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PubMed1994

Comparison of adjuvant activities of aluminium phosphate, calcium phosphate and stearyl tyrosine for tetanus toxoid.

The adjuvant activity of three adjuvants, aluminium phosphate (AIPO4), calcium phosphate (CaHPO4) and stearyl tyrosine for tetanus toxoid (TT) were compared to soluble TT in mice at a dose of 0.5 Lf (1/10th of the single human dose) and in guinea-pigs at a dose of 7.5 Lf (1.5 times the single human dose). Three TT preparations varying in purity were used: (1) ammonium sulphate precipitated formalin detoxified tetanus toxin (AS-TT); (2) AS-TT ultrafiltered to remove low molecular weight peptides (UF-TT): and (3) chromatographically purified tetanus toxin subsequently detoxified with formalin (CP-TT). After primary immunization of mice, AIPO4 absorbed TTs induced higher toxin-neutralizing and IgG (by ELISA) antibodies than CaHPO4, stearyl tyrosine adsorbed or soluble TT preparations, but this difference was no longer present after secondary immunization. TT preparations of varying purities showed similar antibody responses after primary and secondary immunizations when adsorbed on each adjuvant. CP-TT preparation showed the highest neutralizing antibody level amongst soluble preparations after the first dose. All the preparations induced mainly IgG1 antibodies. However, stearyl tyrosine adsorbed TT induced relatively higher IgG2a and IgG2b responses than AIPO4, CaHPO4 adsorbed or soluble TTs particularly after booster injection. No preparation induced detectable IgG3 or IgM antibodies. AIPO4 adsorbed preparations induced higher IgE antibodies than CaHPO4 and stearyl tyrosine adsorbed vaccines. Among the soluble preparations, CP-TT induced lower anti-TT IgE antibodies than standard AS-TT. All these preparations were also tested in the US potency test for adsorbed TT in guinea-pigs. While all the preparations passed this test, AIPO4 adsorbed TT preparations induced higher neutralizing and IgG antibodies than CaHPO4 and stearyl tyrosine adsorbed or soluble TT preparations. In these animal models, purified TT was a strong immunogen and traditional AIPO4 adjuvant gave the highest antibody responses.

Adjuvants, Immunologic↗
PubMed1993

Role of intracellular phosphate in the regulation of renal phosphate transport during development.

Direct correlations have been observed between the renal intracellular concentration of phosphate ([Pi]i) and postnatal age (3-13 weeks in rats, 1-4 weeks in guinea pigs), as well as between the dietary supply of Pi and [Pi]i. In turn, [Pi]i was found to be inversely correlated with the renal tubular transport of phosphate (TRPi). However, age- and diet-related differences in [Pi]i alone do not explain the high capacity of Na(+)-Pi cotransport present in the kidney of the neonate. Therefore, we explored whether changes in TRPi induced by altering Pi demand (whole body growth or bone mineralization) are mediated by factors other than changes in [Pi]i. TRPi was measured in vivo and nuclear magnetic resonance-visible [Pi]i in perfused kidneys of 8-week-old genetically growth hormone (GH)-deficient and GH-treated dwarf rats and in 8-week-old thyroparathyroidectomized (TPTX) Sprague-Dawley (SD) rats treated or untreated with etidronate (EHDP), an inhibitor of bone mineralization. In dwarf rats, [Pi]i was 1.2 +/- 0.2 mM and TRPi 2.4 +/- 0.2 mumol/ml glomerular filtrate. In TPTX SD rats, [Pi]i was 1.6 +/- 0.2 mM and TRPi 4.2 +/- 0.3 mumol/ml glomerular filtrate. Administration of GH to dwarf rats resulted in increases in Pi transport of 38% +/- 8% (P < 0.05), while administration of EHDP to TPTX SD rats decreased TRPi by 52% +/- 7% (P < 0.05). Neither GH nor EHDP significantly affected [Pi]i. Thus, in the rat changes in TRPi due to alterations in Pi demand occur in the absence of significant changes in [Pi]i.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2006

K/DOQI guideline requirements for calcium, phosphate, calcium phosphate product, and parathyroid hormone control in dialysis patients: can we achieve them?

