONCLUSION: Sorbitol dosing is often repeated with activated charcoal during multiple-dose activated charcoal therapy in the ED because of the ready availability (and sometimes exclusive availability) of premixed activated charcoal in sorbitol preparations.

Cathartics↗
PubMed2000

Sorbitol as a marker for drug-induced decreases of variable duration in liver blood flow in healthy volunteers.

OBJECTIVE: Sorbitol has been suggested as a suitable marker to assess liver blood flow (LBF), after it was shown to adequately reflect prolonged changes in LBF but changes of a shorter duration have not been investigated. We therefore used sorbitol to evaluate drug-induced decreases in LBF of variable duration with i.v. infusions of somatostatin and its synthetic analogue octreotide. METHODS: In a double-blind, placebo controlled, randomised study, six healthy males received sorbitol for 170 min. At sorbitol steady state, which was at 45 min after the start of the infusion (t=0), somatostatin or octreotide was infused for 30 min. Sampling for sorbitol assay and echo-Doppler hepatic portal vein flow measurements were done regularly and treatments were compared using ANOVA. RESULTS: The sorbitol AUC over the 30-min intervention period was 15% (95% C.I.: +4, +22%) and 13% (+5, +24%) higher compared to placebo after somatostatin and octreotide respectively. The decline of sorbitol levels after termination of the intervention was faster for somatostatin compared to octreotide, demonstrated by the difference in the AUC (0-2 h) with placebo which was 8% (-3, +19%) lower after somatostatin, and 15% (+5, +26%) after octreotide. Portal venous blood flow decreased during the 30-min interventions; after somatostatin 27% (-14, -40%) and after octreotide 29% (-17, -42%). Portal flow was lower than placebo during the entire experiment after octreotide 30% (-10, -50%), but not after somatostatin 13% (-33, +7%). Changes in sorbitol levels and portal venous blood flow occurred simultaneously and were well correlated for each individual, making it likely that the interventions did not interfere with metabolism. CONCLUSION: Sorbitol can be used to adequately assess decreases in LBF of variable duration in healthy volunteers.

Adult↗
PubMed1975

The localisation of sorbitol pathway activity in the rat renal cortex and its relationship to the pathogenesis of the renal complications of diabetes mellitus.

A series of in vivo and in vitro investigations was performed to examine the localisation of sorbitol pathway activity in the rat renal cortex and to investigate the possible relation that the acculumation of sorbitol pathway intermediates in renal cortical tissue may have to the pathogenesis of renal complications in diabetes mellitus. Neither of the sorbitol pathway intermediates, sorbitol or fructose, were detected either in intact glomeruli which had been isolated from rats rendered chronically diabetic with streptozotocin, or in metabolically active glomeruli which had been incubated in vitro in high glucose media. Such data agreed with previously published observations that the enzyme aldose reductase is not present in renal glomeruli, and suggested that changes in sorbitol pathway activity cannot be directly related to the pathogenesis of diabetic glomerulosclerosis. Sorbitol was detected in low concentrations (3.1 mu-mol/g protein) in cortical tubules which had been isolated from the renal cortex of rats rendered chronically diabetic with streptozotocin. This concentration of sorbitol was higher than that in the intact renal cortex of the diabetic animal (0.3 mu-mol/g protein) or in the cortical tubules of non-diabetic animals (0.5 mu-mol/g protein). It is apparent that the renal cortical tubule is a major site of sorbitol pathway activity in the renal cortex. However, there is presently no obvious causal relationship between the accumulation of such relatively low concentrations of sorbitol in the renal cortical tubule and the pathogenesis of glomerulosclerosis or cortical tubular lesions in diabetes.

Animals↗
PubMed1990

Diarrhea in diabetics: the role of sorbitol.

Diabetics often consume dietetic foods with sorbitol as the sweetener. Sorbitol, in amounts as little as 10 g. may produce diarrhea in healthy individuals. Sorbitol intolerance was studied in 12 diabetics and 23 nondiabetics. Similar numbers of diabetics (n = 10, 83.3%) and nondiabetics (n = 18, 78.3%) were found intolerant as judged by a greater than or equal to 20 ppm rise in postprandial breath hydrogen levels. Six diabetics (50%) and 13 nondiabetics (56.5%) developed abdominal symptoms after sorbitol ingestion. Subsequently, 100 diabetics and 100 nondiabetics were interviewed to determine the relationship between regular sorbitol consumption and abdominal symptoms. The interview revealed that (1) most individuals consuming sorbitol were unaware of its presence in their diet and (2) diarrhea was significantly (p less than 0.001) more prevalent in diabetics consuming sorbitol than diabetics not consuming it. We conclude that (1) many diabetics are intolerant to sorbitol and (2) regular sorbitol consumption may explain the "idiopathic" diarrhea in some diabetics.

Abdominal Pain↗
PubMed2002

Cross-talk between the L-sorbose and D-sorbitol (D-glucitol) metabolic pathways in Lactobacillus casei.

A gene encoding sorbitol-6-phosphate dehydrogenase (SorF) belonging to the sorbose operon (sorFABCDG) has been characterized in Lactobacillus casei. Inactivation of this gene revealed the presence of another sorbitol-6-phosphate dehydrogenase that was induced by D-sorbitol (D-glucitol). The gene encoding this activity (gutF) has also been isolated, sequenced and disrupted. The sorbitol-6-phosphate dehydrogenase genes (sorF, gutF) were required for growth on L-sorbose and D-sorbitol, respectively. Biochemical and transcriptional analyses of the wild-type and mutant strains demonstrated that L-sorbose and D-sorbitol induced sorF and the gene encoding the sorbose operon activator (sorR), while the expression of gutF was only activated by D-sorbitol. Furthermore, these studies indirectly suggested that a common metabolite of the L-sorbose and D-sorbitol metabolic pathways (probably D-sorbitol 6-phosphate) would act as the effector of SorR. The same effector would also be the inducer of gutF, although the two pathways seem to be subject to distinct regulatory mechanisms.

Bacterial Proteins↗
PubMed1987

Sorbitol as a sweetener in the diet of insulin-dependent diabetes.

UNLABELLED: We compared sorbitol given alone and as part of a mixed meal to nine insulin-dependent diabetics (IDD's) during continuous subcutaneous insulin infusion (CSII). Blood glucose, sorbitol and breath hydrogen + methane were measured following six test meals: Pure glucose, sorbitol and lactulose, a mixed meal alone, and sweetened with sorbitol and sucrose. Blood glucose increase was very small after lactulose and sorbitol, significantly larger after glucose. A considerable increase in breath hydrogen + methane appeared after sorbitol and lactulose, but not after glucose. No differences in blood glucose responses were found after the mixed meal alone or sweetened with sorbitol and sucrose. A sustained low level increase in breath hydrogen + methane occurred after all solid meals. Sorbitol was not detected in serum after any meal. CONCLUSION: Sorbitol ingested by IDD's during CSII in watery solution is not absorbed in the small intestine and causes osmotic diarrhoea. Ingested in a composite meal it does not affect blood glucose and does not cause osmotic diarrhoea.

Adolescent↗