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At least 19 recordsLinked to original sources
PubMed1976

Direct transfer of the phosphoryl moiety of mannitol 1-phosphate to [14C]mannitol catalyzed by the enzyme II complexes of the phosphoenolpyruvate: mannitol phosphotransferase systems in Spirochaeta aurantia and Salmonella typhimurium.

Spirochaeta aurantia possesses a phosphoenolpyruvate:mannitol phosphotransferase system which catalyzes the transmembrane transport and phosphorylation of mannitol. In vitro studies showed that both phosphoenolpyruvate and mannitol 1-phosphate could serve as phosphate donors. The phosphoenolpyruvate-dependent reaction required two soluble proteins, Enzyme SI and HPr, and an integral membrane complex, Enzyme SII. Only Enzyme SII was required for the mannitol 1-phosphate-dependent reaction. Enzyme II-dependent transphosphorylation of sugars was also demonstrated in eubacterial extracts. The results lead to the suggestion that the Enzyme II complexes of bacterial phosphotransferase systems possess nonoverlapping binding sites for sugar and sugar phosphate.

Edetic Acid↗
PubMed1992

Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system.

Streptococcus mutans, the causative agent of dental caries, utilizes carbohydrates by means of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The PTS facilitates vectorial translocation of metabolizable carbohydrates to form the corresponding sugar-phosphates, which are subsequently converted to glycolytic intermediates. The PTS consists of both sugar-specific and sugar-independent components. Complementation of an Escherichia coli mtlD mutation with a streptococcal recombinant DNA library allowed isolation of the mannitol-1-phosphate dehydrogenase gene (mtlD) and the adjacent sugar-specific mannitol factor III gene (mtlF) from S. mutans. Subsequent transposon mutagenesis of the complementing DNA fragment with Tn5seq1 defined the region that encodes the mtlD-complementing activity, the streptococcal mtlD gene. Nucleotide sequence analysis of this region revealed two complete open reading frames (ORFs) from within the streptococcal mannitol PTS operon. One ORF encodes the mtlD gene product, a 43.0-kDa protein which exhibits similarity to the E. coli and Enterococcus faecalis mannitol-1-phosphate dehydrogenases. The second ORF encodes a 15.8-kDa protein which exhibits similarity to mannitol factor III proteins from several bacterial species. In vitro transcription-translation assays were used to produce proteins of the sizes predicted by the streptococcal ORFs. These data indicate that the S. mutans mannitol PTS utilizes an enzyme II-factor III complex similar to the mannitol system found in other gram-positive organisms, as opposed to that of E. coli, which utilizes an independent enzyme II system.

Amino Acid Sequence↗
PubMed1977

D-Mannitol dehydrogenase from Absidia glauca. Steady-state kinetic properties and the inhibitory role of mannitol 1-phosphate.

Steady-state kinetic studies including initial velocity for mannitol oxidation and fructose reduction and product inhibition for mannitol oxidation using fructose and reduced nicotinamide adenine dinucleotide (NADH) are in accord with a reaction mechanism best described as ordered Bi-Bi with NAD+ and NADH designated as the first substrate, last product, respectively at pH 8.8. All replots of slopes and intercepts from product inhibition studies were linear. Dead-end inhibition studies using mannitol 1-phosphate gave slope-parabolic, intercept-linear noncompetitive inhibition for both NAD+ and mannitol as substrates. The dead-end inhibitor is capable of binding multiply to the E, EA, and EQ forms of the enzyme to an extent that is controlled by the concentration of substrates. The EQ complex is inferred to undergo a conformational change, E'Q equilibrium EQ, since (V1/E1) greater than (KiqV2)/(KqE1), and no evidence for dead-end complex formation with NADH can be adduced. This is interpreted to mean that the release of fructose from the central complex is faster than the isomerization of the E-NADH complex. When mannitol is saturating, the noncompetitive inhibition against NAD+, as the variable substrate, becomes parabolic uncompetitive. A replot of the slopes of the parabola against mannitol 1-phosphate remains concave upward. This situation could arise if the conformational change we infer in the EQ complex opens up additional sites on the protein which can interact with the dead-end inhibitor.

Fungi↗
PubMed1976

Mannitol production in fungi during glucose catabolism.