BACKGROUND: Mineral metabolism has emerged as an important predictor of morbidity and mortality in dialysis patients. Kidney Disease Outcomes Quality Initiative (K/DOQI) clinical practice guidelines for bone metabolism and disease in chronic kidney disease (CKD) recommend that, in Stage 5 CKD, the target levels for calcium (Ca) (corrected for serum albumin), phosphate (P), calcium x phosphate (CaxP) product and parathyroid hormone (PTH) levels should be maintained at 8.4-9.5 mg/dl, 3.5-5.5 mg/dl, <55 mg2/dl2 and 150-300 pg/ml, respectively. OBJECTIVES: To evaluate our ability to achieve K/DOQI guidelines for bone metabolism and disease targets in our patients and to compare them between patients on hemodialysis (HD) and peritoneal dialysis (PD) and also with those reported in the literature. METHODS: We reviewed bone metabolism laboratory parameters in 57 HD patients and 69 PD patients, who had been on dialysis for more than 9 months. RESULTS: The percentage of patients whose serum Ca, P, CaxP product and PTH were within K/DOQI recommended target ranges were 46%, 53%, 77% and 28% in HD patients and 52%, 65%, 77% and 23% in PD patients, respectively. There were no significant differences between HD and PD patients in the percentage of all parameters that were within K/DOQI recommended target ranges. The percentage of our HD patients who had Ca, P, and PTH levels within recommended target range was similar to those in previous reports. CONCLUSION: In our unit, the management of bone and mineral metabolism in HD and PD patients is still far short of meeting K/DOQI guidelines. These findings appear similar in HD and PD patients. Our findings resemble those reported in the literature.

Calcium↗
PubMed1996

Phosphate deprivation induces overexpression of two proteins related to the rat renal phosphate cotransporter NaPi-2.

Polyclonal antibodies were raised in rabbits against the C-terminal portion of the rat renal brush-border membrane sodium/phosphate cotransporter NaPi-2. Antibody specificity and molecular sizes of proteins related to NaPi-2 were assayed by Western blot analysis. Proteins of 40 and 70-75 kDa (p40 and p70) were immunodetected in rat and mouse brush-border membranes and proteins of 72 and 82 kDa were detected in rabbit. The absence or presence of beta-EtSH in the samples before electrophoresis greatly influenced the immunodetection profile of the rat proteins. Since the 40 kDa protein (p40) can only be detected under reducing conditions, it probably originates from reduction of disulfide bonds in p70. Tryptic cleavage of p40 and p70 revealed identical protein fragments showing the close structural identity of those proteins. Both proteins were more abundant in the outer cortex portion of the rat kidney than in the juxtamedullary portion. Furthermore, rats fed a low-phosphate diet for 24 h showed a 20- and 14-fold increase in the amount of p40 and p70, respectively, compared to control rats, showing that the adaptation to P(i) deprivation by increasing renal phosphate reabsorption is not only the result of overproduction of p70, as previously shown, but is also due to the novel p40 which most probably derives from p70.

Amino Acid Sequence↗
PubMed1993

Glyceraldehyde-3-phosphate activates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase.

Nitric oxide was recently demonstrated to stimulate ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Our studies on the effect of glyceraldehyde-3-phosphate (GA3P), the natural substrate of dehydrogenase activity of GAPDH, indicated GA3P to be another very potent activator of ADP-ribosylation of the enzyme. GA3P was able to activate ADP-ribosylation only in the presence of DTT. The action of GA3P was associated with inhibition of GAPDH dehydrogenase activity. Ka for GA3P was at least 50-fold lower and maximal activation was somewhat higher than these values for other aldehydes that were also able to enhance GAPDH ADP-ribosylation in the presence of DTT. ADP-ribosylation was blocked by carboxamidomethylation of the essential cysteine SH-group. The bond between the prelabeled protein and ADP-ribose was resistant to hydrolysis with hydroxylamine and HgCl2, suggesting that a lysine epsilon-amino group is the target for ADP-ribosylation.

