Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “SORBITOL”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 343 records · Page 19Linked to original sources
PubMed1993

A cold-inducible Bombyx gene encoding a protein similar to mammalian sorbitol dehydrogenase. Yolk nuclei-dependent gene expression in diapause eggs.

To facilitate the study of the induction of sorbitol dehydrogenase by acclimation to 5 degrees C in diapause eggs of the silkworm, Bombyx mori, two cDNA libraries from eggs and larval fat bodies were screened with anti-(sorbitol dehydrogenase) serum, and a positive cDNA was cloned from the fat-body cDNA library. 1039 nucleotides determined from the cDNA corresponded to a protein-coding region consisting of 346 amino acids. The missing regions (containing two amino acids at the 5' end and a stop codon at the 3' end) were supplemented with the genome sequence. The deduced amino-acid sequence had 45-47% identity with mammalian sorbitol dehydrogenases. The results led us to conclude that the cDNA for a Bombyx homolog of mammalian sorbitol dehydrogenase was isolated, which was designated as BmSDH. Analyses of Northern hybridization and reverse transcription/polymerase chain reaction showed that the transcript of BmSDH occurred after chilling for 40-50 days when the diapause eggs were exposed to 5 degrees C from two days after oviposition to break the diapause. The changing pattern in the amount of BmSDH transcript was well correlated with those in the activity of sorbitol dehydrogenase and the amount of the enzyme protein in diapause eggs. Further, the transcript of BmSDH was localized in yolk cells. The results indicate that the yolk nuclei-dependent gene expression of BmSDH is induced by acclimation to 5 degrees C in diapause eggs.

Amino Acid Sequence↗
PubMed1993

Zinc coordination in mammalian sorbitol dehydrogenase. Replacement of putative zinc ligands by site-directed mutagenesis.

Rat sorbitol dehydrogenase was expressed in Escherichia coli and purified to homogeneity, resulting in a protein with a specific activity of 4.7 U/mg, close to that of the enzyme isolated from mammalian liver. A Glu residue has been postulated to replace the Cys of alcohol dehydrogenase as a ligand to the active-site zinc atom of sorbitol dehydrogenase. This Glu (position 155 in the rat enzyme) was mutated both to Cys, in order to mimic the alcohol dehydrogenase relationships, and to Ala, as a control. A third mutation, Cys164 to Ala, was also performed since Cys has also been considered as a possible zinc ligand. With Ala at position 155, an inactive enzyme was obtained, showing that correct active-site relationships have been destroyed. With Cys at position 155, the enzyme is still partly active, but rapidly looses activity unless stabilized by the addition of ZnSO4. The catalytic efficiency in the oxidation of sorbitol is 120-fold less than that of the native form, and reduction of fructose is lost completely. In contrast, the activity of the Cys164Ala mutant is comparable with that of the native enzyme and, in fact, even increased in the oxidation of sorbitol. Combined, the results strongly suggest that Glu155 is a ligand to the active-site zinc atom. Zinc analysis of the different variants of sorbitol dehydrogenase establishes that all contain one atom of zinc/subunit, also when the catalytic function is lost. Apparently, zinc remains coordinated even after replacement with an amino acid residue (Ala) unable to ligand metal atoms.

Animals↗
PubMed1994

Inhibition and activation studies on sheep liver sorbitol dehydrogenase.

Reversible inhibition and activation, as well as protection against affinity labelling with DL-2-bromo-3-(5-imidazolyl)propionic acid, of sheep liver sorbitol dehydrogenase have been studied. The results presented are discussed in terms of enzyme active-site properties and may have potential applications for drug design. Kinetics with mainly sorbitol competitive inhibitors reveals that aliphatic thiols are generally the most potent inhibitors of enzyme activity. Inhibition and inactivation by heterocyclics parallel that seen previously with sorbitol dehydrogenase from other sources as well as with alcohol dehydrogenase from yeast. However, there are significant differences in relation to the structurally similar horse liver alcohol dehydrogenase, as the catalytic zinc of sorbitol dehydrogenase is more easily removed by chelating molecules. Several aldose reductase inhibitors are shown to also inhibit sorbitol dehydrogenase, but at concentrations unlikely to be reached clinically. Enzyme activation has been observed with various compounds, in particular halo-alcohols and detergents. Several inhibitors provide competitive protection against enzyme inactivation by DL-2-bromo-3-(5-imidazolyl)propionic acid. This enables the dissociation constants for binary enzyme-inhibitor complexes to be determined. NADH protects noncompetitively against inactivation. The presence of some binary and ternary enzyme-NADH complexes is indicated from fluorescence emission spectra, as a shift in the fluorescence maximum and intensity is observed due to their formation.

