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PubMed2000

Sorbitol as an arrester of embryonic development in diapausing eggs of the silkworm, Bombyx mori.

Recently, it was confirmed that embryos derived from diapausing eggs of the silkworm, Bombyx mori, begin their development and reach larval maturity on mulberry leaves, when the naked eggs are cultured in vitro. In this study, we found that the method of embryo culture is useful for determining the physiological regulation of diapause. We show that the development of embryos derived from diapausing eggs was strongly inhibited by the addition of either sorbitol or trehalose to the culture medium. Furthermore, this inhibitory effect disappeared when the embryos were cultured in a control medium which did not contain either sorbitol or trehalose, indicating that the inhibitory reactions caused by both substances are reversible. The minimal effective dose of either sorbitol or trehalose was approximately 0.2 M, a value similar to the in vivo concentration of sorbitol in diapausing eggs (0.2 M). Glycerol, mannitol or glucose were moderately effective for inhibition. Sorbitol present in diapausing silkworm eggs does not appear to serve as an antifreeze, but as an strong arresting factor of embryonic development. Furthermore, these results show that a decrease in sorbitol releases the embryos from diapause at the termination of diapause.

Journal Article↗
PubMed2001

Transformation of Japanese persimmon (Diospyros kaki Thunb.) with apple cDNA encoding NADP-dependent sorbitol-6-phosphate dehydrogenase.

Japanese persimmon (Diospyros kaki Thunb. cv Jiro) was transformed with apple (Malus x domestica Borkh.) cDNA encoding NADP-dependent sorbitol-6-phosphate dehydrogenase (S6PDH) by an Agrobacterium-mediated leaf-disc transformation system. Integration and expression of the transgene were confirmed by genomic DNA blot and immunoblot analyses. Sorbitol accumulation in five of six transgenic plants obtained was confirmed by GC-MS. The amount of sorbitol in the leaves of transgenic plants varied from 14.5 to 61.5 µmol g(-1) fr wt(-1). Sorbitol was not found in leaves of non-transformed 'Jiro' or the line PS7 that produced S6PDH protein with no S6PDH activity. Eventually, two transformed lines producing high (PS1) and medium (PS6) amounts of sorbitol, one control transformed line (PS7), and non-transformed 'Jiro' were selected and evaluated for salt-stress tolerance. Under NaCl stress, the activity of photosystem II in leaves was determined in terms of the ratio of the variable (Fv) to the maximum (Fm) fluorescence of chlorophyll. The rate of decline in Fv/Fm under NaCl stress was lower in PS1 than the other three lines, suggesting that PS1 is more tolerant to NaCl stress than the other three lines. The factors that caused enhanced salt stress tolerance in PS1 are discussed in relation to sorbitol biosynthesis and its growth.

Journal Article↗
PubMed1979

Detection and characterization of sorbitol dehydrogenase from apple callus tissue.

Sorbitol dehydrogenase (l-iditol:NAD(+) oxidoreductase, EC 1.1.1.14) has been detected and characterized from apple (Malus domestica cv. Granny Smith) mesocarp tissue cultures. The enzyme oxidized sorbitol, xylitol, l-arabitol, ribitol, and l-threitol in the presence of NAD. NADP could not replace NAD. Mannitol was slightly oxidized (8% of sorbitol). Other polyols that did not serve as substrate were galactitol, myo-inositol, d-arabitol, erythritol, and glycerol. The dehydrogenase oxidized NADH in the presence of d-fructose or l-sorbose. No detectable activity was observed with d-tagatose. NADPH could partially substitute for NADH.Maximum rate of NAD reduction in the presence of sorbitol occurred in tris(hydroxymethyl)aminomethane-HCl buffer (pH 9), or in 2-amino-2-methyl-1,3-propanediol buffer (pH 9.5). Maximum rates of NADH oxidation in the presence of fructose were observed between pH 5.7 and 7.0 with phosphate buffer. Reaction rates increased with increasing temperature up to 60 C. The K(m) for sorbitol and xylitol oxidation were 86 millimolar and 37 millimolar, respectively. The K(m) for fructose reduction was 1.5 molar.Sorbitol oxidation was completely inhibited by heavy metal ions, iodoacetate, p-chloromercuribenzoate, and cysteine. ZnSO(4) (0.25 millimolar) reversed the cysteine inhibition. It is suggested that apple sorbitol dehydrogenase contains sulfhydryl groups and requires a metal ion for full activity.