Adenosine Diphosphate Ribose↗
PubMed1991

The inhibition of rat liver threonine dehydratase by carbamoyl-phosphate. The formation of carbamoylpyridoxal 5'-phosphate.

The effects exerted by carbamoyl phosphate (CP) and cyanate (KCNO) on rat liver L-threonine deaminase have been studied. The two compounds showed that same effects, inhibiting through a competitive mechanism both the holoenzyme and the dialyzed enzyme; inhibition was more evident for the latter. Ki values, both for L-threonine and pyridoxal 5'-phosphate (PLP), were lower for the apoenzyme and the inhibitors also affected the Km of the apoenzyme for PLP. The effects of CP and KCNO are mainly due to an interference in the association reaction apoenzyme + PLP in equilibrium holoenzyme This was clearly demonstrated by the fact that, when PLP was incubated with CP or KCNO, it failed to enhance the activity of the holoenzyme nor did it reactivate the resolved apoenzyme. Such interference of CP and KCNO in the L-threonine deaminase activity was mainly due to a specific mechanism, the formation of a new derivative of PLP. The reaction of PLP with either CP or KCNO occurred readily, at low concentrations, under physiological conditions. The new compound was identified as 3,4-dihydro-2H-pyrido[3,4-e]1,3-oxazin-2-one derivative by ultraviolet-visible spectra, elemental analysis, infrared, NMR and MS spectra. In this paper we formulate the hypothesis that this compound is involved in the regulation of the CP and PLP intracellular content and in the control of PLP dependent enzymes.

Animals↗
PubMed1989

Kinetic studies on improved phosphate dental cement: the measurement of some improved dental cements containing phosphate polymers by an electric conductance method.

The rate of the setting process of zinc phosphate dental cement with organic phosphate polymers as additives was measured by a conductance technique. There are two rate-determining parameters, namely an induction period and a first-order reaction constant. The values of the latter constant are not affected by the additives.

Chemical Phenomena↗
PubMed1989

Nucleotide sequence of pho-4+, encoding a phosphate-repressible phosphate permease of Neurospora crassa.

The nucleotide (nt) sequence of the Neurospora crassa pho-4+ gene, which encodes a phosphate-repressible phosphate permease, has been determined. The gene specifies a protein of 590 amino acids (aa) and contains two introns. Two RNA transcripts of 3.3 and 2.4 kb have been identified, and transcription start points (tsp) and termination sites and/or processing sites have been located. The 3.3-kb message is initiated about 890 nt upstream from the tsp for the 2.4-kb transcript. A hydropathy profile of the aa sequence suggests ten to twelve membrane-spanning helices with a large hydrophilic domain between the eighth and ninth helices. This model for the predicted secondary structure of the protein is very similar to models proposed for other sequenced integral membrane proteins from both prokaryotes and eukaryotes. Since very few permease-encoding genes of eukaryotes have been examined in molecular detail, it will be of interest to compare the sequence of pho-4+ with those encoding other anion transport proteins, as they become available.

Amino Acid Sequence↗
PubMed1997

Desensitization to glucose 6-phosphate of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal 5'-phosphate.

Incubation of the nonphosphorylated form of maize-leaf phospho enol pyruvate carboxylase (orthophosphate: oxaloacetate carboxy-lyase (phosphorylating), PEPC, EC 4.1.1.31) with the reagent pyridoxal 5'-phosphate (PLP) resulted in time-dependent, reversible inactivation and desensitization to the activator glucose 6-phosphate (Glc6P) and other related phosphorylated compounds. Both processes are not connected, since (i) when the PLP-modification was carried out in the presence of saturating ligands of the active site, which prevents inactivation, the desensitization to Glc6P is still observed, and (ii) under some experimental conditions the desensitization reaction is 4-times faster than the inactivation. Desensitization to Glc6P is first order with respect to PLP and has a second-order forward rate constant of 4.7 +/- 0.3 s-1 M-1 and a first-order reverse rate constant of 0.0046 +/- 0.0002 s-1. Correlation studies between the remaining Glc6P sensitivity and mol of PLP residues incorporated per mol of enzyme subunit indicate that one lysyl group for enzyme monomer is involved in the sensitivity of the enzyme to Glc6P. The reactivity of this group is increased by polyethylene glycol and glycerol, while the reactivity of the lysyl group of the active site is not affected by these organic cosolutes. In the presence but not in the absence of the organic cosolutes, Glc6P by itself offers significant protection against desensitization, while increases the extent of inactivation. Free PEP or PEP-Mg have opposite effects, protecting the enzyme against inactivation and increasing the degree of desensitization. They also increases the protection against desensitization afforded by Glc6P. Finally, the PEPC inhibitor malate provides some protection against both inactivation and desensitization. Taken together, these results are consistent with PLP-modification of a highly reactive lysyl group at or near the allosteric Glc6P-site.