Affinity Labels↗
PubMed1998

Rat renal expression of mRNA coding for aldose reductase and sorbitol dehydrogenase and its osmotic regulation in inner medullary collecting duct cells.

Sorbitol plays an important role in the osmoregulation of several renal cell types, especially the inner medullary collecting duct (IMCD) cells. Very little information is available concerning the expression of the enzymes of sorbitol metabolism (aldose reductase (AR) and sorbitol dehydrogenase (SDH)) on the RNA level under different osmotic conditions. We employed a RT-PCR-based strategy to investigate the regulation of mRNA coding for AR and SDH. For AR two primers (derived from the sequence of the rat eye lens) were chosen which amplify a 668-bp product. For SDH (considering the sequence of rat liver) three primers were chosen, amplifying a 367- and a 1, 068-bp fragment. Digestion with restriction enzymes and sequencing of the products clearly indicate that the specific mRNA of AR and SDH was amplified. By relative quantitative determination of the amplification products a more than 4-fold increase in mRNA for AR in IMCD cells was observed within 24 h after increasing the extracellular osmolarity from 600 to 900 mosm/l. Decreasing the osmolarity from 600 to 300 mosm/l resulted in a reduction in the mRNA level by 70%. The complete adaptation of the AR activity needed 3 (increasing osmolarity) and 6 days (decreasing osmolarity). Osmotically induced alterations in the levels of mRNA coding for SDH could not be observed. These results suggest that the adaptation of sorbitol synthesis occurs by a rapid regulation of transcription or stability of specific mRNA. For a complete synthesis or degradation of AR 3-6 days are necessary. Thus sorbitol synthesis in IMCD is more rapidly adapted to increasing osmolarities than to decreasing osmolarities.

Aldehyde Reductase↗
PubMed2005

Children's acceptance of milk with xylitol or sorbitol for dental caries prevention.

BACKGROUND: Xylitol, a polyol sugar, has been shown to reduce dental caries when mixed with food or chewing gum. This study examines the taste acceptability of xylitol in milk as a first step toward measuring the effectiveness of xylitol in milk for the reduction of dental caries in a public health program. METHODS: Three different types of milk (Ultra High Temperature (UHT), powder and evaporated) were tested for acceptability by 75 Peruvian children (25 per milk group, ages 4 to 7 years). Each group evaluated xylitol and sorbitol in one type of milk. In the first phase, each child was presented with a tray of four plastic cups containing 50 ml of milk with 0.021 g/ml xylitol, 0.042 g/ml xylitol, 0.042 g/ml sorbitol or no sugar. Each child was asked to taste the samples in a self-selected order. After tasting each sample, the child placed the milk cup in front of one of three cartoon faces (smile, frown or neutral) representing the child's response to the taste of each sample. In the second phase, the child was asked to rank order the milk samples within each category (smile, frown or neutral). Ranks within categories were then combined to obtain a rank ordering for all the test samples. RESULTS: The ranking from best to worst for the samples across categories (UHT, powder, evaporated) was xylitol (0.0.042 g/ml), sorbitol (0.042 g/ml), xylitol (0.021 g/ml) and milk alone (Friedman's ANOVA). Xylitol and sorbitol were preferred over milk alone, and xylitol (0.042 g/ml) was preferred to sorbitol (0.042 g/ml)(p < .05 sign test). CONCLUSION: Milk sweetened with xylitol is well accepted by Peruvian children ages 4-7 years.

Journal Article↗
PubMed2002

Main polyol dehydrogenase of Gluconobacter suboxydans IFO 3255, membrane-bound D-sorbitol dehydrogenase, that needs product of upstream gene, sldB, for activity.