Journal Article↗
PubMed1981

Purification and Characteristics of Sorbitol-6-phosphate Dehydrogenase from Loquat Leaves.

To study the role of sorbitol-6-phosphate dehydrogenase in sorbitol synthesis in leaves of Rosaceous plants, properties of the enzyme and its presence in several plants in the family was investigated. The activity of the enzyme, which catalyzes an NADP-dependent oxidation of the substrate to glucose-6-phosphate, was detected in leaves of Prunus mume, Prunus persica, Rhaphiolepsis indica, Sorbus aucuparia, Cydonia oblonga, Photinia glabra, Sorbaria kirilowii, and Spiraea thunbergii.The enzyme was purified about 60-fold from leaves of loquat (Eriobotrya japonica) using affinity chromatography with Blue Sepharose. Neither mannitol-1-phosphate nor fructose-6-phosphate served as substrate. Molecular weight of the enzyme was calculated to be 65,000 at pH 8.0 by gel filtration. Since sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed a peptide of 33,000 daltons, the enzyme was assumed to be a dimer at pH 8.0 K(m) values for sorbitol-6-phosphate, glucose-6-phosphate, NADP, and NADPH were 2.22 millimolar, 11.6 millimolar, 13.5 micromolar, and 1.61 micromolar, respectively. Equilibrium constant for sorbitol-6-phosphate oxidation was 5.12 x 10(-10). Optimal pH for sorbitol-6-phosphate oxidation was 9.8. The enzyme showed its maximum activity within a broad pH range between 7 and 9 for glucose-6-phosphate reduction. The enzyme was more effective in the direction of glucose-6-phosphate reduction than in the reverse direction at neutral pH. Thus, it is suggested that the enzyme catalyzes sorbitol synthesis from glucose-6-phosphate during photosynthesis in leaves of Rosaceous plants.

Journal Article↗
PubMed1995

Effect of pH on sheep liver sorbitol dehydrogenase steady-state kinetics.

The variation with pH of the kinetic parameters for sorbitol oxidation and fructose reduction by sheep liver sorbitol dehydrogenase has been studied over the pH 5-10 range. The reaction is compulsory ordered in both directions with the coenzyme as the leading substrate, and the rate-determining step in either direction is the enzyme-coenzyme product dissociation. Throughout the pH range, the lack of a primary kinetic isotope effect on Vm with (2H8) sorbitol confirms that the ternary complexes are not of rate-determining significance under maximum velocity conditions. The association rate constants for NAD and NADH increase and decrease, respectively, towards high pH. NAD binding to the enzyme is dependent upon pK values of 9.2 and 9.6. Whereas the dissociation rate constant for NAD release from the enzyme shows no pronounced variation with pH, NADH release is dependent upon pK values of 7.2 and 7.7. The kinetic constants that characterize the dependence on substrate concentration of the steady-state rate of catalysis vary with pH in accordance with a single pK of 7.1 for sorbitol oxidation and of 7.7 for fructose reduction. These pK values reflect the ionization properties of a catalytically essential group, which is tentatively considered to be either the H2O/OH- ligand binding to the catalytic zinc atom or a histidine residue. Catalysis by sorbitol dehydrogenase, due to the absence of a second ionization contribution, appears not to involve any obligatory step of proton transfer to solution at the ternary complex level. A mechanism for sorbitol dehydrogenase catalysis is proposed.

Animals↗
PubMed1995

Regulation of aldose reductase, sorbitol dehydrogenase, and taurine cotransporter mRNA in rat medulla.

