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At least 865 records · Page 48Linked to original sources
PubMed1986

The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle.

Thin ventricular trabeculae from rat hearts were skinned with the non-ionic detergent Triton X-100. The isometric force development of these muscles was investigated over a range of Ca2+ concentrations (0.2-200 microM) in the presence of various concentrations of creatine phosphate (CP), creatine and inorganic phosphate (Pi). The addition of Pi (1-30 microM) at constant ionic strength reduced the maximum Ca2+-regulated force (obtained at 200 microM-Ca2+). At 20 mM-Pi force was 31 +/- 5% (mean +/- S.E. of mean, n = 7) of that in Pi-free solution. This inhibitory action of Pi was not due to an inhibition of creatine kinase activity or to a reduction in the amount of free energy available for work from ATP hydrolysis. Increases in Pi concentration over the range 0-20 mM shifted the sigmoid relationship between force and [Ca2+] to higher Ca2+ concentrations. The [Ca2+] required for 50% activation rose from 8.3 +/- 1.5 microM (mean +/- S.E. of mean, n = 7) in Pi-free solutions to 19.8 +/- 4.2 microM in 20 mM-Pi. An increase in CP concentration in the range 10-30 mM had a small inhibitory effect on maximum Ca2+-regulated force but did not alter the force--[Ca2+] relationship. Creatine (0-30 mM) was without effect on the skinned muscles. The inhibitory effects of Pi suggest that a net hydrolysis of CP to Pi and creatine in the myoplasm of intact cardiac cells could reduce force development at a given myoplasmic [Ca2+], especially if the latter was below the level needed to fully activate the myofibrils. This suggestion is discussed in relation to the CP hydrolysis and decrease in force development that are observed in cardiac muscle during hypoxia or ischaemia.

Animals↗
PubMed1995

Effects of creatine phosphate and inorganic phosphate on the sarcoplasmic reticulum of saponin-treated rat heart.

1. Ventricular trabeculae from rat heart were permeabilized by treatment with saponin. In the presence of 150 nM Ca2+, application of 20 mM caffeine released Ca2+ from the sarcoplasmic reticulum (SR), resulting in a transient contracture. Ca2+ released from the SR was detected using fura-2 fluorescence. The amplitudes of the caffeine-induced Ca2+ transients were used to assess SR Ca2+ content. 2. In the absence of creatine phosphate (CP), introduction of 5-30 mM inorganic phosphate (Pi) caused a net release of Ca2+ from the SR. Subsequent caffeine-induced Ca2+ and tension transients were smaller in the presence of Pi. Under these conditions, 30 mM Pi decreased the caffeine-induced Ca2+ transients by 45 +/- 3.1% (mean +/- S.D., n = 14). On removal of Pi, the [Ca2+] transiently decreased and the caffeine-induced Ca2+ transients returned to control levels over 4-6 min. 3. In the presence of CP (5-15 mM), the Ca2+ transients were unaffected by the introduction of Pi (5-30 mM) or slightly increased in amplitude. Pi (30 mM) significantly increased the caffeine-induced Ca2+ transients by 7 +/- 8.8% (mean +/- S.D., n = 19, P < 0.05) in the presence of 15 mM CP. The release of Ca2+ on addition of Pi and decrease in [Ca2+] on Pi withdrawal was less pronounced or absent completely in the presence of CP. The inhibitory effects of Pi on caffeine-induced Ca2+ release became apparent as the [CP] was decreased from 5 to 0 mM. 4. In the presence of the creatine phosphokinase inhibitor dinitro-fluorobenzene (DNFB) the effects of Pi (in the presence of CP) were qualitatively similar to the results obtained in the absence of CP, although the decrease in caffeine-induced Ca2+ release was less pronounced. 5. These results suggest that the rise in [Pi]i during ischaemia or anoxia will have little effect on the regulation of Ca2+ by the SR while the [CP]i remains above 5 mM. However, as the [CP] decreases below 5 mM, the accumulation of Pi within the cytosol will progressively reduce the SR Ca2+ content. CP may act in conjunction with endogenous creatine phosphokinase to modify the response of the SR to Pi, and possible mechanisms are considered.

Adenosine Triphosphate↗
PubMed1967

Sodium-potassium adenosine triphosphatase: acyl phosphate "intermediate" shown to be L-glutamyl-gamma-phosphate.