Allosteric Site↗
PubMed1997

Identification of critical amino acid residues of Saccharomyces cerevisiae carbamoyl-phosphate synthetase: definition of the ATP site involved in carboxy-phosphate formation.

Carbamoyl-phosphate synthetases (CPSases) utilize two molecules of ATP at two homologous domains, B and C, with ATP(B) used to form the enzyme-bound intermediate carboxy-phosphate and ATP(C) used to phosphorylate the carbamate intermediate. To further define the role of one CPSase peptide suggested by affinity labeling studies to be near the ATP(B) site, we have carried out site-directed mutagenic analysis of peptide 234-242 of the Saccharomyces cerevisiae arginine-specific CPSase. Mutants E234A, E234D, E236A, E236D and E238A were unable to complement the CPSase-deficient yeast strain LPL26 whereas mutants Y237A, E238D, R241K, R241E and R241P supported LPL26 growth as well as wild-type CPSase. Kinetic analysis of E234A and Y237A indicated impaired utilization of ATP(B) but not of ATP(C). D242A, a temperature-sensitive mutant, retained no detectable activity when assayed in vitro. These findings, together with the affinity labeling data and primary sequence analysis, strongly suggest that the yeast CPSase peptide 234-242 is located at the ATP(B) site and that some of its residues are important for functioning of the enzyme. D242 appears to occupy a critical structural position and E234, E236 and E238 appear to be critical for function, with the spatial arrangement of the carboxyl side chain also critical for E234 and E236.

Adenosine Triphosphate↗
PubMed2002

Crocidolite asbestos inhibits pentose phosphate oxidative pathway and glucose 6-phosphate dehydrogenase activity in human lung epithelial cells.

The cytotoxicity of asbestos has been related to its ability to increase the production of reactive oxygen species (ROS), via the iron-catalyzed reduction of oxygen and/or the activation of NADPH oxidase. The pentose phosphate pathway (PPP) is generally activated by the cell exposure to oxidant molecules. Contrary to our expectations, asbestos (crocidolite) fibers caused a dose- and time-dependent inhibition of PPP and decreased its activation by an oxidative stress in human lung epithelial cells A549. In parallel, the intracellular activity of the PPP rate-limiting enzyme, glucose 6-phosphate dehydrogenase (G6PD), was significantly diminished by crocidolite exposure. This inhibition was selective, as the activity of other PPP and glycolysis enzymes was not modified, and was not attributable to a decreased expression of G6PD. On the opposite, the incubation with glass fibers MMVF10 did not modify PPP and G6PD activity. PPP and G6PD inhibition did not correlate with the increased nitric oxide (NO) production elicited by crocidolite in A549 cells. Experiments with the purified enzyme suggest that crocidolite inhibits G6PD by directly interacting with the protein. We propose here a new mechanism of asbestos-evoked oxidative stress, wherein fibers increase the intracellular ROS levels also by inhibiting the main antioxidant pathway of the cell.

Asbestos, Crocidolite↗
PubMed2003

Hydrophobic derivatives of 2-amino-2-deoxy-D-glucitol-6-phosphate: a new type of D-glucosamine-6-phosphate synthase inhibitors with antifungal action.