The regulation of mRNA for aldose reductase, sorbitol dehydrogenase, and the Na+/Cl-/taurine cotransporter was studied with three in vivo models in which urinary concentration is reduced: Sprague-Dawley rats undergoing a water diuresis or fed a low-protein diet or Brattleboro rats. In Sprague-Dawley rats, 3 days of water diuresis reduced inner medullary aldose reductase mRNA abundance 6.5-fold compared with untreated rats, whereas sorbitol dehydrogenase and taurine cotransporter mRNA were unchanged. When water diuretic rats were acutely deprived of water, urine osmolality increased significantly after 4 h but aldose reductase mRNA did not increase until 12 h. Heat shock protein-70 mRNA was not increased by water deprivation. Second, in rats fed a low-protein diet for 3 wk, aldose reductase mRNA increased two-fold, whereas sorbitol dehydrogenase and taurine cotransporter mRNA were unchanged. Finally, in Brattleboro rats, urine osmolality and levels of aldose reductase and taurine cotransporter mRNA increased in response to 1 day of water deprivation, whereas sorbitol dehydrogenase mRNA was unchanged. Administering vasopressin (1 U/day) to Brattleboro rats for 8 days also increased urine osmolality and aldose reductase mRNA but did not alter sorbitol dehydrogenase or taurine cotransporter mRNA. This result is consistent with the hypothesis that changes in urine osmolality induce changes in aldose reductase mRNA abundance that are independent of vasopressin. It was concluded that, in rat inner medulla: (1) aldose reductase mRNA abundance varies with changes in water balance or dietary protein, whereas sorbitol dehydrogenase and taurine cotransporter mRNA do not; and (2) heat shock protein-70 mRNA abundance is not increased during acute osmotic stress.

Aldehyde Reductase↗
PubMed2000

Activities of NADPH-dependent reductases and sorbitol dehydrogenase in canine and feline lenses.

OBJECTIVE: To measure activities of NADPH-dependent reductases and sorbitol dehydrogenase in lenses from healthy dogs and cats. SAMPLE POPULATION: Lenses from 37 dogs and 23 cats. All animals were healthy and had serum glucose concentrations within reference limits. PROCEDURE: Lenses were homogenized, and activities of NADPH-dependent reductases and sorbitol dehydrogenase were measured spectrophotometrically. RESULTS: Activities of NADPH-dependent reductases and sorbitol dehydrogenase were significantly lower in lenses from cats than in lenses from dogs. However, the ratio of NADPH-dependent reductases activity-to-sorbitol dehydrogenase activity was significantly higher in lenses from cats than in lenses from dogs. CONCLUSIONS AND CLINICAL RELEVANCE: Results indicate that during periods of hyperglycemia, sorbitol would accumulate at a faster rate in the lenses of cats than in the lenses of dogs. Thus, the higher incidence of diabetic cataracts in dogs, compared with cats, is likely not attributable to a difference in the ratio of NADPH-dependent reductases activity-to-sorbitol dehydrogenase activity.

Aldehyde Reductase↗
PubMed2000

Optimized synthesis of L-sorbose by C(5)-dehydrogenation of D-sorbitol with Gluconobacter oxydans.

The optimization of L-sorbose synthesis by regiospecific dehydrogenation of D-sorbitol using Gluconobacter oxydans is reported. The current L-sorbose production processes that are based on G. oxydans and other bacterial strains are suboptimal as to yield and rate of L-sorbose synthesis. One reason for these problems is the toxicity that is induced by the substrate D-sorbitol when used in concentrations of >10% (w/v). This phenomenon significantly limits the potentials of L-sorbose production from an industrial point of view. The goal of this study was to develop a fast production process that yields L-sorbose in stoichiometric amounts starting from D-sorbitol concentrations that exceed 10% (w/v). A gradual improvement of the inoculum build-up procedure, culture medium composition, and process parameters ultimately led to a theoretically maximal L-sorbose productivity (200 g L(-1) of L-sorbose from 200 g L(-1) of D-sorbitol in 28 h of fermentation) using a Gluconobacter oxydans mutant strain that was selected under conditions of substrate inhibition. Because the D-sorbitol/L‐sorbose bioconversion is used to mass-produce vitamin C, the procedure reported here will contribute to a more efficient and more economic synthesis of vitamin C.