The levels of phosphofructokinase (EC 2.7.1.11) and mannitol-1-phosphate dehydrogenase (EC 1.1.1.17) have been determined in a number of Mucor and Penicillium species. Mannitol-1-phosphate dehydrogenase was found in only one species of mucor, Mucor rouxii, and this with a specific activity much lower than that found in Penicillium species. All of the fungi tested in the Ascomycetes class exhibited mannitol-1-phosphate dehydrogenase activity. Interference from both mannitol-1-phosphate dehydrogenase and NADH oxidase (EC 1.6.99.5) caused some difficulty initially in detecting phosphofructokinase in Penicillium species; the Penicillium phosphofructokinase is very unstable. Penicillium notatum accumulates mannitol intracellularly; detection of mannitol-1-phosphate dehydrogenase and mannitol-1-phosphatase (EC 3.1.3.22) activity in cell-free extracts indicates that the mannitol is formed from glucose via fructose-6-phosphate and mannitol-1-phosphate; no direct reduction of fructose to mannitol could be detected. The mannitol-1-phosphate dehydrogenase was specific for mannitol-1-phosphate and fructose-6-phosphate; NADP+(H) could not replace NAD+(H). The phosphatase (EC3.1.3.22) exhibited a distinct preference for mannitol-1-phosphate as substrate; all other substrates tested exhibited less than 25% of the activity observed with mannitol-1-phosphate.

Alcohol Oxidoreductases↗
PubMed1976

Effect of mannitol on phosphate transport in intact and acutely thyroparathyroidectomized rats.

Clearance experiments were performed in male Sprague-Dawley rats to determine the effect of mannitol on phosphate (Pi) transport. Solutions of 10 per cent mannitol or normal saline were infused at progressively increasing flow rates with or without parathyroid extract (PTE) infusion into the following animals: Group I: Intact Rats-Mannitol Infusion: A--Intact, hypocalcemic; B--Intact, normocalcemic, normomagnesemic; Group II: TPTX Rats: A--Mannitol infusion; B--Mannitol + PTE infusion; C--Hydropenia + PTE infusion; and D--Saline + PTE infusion. In contrast to previous reports, mannitol increased Pi excretion in intact rats. When Ca + Mg were maintained constant in intact rats or after TPTX, mannitol failed to increase Pi excretion. In TPTX rats receiving mannitol + PTE, increased Pi excretion was again noted. Comparison of Pi excretion during PTE infusion during hydropenia and volume expansion with mannitol or saline in TPTX rats revealed significantly higher Pi excretion with volume expansion. Pi excretion paralleled Na excretion in intact mannitol-loaded and PTE-infused TPTX animals undergoing a mannitol or saline diuresis. Pi and Na excretions, however, were dissociated in mannitol-loaded TPTX rats, intact animals receiving simultaneous Ca and Mg infusion, and TPTX hydropenic animals receiving PTE. These studies indicate that (1) mannitol increases Pi excretion in intact rat, (2) the phosphaturia is PTH-mediated, (3) Pi and Na excretions can be dissociated, and (4) volume expansion with either mannitol or saline enhances the effect of PTH on Pi transport in the renal tubule.

Animals↗
PubMed1977

Mannitol oxidation in two Micromonospora isolates and in representative species of other actinomycetes.

Mannitol kinase and mannitol-1-phosphate dehydrogenase activities were detected in two Micromonospora isolates. The presence of these enzyme activities indicates that mannitol is catabolized first to mannitol-1-phosphate and then to fructose-6-phosphate. Mannitol-oxidizing enzymes were also surveyed in representative species of four other genera of actinomycetes. Mannitol-1-phosphate dehydrogenase was detected in cell-free extracts of Streptomyces lactamdurans. In contrast, cell-free extracts of Mycobacterium smegmatis, Nocardia erythrophila, Streptomyces lavendulae, and Actinoplanes missouriensis contained mannitol dehydrogenase activity but no detectable mannitol-1-phosphate dehydrogenase activity. The mannitol dehydrogenase activities in the latter species support the operation of a pathway for catabolism of mannitol that involves the oxidation of mannitol to fructose, followed by phosphorylation to fructose-6-phosphate.

Actinomycetales↗
PubMed1979

Mannitol and maintenance hemodialysis.

The extensive use of mannitol during maintenance hemodialysis prompted a study of mannitol kinetics. In 17 patients receiving empirical mannitol therapy of mannitol kinetics. In 17 patients receiving empirical mannitol therapy, residual levels range from 19 to 100 mg% In vitro mannitol clearance exceeds 125 ml/min for the CDAK 5 and PF 1.6 dialyzers, while in vivo clearance ranges from 98 to 140 ml/min in the Triex 1, PF 1.6 and CDAK 5. Despite an apparently adequate clearance rate, mannitol administered during dialysis is incompletely removed. Repeated use of mannitol during dialysis leads to mannitol accumulation. Clinical significance of the residual mannitol levels needs further evaluation.

Humans↗
PubMed1978

Mannitol and fructose catabolic pathways of Pseudomonas aeruginosa carbohydrate-negative mutants and pleiotropic effects of certain enzyme deficiencies.