Peptides obtained from pepsin digestion of the phosphorylated and nonphosphorylated forms of a preparation of brain microsomal sodium-potassium-activated adenosine triphosphatase were treated at pH 5.4 with N-(n-propyl-2,3-(3)H) hydroxylamine of high specific activity, then separated by column chromatography, and further digested with pronase. A compound isolated in higher amounts from the phosphorylated enzyme than from the nonphosphorylated enzyme migrated with authentic L-glutamyl-gamma-propylhydroxamate in four chromatographic systems and on electrophoresis on paper at three different pH's. The acyl phosphate "intermediate" in the phosphorylated form of the adenosine-triphosphatase therefore appears to be an L-glutamyl-gamma-phosphate residue.

Adenosine Triphosphatases↗
PubMed2005

Intracellular butyryl phosphate and acetyl phosphate concentrations in Clostridium acetobutylicum and their implications for solvent formation.

It has been suggested (L. H. Harris, R. P. Desai, N. E. Welker, and E. T. Papoutsakis, Biotechnol. Bioeng. 67:1-11, 2000) that butyryl phosphate (BuP) is a regulator of solventogenesis in Clostridium acetobutylicum. Here, we determined BuP and acetyl phosphate (AcP) levels in fermentations of C. acetobutylicum wild type (WT), degenerate strain M5, a butyrate kinase (buk) mutant, and a phosphotransacetylase (pta) mutant. A sensitive method was developed to measure BuP and AcP in the same sample. Compared to the WT, the buk mutant had higher levels of BuP and AcP; the BuP levels were high during the early exponential phase, and there was a peak corresponding to solvent production. Consistent with this, solvent formation was initiated significantly earlier and was much stronger in the buk mutant than in all other strains. For all strains, initiation of butanol formation corresponded to a BuP peak concentration that was more than 60 to 70 pmol/g (dry weight), and higher and sustained levels corresponded to higher butanol formation fluxes. The BuP levels never exceeded 40 to 50 pmol/g (dry weight) in strain M5, which produces no solvents. The BuP profiles were bimodal, and there was a second peak midway through solventogenesis that corresponded to carboxylic acid reutilization. AcP showed a delayed single peak during late solventogenesis corresponding to acetate reutilization. As expected, in the pta mutant the AcP levels were very low, yet this strain exhibited strong butanol production. These data suggest that BuP is a regulatory molecule that may act as a phosphodonor of transcriptional factors. DNA array-based transcriptional analysis of the buk and M5 mutants demonstrated that high BuP levels corresponded to downregulation of flagellar genes and upregulation of solvent formation and stress genes.

Bacterial Proteins↗
PubMed1986

Kinetics of phosphate uptake, growth, and accumulation of cyclic diphosphoglycerate in a phosphate-limited continuous culture of Methanobacterium thermoautotrophicum.

The archaebacterium Methanobacterium thermoautotrophicum was grown in continuous culture at 65 degrees C in a phosphate-limited medium at specific growth rates from 0.06 to 0.28 h-1 (maximum growth rate [mu max] = 0.36 h-1). Cyclic-2,3-diphosphoglycerate (cyclic DPG) levels ranged from 2 to 20 mM in Pi-limited cells, compared with about 30 mM in batch-grown cells. The Monod constant for Pi-limited growth was 5 nM. Pi uptake rates were determined by following the disappearance of 32Pi from the medium. Interrupting the H2 supply stopped the uptake of Pi and the release of organic phosphates. Little or no efflux of Pi occurred in the presence or absence of H2. Pi uptake of cells adapted to nanomolar Pi concentrations could be accounted for by the operation of one uptake system with an apparent Km of about 25 nM and a Vmax of 58 nmol of Pi per min per g (dry weight). Uptake curves at 30 microM Pi or above were biphasic due to a sevenfold decrease in Vmax after an initial phase of rapid movement of Pi into the cell. Under these conditions the growth rate slowed to zero and the cyclic DPG pool expanded before growth resumed. Thus, three properties of M. thermoautotrophicum make it well adapted to live in a low-P environment: the presence of a low-Km, high-Vmax uptake system for Pi; the ability to accumulate cyclic DPG rapidly; and a growth strategy in which accumulation of Pi and cyclic DPG takes precedence over a shift-up in growth rate when excess Pi becomes available.

2,3-Diphosphoglycerate↗
PubMed1998

Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases.