Ascorbic Acid↗
PubMed2004

Gelation behaviors of schizophyllan-sorbitol aqueous solutions.

On addition of D-sorbitol, schizophyllan (SPG) aqueous solution forms a thermoreversible gel upon cooling. The gelation process is characterized by rheology, differential scanning calorimetry (DSC), and optical rotation measurement (ORD). It is found that the Winter-Chambon criterion works well in determining the critical gelation point of the present system, although the criterion has been scarcely applicable to systems that show weak-gel properties even before gelation. Moreover, ORD and DSC results indicate that a disordered to ordered conformational change accompanies the gelation process, which is attributed to the transition from SPG triple helix II to I. The gelation temperature of SPG-sorbitol aqueous solution is almost independent of SPG concentration in the examined concentration range and is slightly decreased by lowering SPG molecular weight, while greatly influenced by sorbitol content. The gelation is considered to be induced by the transition from SPG triple helix II to I, which leads to a three-dimensional network constituted by the extremely entangled and stiff SPG triple helices I. Furthermore, it is proved that neither junction zone nor aggregation of SPG triple helices is involved in the SPG-sorbitol gels. The SPG-sorbitol gel is structurally like a solution that is unable to flow within a timescale of usual observation.

Calorimetry, Differential Scanning↗
PubMed1991

The effect of aluminum ions and sorbitol on collagen and skin: a thermally stimulated current spectroscopy study.

The influence of aluminum ions introduced either directly or with sorbitol, in collagen and skin, has been investigated by Thermally Stimulated Current/TSC spectroscopy. The intramolecular mobility of collagen has been found to be significantly reduced by aluminum ions. The substitution of water molecules by aluminum ions on intramolecular hydrophilic sites is suggested to be responsible for this evolution. The presence of sorbitol minimizes this effect. The intermolecular mobility of collagen is decreased upon introduction of aluminum ions in presence of sorbitol. This result can be explained by the interaction of sorbitol-aluminum entities with the telopeptidic regions of collagen molecules. In skin samples, the intra- and intermolecular mobilities are restored due to the combined actions of sorbitol and noncollagenous proteins and other macromolecules.

Aluminum↗
PubMed1989

Pathways for the synthesis of sorbitol from 13C-labeled hexoses, pentose, and glycerol in renal papillary tissue.

Suspensions of rabbit renal papillary tissue were incubated with D-[6-13C]glucose, D-[1-13C]fructose, D-[1-13C]ribose, and [2-13C]glycerol. The perchloric acid extracts of the above incubations were investigated with 13C NMR spectroscopy. All 13C-labeled substrates give rise to 13C-labeled D-sorbitol. D-[6-13C]Glucose and D-[1-13C]fructose are converted directly into D-sorbitol via the aldose reductase and sorbitol dehydrogenase pathway, respectively, whereas D-[1-13C]ribose and [2-13C]glycerol give rise to labeling of the D-glyceraldehyde pool which on its turn causes a labeling of D-sorbitol. Label exchanges observed from incubations with glycerol and D-ribose indicate that the pentose shunt plays a role in this synthesis of D-sorbitol.

Animals↗
PubMed1998

Effects of two aldose reductase inhibitors upon sorbitol output, D-glucose metabolism and insulin release in islets from normal and hereditarily diabetic rats.