Mutant strains of Pseudomonas aeruginosa PAO were isolated on the basis of their inability to utilize mannitol as sole carbon source for growth. Four linkage groups (I through IV) among these mutant strains were resolved by two-factor crosses using the general transducing phage F116, and the strains appeared to contain point mutations as evidenced by ability to give rise to spontaneous revertants with wild phenotype on mannitol minimal agar. Group I strains were affected only in ability to grow on mannitol; all were deficient in inducible mannitol dehydrogenase activity, and all but one were deficient in inducible mannitol transport activity. Fructokinase was induced in group I strains and in wild-type bacteria during growth in the presence of mannitol but not fructose, indicating the presence of a pathway specific for endogenously generated fructose. Cells grown on fructose contained phosphoenolpyruvate:fructose-1-phosphotransferase activity, and mannitol-grown cells contained a lower level of this activity. Group II mutants were deficient in constitutive phosphoglucoisomerase, failed to grow on mannitol, grew very slowly on glycerol and fructose, but grew normally on glucose and gluconate. Group III strains were deficient in both nicotinamide adenine dinucleotide- and nicotinamide adenine dinucleotide phosphate-linked glucose-6-phosphate dehydrogenase activities that reside in a single enzyme species. 6-Phosphogluconate appeared to be the inductive effector for this enzyme, which was not required for aerobic growth on glucose or gluconate. A single mannitol-negative mutant in group IV also failed to grow on glycerol and glucose, but no biochemical lesion was identified.

Enzyme Induction↗
PubMed1979

Discrepancies in the extracellular space of sympathetic ganglia measured using different isotopes of mannitol and sucrose.

The extracellular space of rat superior cervical ganglia in vitro was measured using mannitol and sucrose labelled with tritium and carbon-14. The volumes of distribution of the 3H-labelled derivatives, especially [3H]mannitol, exceeded those of the 14C-derivatives. The divergence increased with increasing lengths of incubation. Thus, after 30 min incubation, 'spaces' (ml . g-1) were: [14Cu]mannitol, 0.407; [3H]mannitol 0.447; [14C]mannitol, 0.458; [3H]mannitol, 0.645; [14C]sucrose, 0.430; [3H]sucrose, 0.497. Using thin layer chromatography, it was shown that an average of 22% of the label in ganglia incubated for 120 min with [3H]mannitol, but only 4% with [14C]mannitol, was not associated with the parent compound. Both [3H]- and [14C]sucrose appeared to be metabolized by 11%. It is concluded that mannitol and sucrose can be metabolized in isolated ganglia and that this may lead to substantial errors in estimating the extracellular space, particularly when [3H]markers are used.

Animals↗
PubMed1977

Influence of mannitol on contractile responses of isolated perfused arteries.

The influence of hyperosmotic mannitol on vascular smooth muscle contractile responses was examined in isolated arterial preparations. Vasoconstrictor effects of norepinephrine (NE) and potassium chloride (K+) in the perfused central artery of the rabbit's ear and in perfused mesenteric arteries of cats were significantly inhibited by infusion with Krebs bicarbonate solution made hyperosmotic with mannitol (50-200 mosM increase). Similarly, the magnitude and duration of vasoconstrictor responses to transmural stimulation of the central ear artery of the rabbit were decreased by hyperosmotic mannitol (50 mosM). Mannitol (50 mosM) produced a decrease in perfusion pressure when perfusion pressure was maintained at an increased level by K+ (60 mM). Mannitol-induced vasodilatation was not affected by ethacrynic acid (1.5 X 10(-5) M), beta adrenergic blockade or by the development of tachyphylaxis to the vasodilator effects of nitroglycerin. The concentration of cyclic adenosine-monophosphate was not changed by mannitol. Isotonic mannitol also inhibited NE-induced contractile responses. These data indicate that hyperosmotic mannitol produces vasodilatation in isolated arterial smooth muscle by a mechanism(s) that appears dissimilar from that of several other vasodilator substances and suggest that hypertonicity may not be the only factor involved in the vasodilator effect of mannitol.

Animals↗
PubMed1975

The influence of hypertonic mannitol on regional myocardial blood flow during acute and chronic myocardial ischemia in anesthetized and awake intact dogs.