3-Deoxy-D-manno-octulosonate 8-phosphate (KDOP) synthase and 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase catalyze similar phosphoenolpyruvate-utilizing reactions. The genome of Neisseria gonorrhoeae contains one gene encoding KDOP synthase and one gene encoding DAHP synthase. Of the two nonhomologous DAHP synthase families known, the N. gonorrhoeae protein belongs to the family I assemblage. KDOP synthase exhibited an ability to replace arabinose-5-P with either erythrose-4-P or ribose-5-P as alternative substrates. The results of periodate oxidation studies suggested that the product formed by KDOP synthase with erythrose-4-P as the substrate was 3-deoxy-D-ribo-heptulosonate 7-P, an isomer of DAHP. As expected, this product was not utilized as a substrate by dehydroquinate synthase. The significance of the ability of KDOP synthase to substitute erythrose-4-P for arabinose-5-P is (i) recognition of the possibility that the KDOP synthase might otherwise be mistaken for a species of DAHP synthase and (ii) the possibility that the broad-specificity type of KDOP synthase might be a relatively vulnerable target for antimicrobial agents which mimic the normal substrates. An analysis of sequences in the database indicates that the family I group of DAHP synthase has a previously unrecognized membership which includes the KDOP synthases. The KDOP synthases fall into a subfamily grouping which includes a small group of DAHP synthases. Thus, family I DAHP synthases separate into two subfamilies, one of which includes the KDOP synthases. The two subfamilies appear to have diverged prior to the acquisition of allosteric-control mechanisms for DAHP synthases. These allosteric control specificities are highly diverse and correlate with the presence of N-terminal extensions which lack homology with one another.

3-Deoxy-7-Phosphoheptulonate Synthase↗
PubMed2000

Dual transcriptional regulation of the Escherichia coli phosphate-starvation-inducible psiE gene of the phosphate regulon by PhoB and the cyclic AMP (cAMP)-cAMP receptor protein complex.

We have shown that the Escherichia coli phosphate-starvation-inducible psiE gene is regulated by both phosphate and the carbon source by using both lacZ and chloramphenicol acetyltransferase gene (cat) fusions. Yet, under all conditions tested, a single transcriptional start site lying 7 bp downstream of a predicted -10 region was revealed by primer extension analysis. DNase I footprinting showed that the PhoB transcriptional-activator protein protects two predicted pho boxes lying upstream of and near the -35 promoter region. Similar analysis showed that the cyclic AMP (cAMP)-cAMP receptor protein (cAMP-CRP) complex binds a region that overlaps with the downstream pho box. These results, together with measurements of the in vivo psiE promoter activity under various conditions, show that expression of the psiE gene is under direct positive and negative control by PhoB and cAMP-CRP, respectively.

Bacterial Proteins↗
PubMed2002

Pyridoxal 5-phosphate inhibition of substrate selectivity mutants of UhpT, the sugar 6-phosphate carrier of Escherichia coli.

In the sugar phosphate transporter UhpT, gain-of-function derivatives that prefer phosphoenolpyruvate (PEP) as substrate have an uncompensated lysine residue on transmembrane segment 11. We show here that these variants are also highly susceptible to substrate-protectable inhibition by covalent modification of lysine with pyridoxal 5-phosphate. The chemical requirements of this interaction provide evidence that the gain-of-function phenotype results from the pairing of the uncompensated lysines in these mutants with the anionic carboxyl group of PEP.

Escherichia coli Proteins↗
PubMed1978

Phosphate metabolism in blue-green bacteria. V. Factors affecting phosphate uptake in Plectonema boryanum.

Plectonema boryanum requires approximately 5 days of exposure to a culture medium lacking phosphorus to induce the "polyphosphate overplus" phenomenon. At pH9, phosphate uptake is greatest both from normal culture medium and from dilute salt solutions. Phosphate uptake from dilute salt solutions was greatest when Na+ or K+ are combined with Ca2+ or Ca2+ and Mg2+. Cells starved of phosphorus in the presence of a high concentration of K+ or Ca2+ in the medium, and then allowed to take up phosphorus under the same conditions, assimilate more phosphorus than with other major ions.

Cyanobacteria↗
PubMed2006

Effects of external phosphate concentration on glucose-6-phosphate dehydrogenase gene expression in the arbuscular mycorrhizal fungus Glomus intraradices.

Specific primers were developed to amplify a 227 bp segment of the arbuscular mycorrhizal fungus Glomus intraradices gene encoding glucose-6-phosphate dehydrogenase (G6PDH), an enzyme involved in the pentose phosphate pathway. G6PDH gene expression was measured by real-time quantitative reverse transcriptase-polymerase chain reaction in response to phosphorus (P) concentrations in the growth medium of colonized transformed carrot roots. We investigated the effects of different P concentration treatments on carbon (C) metabolism within the intraradical mycelia of G. intraradices. The results showed a significant (P=0.017) down-regulation of G6PDH expression in the intraradical mycelia of G. intraradices cultures grown in high P than low P conditions but no significant difference in regulation in excessive P concentrations when compared with the low P or high P concentrations. These results indicate that a reduction in the C flow from the host could be occurring as a result of elevated P and that a decrease in fungal G6PDH gene expression occurs, but not in the short term (less than 2 h). Reduced C flow from the host could lead to reduced fungal growth and root colonization, as was observed under high soil P conditions.