The effects of two aldose reductase inhibitors, ARI 509 (4.0 microM) and tolrestat (40.0 microM), upon sorbitol output, D-[5-3H]glucose and D-[U-14C]glucose metabolism and insulin release were investigated in pancreatic islets prepared from normal rats or hereditarily diabetic animals (Goto-Kakizaki rats) and incubated in the presence of 16.7 mM D-glucose. At this hexose concentration, the output of sorbitol, the utilization of D-[5-3H]glucose, the oxidation of D-[U-14C]glucose and its conversion to 14C-labelled acidic metabolites and amino acids and the secretion of insulin were all much higher than those found in islets exposed to only 2.8 mM D-glucose. In both normal and diabetic rats, the aldose reductase inhibitors suppressed glucose-stimulated sorbitol output, but failed to affect the metabolism of D-[5(-3H]glucose or D-[U-14C]glucose and the secretory response to the hexose. These findings document the efficiency and specificity of ARI 509 and tolrestat as inhibitors of aldose reductase in islet cells, whilst arguing against any major role of sorbitol formation in the stimulus-secretion coupling process for glucose-induced insulin release and any major perturbation of those factors regulating the generation and output of sorbitol in islets of Goto-Kakizaki rats.

Aldehyde Reductase↗
PubMed1994

Stimulation of ileal calcium absorption by sorbitol, L-xylose, or creatine via a decrease in luminal sodium concentration: relation with concomitant changes in enterocyte energy metabolism.

Ligated ileal loops, 30 cm in length, of 4-month-old male Wistar rats were instilled with 3 ml of a 10 mM CaCl2 solution (added with 0.25 muCi 45Ca) in the absence (control) or presence of 100mM sorbitol, L-xylose, or creatine. Ileal calcium (Ca) transport, measured by plasma 45Ca appearance, was found to be similar 30 minutes after fluid instillation in all four instances. However, thereafter, 45Ca appearance in plasma did not increase further in control animals whereas it increased twice as much during the subsequent 30 minutes in the presence of sorbitol, L-xylose, or creatine. However, when loops of similar length were instilled with only 1.0 ml of such solutions, the sorbitol effect was already observed during the first 30 minutes. The stimulation of ileal Ca absorption induced by the presence of sorbitol appeared to be due to a cellular effect, associated with a decreased flux across the paracellular pathway, as indicated by 3H-mannitol absorption. The presence of sorbitol in instilled ileal solution induced a significant decrease in luminal Na, K, bicarbonate, and Cl concentrations at each time point studied (30, 60, 120, or 240 minutes after instillation). Thirty minutes after instillation, no difference in soluble Ca concentration was observed between control and experimental rats. After 60 minutes, Ca concentration was dramatically decreased in control rats but it remained nearly constant in experimental animals. Thus, the presence of substances enhancing ileal Ca transport favored the maintenance of soluble Ca in ileal solution during longer time periods than their absence. In the ileal enterocyte, these substances induced a twofold increase of ATP content compared with controls.(ABSTRACT TRUNCATED AT 250 WORDS)

Absorption↗
PubMed1975

Uptake of sorbitol by chick embryo heart cells at various stages of development.

Sorbitol enters chick embryo heart cells from five days of development on. The rate of sorbitol entry becomes slower as development proceeds and the data suggest this is principally due to an increase in the apparent Km of transport, the Vmax remaining relatively constant. The uptake of sorbitol displays saturation kinetics and is believed on this ground to be carrier-mediated. Sorbitol does not appear to be actively transported since it is not concentrated against a gradient and its uptake is not inhibited by iodoacetate or 2, 4-dinitrophenol. Sorbitol does not appear to be taken up via the glucose transport system since uptake is not stimulated by insulin or inhibited by glucose or phloretin.

Animals↗
PubMed1989

Sorbitol metabolism in retina studied in vitro.

A new method is described which allows study of the retinal sorbitol metabolism in vitro. Bovine retinal tissue was incubated in tissue culture medium for 24 h and after this time showed only small morphological changes. The sorbitol content doubled at a glucose level of 5.5 mM compared with freshly prepared noncultured retina. Increasing glucose concentrations led to a gradual increase of the sorbitol content. Supplementation of the culture medium with fructose likewise enhanced the retinal sorbitol accumulation. An aldose reductase inhibitor (ICI 128436; Statil) significantly decreased the sorbitol content.