The influence of hypertonic mannitol on regional myocardial blood flow and ventricular performance was studied during acute myocardial ischemia in awake, unsedated and in anesthesized dogs and after myocardial infarction in awake unsedated dogs. Regional myocardial blood flow was measured with radioactive microspheres. Generalized increases in regional myocardial blood flow occurred after mannitol in all of the different animal models studied. The increases in coronary blood flow after mannitol were just as impressive in the nonischemic regions as in the ischemic portion of the left ventricle in all of the different models that were examined in this study. Improvement in regional myocardial blood flow to the ischemic area of the left ventricle after mannitol was associated with a reduction in ST segment elevation during acute myocardial ischemia in anesthetized dogs. The increases in regional myocardial flow after mannitol were also associated with increases in contractility, but the increases in flow appeared to be more impressive than the changes in contractility. The data obtained demonstrate that mannitol increases regional coronary blood flow to both ischemic and nonischemic myocardium in both anesthetized and awake, unsedated, intact dogs with acute and chronic myocardial ischemia and that mannitol reduces ST segment elevation during acute myocardial ischemia in anesthetized dogs. Thus the results suggest that under these circumstances the increases in regional myocardial blood flow after mannitol are of physiological importance in reducing the extent of myocardial injury. Since coronary blood flow increased to nonischemic regions the increases in regional myocardial flow demonstrated in this study after mannitol cannot be entirely explained by the mechanism of reduction in ischemic cell swelling.

Acute Disease↗
PubMed1992

Retraction brain ischaemia: mannitol plus nimodipine preserves both cerebral blood flow and evoked potentials during normoventilation and hyperventilation.

In our miniature swine model simulating operating room brain retraction, we investigated the effects of mannitol plus nimodipine on cerebral blood flow (CBF) and evoked potentials (EP) ipsilateral and contralateral to retraction, in comparison with either agent alone, during both normoventilation and hyperventilation. We here report results in 27 animals with intravenous mannitol (2 g kg-1 over 15 min) and/or nimodipine (1 microgram kg-1 min-1 constant infusion). Mannitol plus nimodipine was superior both to controls and to either mannitol alone or nimodipine alone in preserving EP amplitude ipsilateral to retraction during both normoventilation and hyperventilation. Mannitol alone was effective in normoventilation at preserving EP, while nimodipine alone was effective in hyperventilation. No significant asymmetries in CBF or EP were seen with mannitol plus nimodipine in either normoventilation or hyperventilation. By five minutes postretraction CBF had returned to preretraction values for all groups, and EP amplitude had returned also except for hyperventilated controls. In this model of brain retraction, mannitol plus nimodipine is superior to either agent alone in maintaining both CBF and EP when normoventilation and hyperventilation are employed. The results are discussed in terms of the possible mechanisms for the different and complementary effects of mannitol and nimodipine.

Animals↗
PubMedDate not supplied

Effects of hypertonic mannitol on contractile responses and 45Ca movements in isolated canine arteries.

The effects of hyperosmotic mannitol on vascular smooth muscle contractile responses and on 45Ca movements were examined in different isolated canine arteries. Prior exposure to 50 mM mannitol decreased contractile responses elicited with dopamine (DA) in helical strips of canine terminal mesenteric arteries (Tm) and decreased the contractile response elicited with potassium (K+) in both isolated left anterior descending (LAD) and circumflex coronary arteries. Tension responses induced by norepinephrine or DA in the Tm and K+ and prostaglandin F2 alpha in LAD were relaxed by subsequent exposure to mannitol. Mannitol increased the uptake of 45Ca in Tm arteries. Exposure of the Tm and branches of the LAD to mannitol during the washout of 45Ca resulted in a decrease in the rate of loss of 45Ca; the presence of either K+, Mg2+, or ethylenediamine tetraacetic acid during the washout did not prevent the observed mannitol-induced decrease in 45Ca efflux. These effects of mannitol on 45Ca efflux without a concomitant major change in net 45Ca uptake could be attributed to an increase in bound Ca2+ at relevant membrane sites or stores. Thus, hypertonic mannitol may alter contractile responsiveness of selected canine arteries by impeding the release of bound and/or sequestered Ca2+ and, in this manner, decreasing the Ca2+ concentration at the contractile elements.

Animals↗
PubMed1992

A comparison between two hypotonic irrigating solutions used in transurethral resections of the prostate: sorbitol (2%)-mannitol (1%) and 1.5% glycine solutions.