Amino Acid Sequence↗
PubMed2002

Phosphate determination during hypokinesia and ambulation in establishing phosphate changes in trained and untrained subjects.

Hypokinesia (diminished movement) induces phosphate (P) changes; however, it is not known if P change is greater in trained than untrained subjects. Measuring P balance and P retention during hypokinesia (HK) and P load, we studied if changes in P retention and P depletion were significantly (p<0.05) greater in trained than untrained subjects. Studies were done during a 30-d pre-HK period and a 364-d HK period. Forty male trained and untrained healthy individuals aged 24.5+/-5.4 yr were chosen as subjects. All volunteers were equally divided into four groups: trained ambulatory control subjects (TACS), trained hypokinetic subjects (THKS), untrained ambulatory control subjects (UACS), and untrained hypokinetic subjects (UHKS). All THKS and UHKS were limited to an average walking distance of 0.3 km/d, and TACS and UACS were on an average running distance of 9.8 and 1.8 km/d, respectively. Subjects took daily 12.7-mmol dicalcium-phosphate/kg body weight in the form of supplementation. Negative P balance, fecal P loss, urinary P and calcium (Ca) excretion, serum P, and total Ca (Cat) levels increased significantly (p<0.05), whereas P retention, serum 1,25-dihydroxyvitamin D [1,25 (OH)2D3] and intact parathyroid hormone (iPTH) level decreased significantly (p<0.05) in THKS and UHKS when compared with their pre-HK values and their respective ambulatory controls (TACS and UACS). However, P retention, P balance, serum, urinary, and fecal P, and serum hormone level changed significantly (p<0.05) more in THKS than UHKS. Retention of P, fecal P, urinary P and Ca loss, serum P and Cat level, P balance, 1,25(OH)2D3, and iPTH level change insignificantly (p>0.05) in TACS and UACS when compared with their pre-HK control values. It was concluded that significant negative P balance may indicate P depletion, whereas significant P loss in spite of negative P balance and P load may suggest P retention incapacity; however, P depletion was greater in THKS than UHKS. Clearly, P is wasted much more in THKS than UHKS.

Adult↗
PubMed1978

[Neurotoxicity of acrylamide in rats. I. Subacute intoxication. Absence of effect on incorporation of plasma phosphates into the acid-soluble phosphates of the sciatic nerve and the gastrocnemius muscle, in anatomic continuity and after neural section].

The subcutaneous injection of acrylamide (30 mg kg-1 day-1) in adult male rats induces a severe impairment of the general state of health and a progressive polyneuropathy at the cumulative dose of 180 mg/kg. At the cumulative dose of 400 mg acrylamide does not interfere with the incorporation of plasma inorganic phosphate into the inorganic and organic acid-soluble phosphate fractions of either the gastrocnemius muscle or the sciatic nerve Schwann cells. Nor does it modify the characteristic metabolic response of these fractions to Wallerian degeneration and neurogenic muscle atrophy.

Acrylamides↗
PubMed1999

Regulation of UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase by retinoic acid in P19 cells.

UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase (GPT) is the first enzyme in the dolichol pathway of protein N-glycosylation, and is implicated in the developmental programmes of a variety of eukaryotes. In the present study we describe the effects of all-trans-retinoic acid (RA) on the levels of GPT protein and enzymic activity, and on the transcription rate of the GPT gene, in mouse P19 teratocarcinoma cells. RA caused a dose-dependent and protein-synthesis-dependent induction of enzyme activity. The maximum induction of GPT activity (about 3-fold) required 2 days of exposure to 1 microM RA. Induced GPT activity also resulted in an increase in the rate of incorporation of [3H]mannose into Glc3Man9GlcNAc2. Enzymic activities paralleled GPT gene expression. The GPT gene was induced (2-fold) after 7 h of RA treatment. An approx. 3-fold increase in a 48 kDa GPT protein and approx. 4-fold increases in the levels of three GPT transcripts (1.8, 2.0 and 2.2 kb) were observed after 2 days of RA treatment. The enhanced levels of GPT protein and mRNAs began to decline 3 days after the initiation of differentiation, and GPT expression was down-regulated during cellular differentiation. GPT activity decreased about 2. 8-fold to a constant level in differentiated P19 cells. The results indicate that the RA-induced enzyme activity was mainly determined by increased transcription of the GPT gene. RA-treated P19 cells were about 4-fold more resistant to tunicamycin, a fungal antibiotic which inhibits GPT, than were control cells. In addition, GPT activity in membranes from RA-treated P19 cells exhibited approx. 4-fold increased resistance to tunicamycin compared with activity in membranes from untreated control cells, demonstrating that resistance to tunicamycin is correlated with induced GPT activity. Furthermore, increased GPT activity had regulatory significance with regard to the rate of incorporation of [3H]mannose into Glc3Man9GlcNAc2-P-P-dolichol and into glycoproteins. Together, the data provide additional insights into the hormonal regulation of GPT and present evidence that the RA-mediated induction of GPT has a regulatory impact on the dolichol pathway.