The D-sorbitol dehydrogenase gene, sldA, and an upstream gene, sldB, encoding a hydrophobic polypeptide, SldB, of Gluconobacter suboxydans IFO 3255 were disrupted in a check of their biological functions. The bacterial cells with the sldA gene disrupted did not produce L-sorbose by oxidation of D-sorbitol in resting-cell reactions at pHs 4.5 and 7.0, indicating that the dehydrogenase was the main D-sorbitol-oxidizing enzyme in this bacterium. The cells did not produce D-fructose from D-mannitol or dihydroxyacetone from glycerol. The disruption of the sldB gene resulted in undetectable oxidation of D-sorbitol, D-mannitol, or glycerol, although the cells produced the dehydrogenase. The cells with the sldB gene disrupted produced more of what might be signal-unprocessed SldA than the wild-type cells did. SldB may be a chaperone-like component that assists signal processing and folding of the SldA polypeptide to form active D-sorbitol dehydrogenase.

Base Sequence↗
PubMed1990

Identification of sorbitol 3-phosphate and fructose 3-phosphate in normal and diabetic human erythrocytes.

Using 31P NMR spectroscopy, we have identified sorbitol 3-phosphate and fructose 3-phosphate in normal human erythrocytes wherein their concentrations are estimated to be 13 mumol/liter cells. Incubation of hemolysates with sorbitol, fructose and ATP suggest that both sorbitol and fructose are phosphorylated separately and directly at the 3-hydroxyl position suggesting the presence in these cells of a novel and specific kinase(s). In addition to sorbitol 3-phosphate and fructose 3-phosphate which were previously identified in the mammalian lens and sciatic nerve, erythrocytes have two extra metabolites resonating at 6.7 and 6.8 ppm in the 31P NMR spectrum. Although not identified in this study, the unusual chemical shifts of these compounds, their low pKa values and the fact that they appear as doublet in proton-coupled 31P NMR spectra, suggest that these phosphomonoesters belong to the same class of metabolites as sorbitol 3-phosphate and fructose 3-phosphate. Preliminary studies of erythrocytes from an unselected group of diabetic subjects showed an overall increase in the concentration of all four metabolites, although an overlap with normal values was noted.

Adult↗
PubMed1990

[Kinetic properties of sorbitol dehydrogenase from calf liver cell cytoplasm].

The kinetic properties of sorbitol dehydrogenase from calf liver cell cytoplasm during sorbitol oxidation were studied at pH 7.0, 7.5, 8.0, 9.0 and 10.0. It was found that the shape of kinetic curves for NADH accumulation depends on pH and substrate concentration. At pH 7.0, 7.5 and 8.0 the enzymatic reaction obeys the Michaelis-Menten kinetics with Km of 3.3 x 10(-3) M. 2.3 x 10(-3) M and 2.08 x 10(-3) M, respectively. At pH 9.0 and 10.0 the vovs [So] curves have an "intermediate plateau". The Hill plots for this reaction reveal two slopes that are dependent on substrate concentration. The nH values for sorbitol (up to 2 mM) are 1.0 and 1.16 at pH 9.0 and 10.0, respectively. With a further rise in the substrate concentration, the nH value increases up to 2.4 and 2.18 at pH 9.0 and 10.0, respectively. This is suggestive of the existence of a slowly dissociating enzymatic system of the Np in equilibrium P type (where P is the oligomeric and p the monomeric forms of the enzyme); N approximately greater than 2. The vovs NAD plots are S-shaped at all pH values studied. The data obtained are discussed in terms of regulatory effects of sorbitol and acidity on association-dissociation of sorbitol dehydrogenase from liver cell cytoplasm.

Animals↗
PubMed1990

[The thiobarbituric method for analyzing sugars. III. A method for studying sorbitol dehydrogenase activity].