Two hypotonic but non-haemolysing irrigating solutions, sorbitol-mannitol (2% + 1%) and glycine (1.5%), were compared in 40 TURP cases using a continuous resection technique. Ethanol (1%) was added to the irrigating fluid as a marker to make possible early detection of fluid absorption by breath analysis. Mannitol and sorbitol were determined in plasma and urine; glycine and ethanol were determined in plasma. Apparent absorbed fluid volumes were calculated from the immediate postoperative plasma concentrations of ethanol, mannitol, sorbitol and glycine and from the elimination of mannitol in urine during 24 hours following the operation. The use of a continuous operating technique with a suprapubic trocar resulted in very small absorptions (less than 1 l) in this series. The concentrations of the two solutes in the sorbitol-mannitol irrigating fluid were balanced so that the plasma concentrations immediately postoperatively were of the same order when absorption occurred. The sorbitol concentration declined more rapidly than the mannitol concentration in conformity with previous findings. In most cases the peak plasma level was observed immediately postoperatively but in some cases at a later time (during the interval 0-2 hours), indicating absorption from a depot of fluid accumulated extravesically in addition to direct intravenous absorption. The best estimate of fluid absorption seems to be obtained from the urinary elimination of mannitol, followed by estimates based on the plasma mannitol concentration immediately postoperatively. The plasma ethanol level determined at the same time gave an estimate of the same order, whereas plasma sorbitol and glycine levels gave lower estimates (owing to rapid redistribution and metabolism).(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗
PubMed1979

The growth response of cells in medium made hyperosmolal with electrolytes or mannitol.

A comparison of the growth rates of established human lymphoid and tumor cell lines was performed in nutrient medium made hyperosmolal with mannitol, NaCl, or mixtures of NaCl and KCl at a constant Na/K ratio. It was found that considerably higher osmolalities were attained with mannitol than electrolytes before a reduction in the growth rate of the culture was observed. This suggests that mannitol and electrolytes affected the growth rate through different mechanisms. Mannitol uptake was studied with two of the cell lines and both cell lines were found to be permeable to mannitol. This eventually would have eliminated the osmolality gradient between the interior of the cell and the medium, and could explain why higher osmolalities were obtained with mannitol before the growth rate was effected. In addition, initial experiments showed that these cell lines may also be able to metabolize mannitol.

Carcinoma, Transitional Cell↗
PubMed1976

Effect of hypertonic mannitol and intraaortic counterpulsation on regional myocardial blood flow and ventricular performance in dogs during myocardial ischemia.

Studies were performed to determine if intervention with hypertonic mannitol and intraaortic balloon counterpulsation increases regional myocardial blood flow during acute myocardial ischemia. Anesthetized dogs on right heart bypass were studied. Heart rate was kept constant by atrial pacing. Myocardial ischemia was provided by ligating the proximal left anterior descending coronary artery for 12 minute periods. Infusion of hypertonic mannitol begun immediately after ligation increased coronary blood flow to the ischemic area by 36 +/- 9.0% (standard error) (P less than 0.01) and to the nonischemic left ventricle by 21 +/- 8.8% (P less than 0.05) as compared with flow in the same regions during the control coronary ligation. Intraaortic balloon counterpulsation begun immediately after ligation increased regional coronary flow to the ischemic region by 20 +/- 8.4% (P less than 0.05) but did not significantly alter flow to the nonischemic left ventricle as compared with levels during the control ligation. Combined intraaortic counterpulsation and hypertonic mannitol increased coronary flow to the ischemic region by 46 +/- 13% (P less than 0.02) and to the nonischemic left ventricle by 59 +/- 22% (P less than 0.05) as compared with flow during occlusion of the left anterior descending artery with mannitol alone. The data demonstrate that both hypertonic mannitol and intraaortic counterpulsation increase left ventricular ischemic regional flow and that combined hypertonic mannitol and intraaortic balloon counterpulsation provide a greater increase in regional coronary blood flow to both the ischemic and nonischemic regions of the left ventricle than mannitol alone.

Acute Disease↗
PubMed1977

Influence of mannitol on maintaining coronary flows and salvaging myocardium during ventriculotomy and during prolonged coronary artery ligation.

We investigated whether prolonged infusion of hypertonic mannitol results in a sustained increase in coronary flow and reduces myocardial necrosis after ventriculotomy or two hours of circumflex coronary artery occlusion. Cardiac outputs, intracardiac pressures, and heart rates did not differ between mannitol and control animals. Those receiving mannitol after ventriculotomy had coronary flows to myocardium near the incision which did not differ from controls. During coronary occlusion, mannitol did increase flow to ischemic and peri-ischemic regions by one hour, but this increase was not sustained at two hours. On histologic examination, myocardial necrosis involving the right ventricular free wall in the ventriculotomy animals and the posterior papillary muscle and subadjacent free wall in the coronary occlusion animals, did not differ between the mannitol treated and control groups. The data obtained in the present study, combined with those from earlier evaluations of the influence of mannitol during ventriculotomy and myocardial ischemia, suggest that mannitol's ability to increase coronary flow to injured areas of myocardium is relatively short-lived.

Animals↗