Several N-acyl and ester derivatives of 2-amino-2-deoxy-D-glucitol-6-phosphate (ADGP) have been synthesised and tested as inhibitors of fungal enzymes involved in early steps of chitin biosynthesis and for antifungal activity. All the tested derivatives were found to be much poorer inhibitors of the enzyme, D-glucosamine-6-phosphate (GlcN-6-P) synthase, than the parent compound but some of them exhibited much better antifungal activity. MIC values for the investigated compounds ranged between 10 mg mL(-1), found for ADGP and 0.3 mg mL(-1) for the most active derivative, namely ADGP dimethyl ester. Increased affinity of ADGP derivatives to the artificial immobilised cell membrane was correlated with their enhanced ability to be taken up by fungal cells by free diffusion. It was found that some of the examined derivatives behaved as 'pro-drugs' and after internalisation were converted into ADGP in the cell-free extract. This conversion was relatively rapid for ADGP esters but very slow for N-acyl derivatives. Results of our studies demonstrate a possibility of design and preparation of GlcN-6-P synthase inhibitors exhibiting antifungal activity.

Acylation↗
PubMed1979

The equilibria of calcium and phosphate ions with the micellar calcium phosphate in cow's milk.

Calorimetric measurements of the heat of solution of micellar Ca phosphate suggest that this material more closely resembles OH-apatite than amorphous Ca phosphate or any other crystalline form. Preliminary computer calculations of the ionic equilibria of milk salt solutions indicate that, over a wide range of pH and temperature, such solutions are supersaturated with respect to OH-apatite and to various other Ca salts under certain conditions.

Animals↗
PubMed2006

A biosensor for inorganic phosphate using a rhodamine-labeled phosphate binding protein.

A novel biosensor for inorganic phosphate (Pi) has been developed based on the phosphate binding protein of Escherichia coli. Two cysteine mutations were introduced and labeled with 6-iodoacetamidotetramethylrhodamine. When physically close to each other and correctly oriented, two rhodamine dyes interact to form a noncovalent dimer. In this state, they have little or no fluorescence, unlike the high fluorescence intensity of monomeric rhodamine. The labeling sites were so placed that the distance and orientation between the rhodamines change as a consequence of the conformational change associated with Pi binding. This movement alters the extent of interaction between the dyes. The best mutant of those tested (A17C, A197C) gives rise on average to approximately 18-fold increase in fluorescence intensity as Pi binds. The kinetics of interaction with Pi were measured at 10 degrees C. Under these conditions, the fluorescence increase associated with Pi binding has a maximum rate of 267 s-1. The Pi dissociation rate is 6.6 s-1, and the dissociation constant is 70 nM. An application of the sensor is demonstrated for measuring ATP hydrolysis in real time as a helicase moves along DNA. Advantages of the new sensor are discussed, both in terms of the use of a rhodamine fluorophore and the potential of this double labeling strategy.

Biosensing Techniques↗
PubMed1997

Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate.

We have measured the kinetics of inorganic phosphate (Pi) release during a single turnover of actomyosin nucleoside triphosphate (NTP) hydrolysis using a double-mixing stopped-flow spectrofluorometer, at very low ionic strength to increase the affinity of myosin-ATP and myosin-ADP-Pi to actin. Myosin subfragment 1 and a series of nucleoside triphosphates were mixed and incubated for approximately 1-10 s to allow NTP to bind to myosin and generate a steady state mixture of myosin-NTP and myosin-NDP-Pi. The steady state intermediates were then mixed with actin. The kinetics of Pi release were measured using a fluorescent probe for Pi, based on a phosphate binding protein [Brune et al. (1994) Biochemistry 33, 8262-8271]. These data are correlated with quenched-flow data, where the extent of the rapid burst of hydrolysis during the first turnover of ATP hydrolysis was followed by chemical quenching of the reaction mix at various times after rapidly mixing ATP and myosin subfragment 1. From the double-mixing actomyosin measurements, the kinetics of Pi release are biphasic. The fast phase corresponds to Pi release from the associated actomyosin-ADP-Pi complex. The slow phase measures the rate of the cleavage step on associated actomyosin. At saturating actin, there is a correlation between the amplitude of the fast phase and the size of the Pi burst observed by quenched flow in the absence of actin: the size of this phase corresponds to the amount of myosin-ADP-Pi formed during the first mix. For ATP at 20 degrees C the rate of the Pi release step is 75 (+/-5) s-1, 25-fold larger than the cleavage step, which is the rate-limiting step of actomyosin ATP hydrolysis at saturating actin. The rate constant of Pi release varies only slightly with nucleoside structure. The rate constant of the slow phase of the Pi release (measuring cleavage) is highly dependent upon the structure of the NTP substrate.