A method for studying of sorbitol dehydrogenase activity of Acetobacter suboxydans has been worked out which can be applied to other microbe cells too. The enzyme transformation of D-sorbitol into L-sorbose is determined through the reaction between ketohexose and 2-thiobarbituric acid under heating in 1 M oxalic acid (pH = 0.64) medium for 15 or 30 min. The yellow-coloured product was measured at 400 nm. The method is characterized with its high specificity, good reproducibility and accuracy, which allows for its application for quantitative analysis of sorbitol in dietetic foods. For this purpose a sorbitol dehydrogenase preparation isolated from bacterial cells is needed. The main purpose of the spectrophotometric method is to use it as a control in the process of microbial transformation of sorbitol into sorbose both under laboratory and industrial conditions.

Acetobacter↗
PubMed1978

[Coenzyme-induced slow transitions of NADP-sorbitol dehydrogenase from Gluconobacter oxydans].

The kinetic properties of NADP-dependent sorbitol dehydrogenase from G. oxydans cell extract were studied at pH 8.8 and 9.3 in the direction of D-sorbitol oxydation. It was shown that the shape of the kinetic curves of NADPH accumulation in time is characterised by initial burst whose magnitude depends on the concentration of the enzyme extract used. Preincubation of the enzyme with NADP or D-sorbitol eliminated the initial burst on these curves and transformed them into straight lines coming from the start of co-ordinates. The dependence of the stationary reaction rate on the enzyme extract concentration is not a linear one. The kinetic dependences of stationary rate of the reaction catalysed by the enzyme on the concentration of D-sorbitol and NADP at pH 8.8 and 9.3 were examined under all conditions studied; the shape of these kinetic curves altered to considerable extent with the alteration of the enzyme extract concentration in the reaction mixture and pH. At pH 9.3 several intermiediate plateaux were found on the curves of the D-sorbitol concentration dependent stationary rate of the reaction. The preincubation of the enzyme extract with NADP during 1.5 h removed the intermediate plateau on these curves and made them hyperbolic. Disk-electrophoresis of the enzyme extract in PAAG concentration gradient showed that at pH 8.8 the enzyme exists in one active form, while at pH 9.3 it exists in three major and three minor active forms of the enzyme differing in their molecular weights are found. It is assumed that the enzyme from G. oxydans cell extract can exist in a great number of molecular equilibrium forms, the rate of quilibrium being comparable or significantly less than that of the enzymatic reaction. NADP significantly influences on the equilibrium of the molecular forms of the enzyme.

Hydrogen-Ion Concentration↗
PubMed1962

Parallel induction of D-arabitol and D-sorbitol dehydrogenases.

Scolnick, Edward M. (Harvard Medical School, Boston, Mass.) and Edmund C. C. Lin. Parallel induction of d-arabitol and d-sorbitol dehydrogenases. J. Bacteriol. 84:631-637. 1962.-Two inducible diphosphopyridine nucleotide-linked dehydrogenases are described in a bacterium isolated from the soil, Cellvibrio polyoltrophicus ATCC 14774. The first enzyme catalyzes the dehydrogenation of d-arabitol to d-xylulose and d-mannitol to d-fructose. The data suggest that in vivo this enzyme has the dual function of the utilization of both of these polyhydric alcohols. The second enzyme was found to act only on d-sorbitol, converting it to d-fructose. Evidence for its physiological function as a d-sorbitol dehydrogenase is also given. Both of these enzymes were found to be induced in parallel by any of the three polyhydric alcohols, d-arabitol, d-mannitol, and d-sorbitol. A common stereoconfiguration of the inducers for these enzymes is suggested. The parallel evolution of substrate specificity and inducer specificity is discussed with respect to the functional advantage that such a selective process might offer.

Alcohols↗
PubMed1998

Hepatic plasma flow estimated according to Fick's principle in patients with hepatic encephalopathy: evaluation of indocyanine green and D-sorbitol as test substances.