Animals↗
PubMedDate not supplied

D-sorbitol plasma disappearance rate: an index to evaluate changes in liver circulation.

The hepatic clearance of D-sorbitol was proven to be a reliable parameter for evaluating the functional liver plasma flow. Twenty-five normal subjects and 50 cirrhotic patients were studied in order to assess if the measure of the plasma disappearance rate of sorbitol can be used as a simpler procedure to evaluate changes in liver perfusion and to predict modifications of drug bioavailability due to circulatory events. The plasma disappearance rate was calculated between 10 and 20 min after intravenous administration of a 2-g dose because in this time interval plasma levels were in the optimum range for the chemical assay, and the plasma concentration/time curve fitted a decreasing exponential function. Plasma disappearance rate values were found to correlate significantly (r = 0.666, p less than 0.001) with sorbitol hepatic clearance, as calculated after the 2-h test. The test had a good day-to-day reproducibility both in normal subjects and cirrhotic patients. In 5 patients submitted to surgical side-to-side portacaval shunt, decreases of plasma disappearance rate and sorbitol hepatic clearance showed no significant difference. Mean values (+/- SD) of D-sorbitol plasma disappearance rate were 0.048 +/- 0.014 min-1 in cirrhotic patients, and 0.081 +/- 0.014 min-1 in normal subjects (p less than 0.001).

Blood Flow Velocity↗
PubMed1997

Sorbitol uptake in plasma membrane vesicles isolated from immortalized rabbit TALH cells: activation by a Ca2+/calmodulin-dependent protein kinase.

Apical plasma membrane vesicles were isolated from cultures of immortalized thick ascending limb of Henle's loop (TALH) cells and sorbitol uptake was investigated using a rapid filtration technique. In the presence of Mg2+, Ca2+, ATP, and GTP sorbitol equilibrated within three minutes with the intravesicular space; this uptake was reduced by 75% when the incubation temperature was decreased from 37 degrees C to 4 degrees C. A lower level of uptake was also observed in the presence of 100 microM quinidine and when Ca2+ or ATP were omitted from the medium. Membranes preincubated with Mg2+, Ca2+, ATP, and GTP showed, however, a high sorbitol uptake in ATP-free medium. Staurosporine, but only at high concentrations of 200 nm, inhibited sorbitol uptake when present during the transport experiments or during the preincubation with ATP. Similar results were obtained with 1 microM trifluoperazine. Protein kinase C inhibitory peptide was ineffective whereas 20 nm KT 5926, at low concentrations a specific inhibitor of Ca2+/calmodulin-dependent kinase, attenuated the activation. On the basis of these data we suggest that a Ca2+/calmodulin-dependent kinase is a mediator of regulation of sorbitol plasma membrane permeability in renal medullary cells.

Animals↗
PubMed2001

Zymomonas mobilis CP4 fed-batch fermentations of glucose-fructose mixtures to ethanol and sorbitol.

Zymomonas mobilis CP4 fed-batch fermentations of glucose-fructose mixtures were carried out at different operational conditions (aeration, feed rate and substrate concentration) to test their effects on the system productivity. In these fermentations, the main products were ethanol and sorbitol. Kinetic parameters were calculated using the experimental data. However, parameters in the sorbitol synthesis rate were estimated from data recorded in different experiments in order to avoid the effect of the simultaneous cell growth and ethanol synthesis. In this case, the crude cell extract was used as source of the enzyme responsible for the sorbitol synthesis. The highest degree of conversion of fructose into sorbitol obtained with the extract was equal to 71% in a sugar mixture with an initial concentration of 200 g/l. Results obtained in the fed-batch fermentations showed that aeration of the culture has a positive effect on the final biomass concentration. However, final ethanol concentration is lower under aerated conditions. The best sugar yields to biomass and ethanol were 0.032 and 0.411 g/g, respectively. On the other hand, the highest sorbitol yield in the fed-batch fermentations was 0.148 g/g.

Biomass↗