Actomyosin↗
PubMed2005

Flow injection potentiometric system for the simultaneous determination of inositol phosphates and phosphate: phosphorus nutritional evaluation on seeds and grains.

A simple flow injection potentiometric (FIP) system, which uses a tubular cobalt electrode, has been developed for phosphorus nutritional evaluation of seeds and grains. Inorganic phosphorus, P(i), is determined using a 1 x 10(-2) mol.L(-1) potassium phthalate buffer solution adjusted at pH 4. A sensitivity of 47 mV/decade and an operating range from 10 to 1000 mg.L(-1) (1 x 10(-4)-1 x 10(-2) M) of dihydrogen phosphate are obtained. The inositol phosphates amount, which is referred to the organic phosphorus, P(org), is directly determined from extracts using a 1 x 10(-2) mol.L(-1) Tris-HCl buffer solution adjusted at pH 8. A sensitivity of 127 mV/decade and an operating range of 10-1000 mg.L(-1) (2.5 x 10(-4)-5 x 10(-3) M) of P(org) (expressed as inositol hexakisphosphoric acid monocalcium) are achieved. Some samples of seed and grain are analyzed by an ICP-OES and a spectrophotometric method to compare results to the developed flow system; no significant differences at the 95% confidence level are observed using a paired t test. Other samples such as animal nursing feed, soybean meal, and corn are also analyzed with the proposed FIP system, showing a good correlation to the ICP-OES values.

Edible Grain↗
PubMed2006

Simple enzymatic in situ generation of dihydroxyacetone phosphate and its use in a cascade reaction for the production of carbohydrates: increased efficiency by phosphate cycling.

A new enzymatic method for the generation of dihydroxyacetone phosphate (DHAP) using the acid phosphatase from Shigella flexneri (PhoN-Sf) and the cheap phosphate donor pyrophosphate (PPi) is described. The utility of this method was demonstrated in an aldolase-catalyzed condensation carried out in one pot in which DHAP was generated and coupled to propionaldehyde to give a yield of 53% of the isolated dephosphorylated end product.

Aldehydes↗
PubMed2002

The effects of replacing dicalcium phosphate with Busumbu rock phosphate on performance and the mechanical properties of bone in growing chicks.

Three hundred, day-old broiler chicks, with an average initial weight of 41.8 +/- 1.79 g, were used in a 15-day study (10 birds per battery cage) to characterize their performance and fluorine status when dicalcium phosphate (DCP) was replaced by Busumbu rock phosphate (BRP) as the source of phosphorus in the chicks' ration. The treatments comprised a standard ration with BRP replacing 0, 25%, 50%, 75% or 100% of DCP. Replacing DCP with BRP significantly reduced the final weight of the chicks (p < 0.01), feed intake (p < 0.01), weight gains (p < 0.01) and dry matter digestibility (p < 0.05) but increased (p < 0.05) the feed-to-gain ratio. True phosphorus absorption and the percentage of phosphorus in the tibia were not affected by increasing amounts of BRP in the diet. Increasing levels of BRP in the diet linearly reduced (p < 0.01) the percentage bone ash, calcium, Ca:P ratio, ultimate breaking force, bending moment, stress, and modulus of elasticity. Leg stiffness, lameness, reduced feed intake, and a decline in general health were recorded in 10-40% of the chicks on 75% and 100% BRP, respectively. These results suggest that excessive ingestion of fluorine from the BRP caused the reduction in the chicks' performance.

Absorption↗