The magnitude of hepatic plasma flow in patients with liver failure and hepatic encephalopathy (HE) is unknown because a reliable flow estimate has not been available. The purpose of this study was to estimate hepatic plasma flow in patients with HE and to evaluate indocyanine green (ICG) and sorbitol as test compounds. Fourteen patients with acute liver failure (ALF) and nine patients with chronic liver failure (CLF), all with HE grade II or more, were studied. After hepatic vein catheterization, hepatic plasma flow was estimated by use of constant infusion, simultaneous arterial and hepatic vein concentration measurements, and calculated according to Fick's principle. The hepatic extraction fraction of D-sorbitol 0.179+/-0.144 (mean+/-SD) was higher than the hepatic extraction fraction of ICG 0.054+/-0.085 (P < .001). The low hepatic extraction fraction of ICG rendered this compound unfit for estimation of hepatic plasma flow in these patients. In contrast, by using D-sorbitol the hepatic plasma flow could be estimated in 21 of 23 patients with a median SD of 8.4% (range, 2.6% to 29%). The D-sorbitol estimated hepatic plasma flow was 1.2+/-0.5 L/min (n = 12) in patients with ALF and 1.4+/-0.9 L/min (n = 9) in patients with CLF. These values are higher than what has been reported in normal subjects and in patients with cirrhosis without HE. An elevated hepatic flow should increase oxygen delivery and may enhance the failing liver's ability to remove substances from the blood. At the same time, hepatic first pass metabolism is reduced. We conclude that an elevated hepatic flow in these patients is of clinical importance.

Adult↗
PubMed2003

Interference of bovine herpesvirus 1 (BHV-1) in sorbitol-Induced apoptosis.

In order to determine the ability of bovine herpesvirus type 1 (BHV-1) to suppress apoptosis, we examined the effects of BHV-1 infection on sorbitol-induced apoptosis on Madin-Darby bovine kidney (MDBK) cells. BHV-1 suppresses sorbitol-induced apoptosis in a manner similar to that of herpes simplex virus type 1 (HSV-1), indicating that BHV-1 has one or more anti-apoptotic genes. To elucidate the molecular mechanisms of apoptosis, expression of some genes encoding apoptosis-inhibiting and -promoting factors were analyzed on BHV-1 infected cells during the process of sorbitol-induced apoptosis. Our results revealed that the expression of bcl-2 and bcl-x(L) decreased after 5 and 3 h p.i., respectively; while bax and procaspase-3 expression increased with respect to control as a function of p.i. times and at 7 h p.i. they were not observed. We further show that the expression of p53 gene was also enhanced, suggesting that this apoptotic mechanism is p53 dependent. From these results, we propose that BHV-1 has one or more genes encoding apoptosis-inhibiting factors which interfere with the involvement of bcl-2 gene family members and apoptotic pathway, depending upon caspase-3, triggered by sorbitol.

Animals↗
PubMed2004

Potential role for the sorbitol pathway in the meiotic dysfunction exhibited by oocytes from diabetic mice.

Complications common to type I diabetes, such as cataracts and cardiovascular disorders, have been associated with activation of the polyol pathway, which converts glucose to fructose via the intermediate, sorbitol. Under normal glycemic conditions, glucose is typically targeted for glycolysis or the pentose phosphate pathway through phosphorylation by hexokinase. When glucose levels are elevated under diabetic conditions, hexokinase becomes saturated, and the excess glucose is then shunted to aldose reductase, which converts glucose to sorbitol. In the present study, we examined the potential effects of this pathway on the maturation process in mouse oocytes. Increasing concentrations of sorbitol suppressed FSH-induced maturation in oocytes from control mice. Culturing oocytes from diabetic mice in the presence of inhibitors of aldose reductase reversed the suppression of FSH-induced meiotic maturation. When oocytes from control mice were cultured with activators of aldose reductase, FSH-induced maturation was compromised. In addition, treatment with sorbitol or activators of the polyol pathway led to reduced cell-cell communication between the oocyte and the cumulus cells, as well as compromised FSH-mediated cAMP production and de novo purine synthesis. These data indicate that the suppression of FSH-induced meiotic maturation observed in oocytes from diabetic mice may result from a shunting of glucose through the polyol pathway.

Aldehyde Reductase↗
PubMed1976

Structure of aluminum hydroxide gel III: mechanism of stabilization by sorbitol.

The effect of sorbitol on the aging of aluminum hydroxide gel, prepared by the reaction of aluminum chloride solution with strong ammonia solution to a final pH of 7.0, was studied by potentiometric titration, acid-consuming capacity, pH, hydroxide to aluminum ratio, chloride activity, X-ray diffraction, and IR spectroscopy. Gels containing sorbitol lost less than 10% of their acid-consuming capacity during a 6-month aging period compared with a loss of more than 60% for an identical gel without sorbitol. The mechanism by which sorbitol stabilizes the gel appears to be inhibition of the secondary polymerization reaction which takes place upon aging. Another polyhydroxy compound, quercetin, also stabilizes aluminum hydroxide gel.

Aluminum Hydroxide↗
PubMed1987

Flocculation of suspensions containing nonionic surfactants by sorbitol.

Aqueous suspensions of sulfamerazine, salicylamide, and butamben, containing either polysorbate 20 or polysorbate 80 as a wetting agent, were deflocculated. The presence of relatively high concentrations of sorbitol in the suspensions resulted in flocculation due to dehydration of surfactant polyoxyethylene groups (reflected by the cloud point). The critical flocculation concentration of sorbitol was reduced by raising the storage temperature, lowering the surfactant concentration, switching from polysorbate 80 to polysorbate 20, or adding sodium sulfate to the suspension formulation. Both the cloud point and the sorbitol critical flocculation concentration depended on the particular drug that was suspended. Methylparaben lowered the cloud point, suggesting that the choice of preservative could influence the suspension characteristics in certain cases. The various dehydrating influences were additive. By assuming that interparticle repulsion becomes negligible at the cloud point, it was possible to use cloud point curves to estimate the critical flocculation concentration of sorbitol.

Benzocaine↗
PubMed2002

Role of sorbitol in the up-regulation of urinary bladder M(2) muscarinic receptors in streptozotocin-induced diabetic rats.

This study investigated the role of sorbitol, a metabolic product of glucose, in the pathogenesis of rat diabetic cystopathy. Three-month-old male Wistar rats were divided into four groups: 1) normal controls; 2) rats rendered diabetic by streptozotocin; 3) rats fed with glucose; and 4) rats injected with sorbitol. The M(2) muscarinic receptor (M(2)-mAChR) protein and mRNA densities of the bladder tissue were measured by Western immunoblot and Northern blot, respectively. The streptozotocin-induced diabetic rats were then treated with ONO-2235, an aldose reductase inhibitor. The bladder M(2)-mAChR protein and mRNA were compared between the treated and untreated diabetic rats. The densities of M(2)-mAChR protein and mRNA in the bladder tissue were significantly increased in diabetic rats, and rats given either glucose or sorbitol (increases in receptor protein: 27.3 +/- 3.3, 19.8 +/- 2.3, and 18.0 +/- 2.1%; increases in mRNA: 39.6 +/- 3.7, 33.1 +/- 2.9, and 20.2 +/- 2.2%, respectively). When diabetic rats were treated with ONO-2235, the increases in bladder M(2)-mAChR protein and mRNA were significantly alleviated. The findings suggest that sorbitol plays a role in the pathogenesis of diabetic cystopathy in rats rendered diabetic by streptozotocin. Aldose reductase inhibitors may be useful in the treatment and prevention of diabetic cystopathy.

Aldehyde Reductase↗
PubMed2006

Proteome analysis of sorbitol fermentation specific protein in Vibrio cholerae by 2-DE and MS.

Vibrio cholerae can be differentiated into epidemic and non-epidemic strains by sorbitol fermentation speed, but little research has been done on its mechanisms. In this study, we investigated differential protein expression of the two strains in response to sorbitol metabolism. V. cholerae strains were cultured in media with and without sorbitol, respectively. Proteins were separated by 2-DE, and those that showed different expression in the two media were identified by MALDI-TOF MS. Fifteen proteins in epidemic strains and 11 proteins in non-epidemic strains showed a different expression in sorbitol medium. Among them, 4 proteins were common to epidemic and non-epidemic strains. Gene sequence analysis showed that some mutations occurred in these proteins between the two strains. Potential functions of these proteins included sugar uptake, amino acid uptake, electron transport, sulfate and thiosulfate transport.

Amino Acid Sequence↗