Animals↗
PubMed1976

[Study of the interaction of Na+ and K+-ATPase of erythrocytes with ouabain. Effect of acetyl phosphate and p-nitrophenyl phosphate].

Effects of ATP, acetyl phosphate (AcP) and p-nitrophenyl phosphate (p-NPP) on the inhibition of the Na+, K+-ATPase activity were studied. ATP, AcP and p-NPP were found to facilitate the ouabain-induced inhibition of the enzyme activity only after the injection of these phosphorylyzing agents into the erythrocyte ghosts. Inside the ghosts Na+ ions enhanced the effects of the phosphorylyzing agents. K+ ions in the environment removed the stimulating effects of ATP, AcP and p-NPP on the ouabain-induced inhibition of Na+, K+-ATPase activity. It is concluded that the sites of AcP and p-NPP hydrolysis as well as the active center for ATP are localized on the inner surface of the cell membrane.

Adenosine Triphosphatases↗
PubMedDate not supplied

[Calcium phosphates in otologic surgery. III. The role of fibrin glue in the integration of calcium phosphate implants. Experimental study].

Obliteration of the mastoid cavity has been realized with calcium phosphates associated to heterologous fibrin glue in otologic surgery. 22 artificially created epitympanic and 65 femoral defects in 22 rabbits were closed by means of dense or porous granulates of hydroxyapatite with homologous fibrin glue. Follow-up was for three weeks to 6 months. Osteo-integration of the implants was significantly delayed in the first weeks, comparing the integration of the same phosphates without fibrin glue.

Animals↗
PubMed2004

Phosphate deposition during and after hypokinesia in phosphate supplemented and unsupplemented rats.

The objective of this study was to show that prolonged restriction of motor activity (hypokinesia) could reduce phosphate (P) deposition and contribute to P loss with tissue P depletion. To this end, measurements were made of tissue P content, P absorption, plasma P levels, urinary and fecal P excretion of rats during and after hypokinesia (HK) and daily phosphate supplementation. Studies were conducted on male Wistar rats during a pre-hypokinetic period, a hypokinetic period and a post-hypokinetic period. All rats were equally divided into four groups: unsupplemented vivarium control rats (UVCR), unsupplemented hypokinetic rats (UHKR), supplemented vivarium control rats (SVCR) and supplemented hypokinetic rats (SHKR). Bone and muscle P content, plasma intact parathyroid hormone (iPTH) levels, P absorption, plasma P levels and urinary and fecal P excretion did not change in SVCR and UVCR compared with their pre-HK values. During HK, plasma P levels, urinary and fecal P excretion increased significantly (p<0.05) while muscle and bone P content, P absorption and plasma iPTH levels decreased significantly (p<0.05) in SHKR and UHKR compared with their pre-HK values and the values in their respective vivarium controls (SVCR and UVCR). During the initial 9-days of post-HK, plasma, urinary and fecal P levels decreased significantly (p<0.05), and plasma iPTH levels, muscle and bone P levels remained significantly (p<0.05) depressed in hypokinetic rats compared with their pre-HK values and the values in their respective vivarium control rats. By the 15th day, these values approached the control values. During HK and post-HK, changes in P absorption, plasma iPTH levels, and P levels in muscle, bone, plasma, urine and feces were significantly (p<0.05) greater in SHKR than in UHKR. Decreased tissue P content with increased P loss in animals receiving and not receiving P supplementation demonstrates decreased P deposition during HK. Higher P excretion with lower tissue content in SHKR and UHKR demonstrates that P deposition is decreased more with P supplementation than without. Because SHKR with a lower tissue P content showed higher P excretion than UHKR it was concluded that the risk of decreased P deposition with greater tissue P depletion is inversely related to P intake, that is, the higher the P intake the greater the risk for decreased P deposition and the greater tissue P depletion. It was shown that P (regardless of the intensity of its tissue depletion) is lost during HK unless factors contributing to the decreased P deposition are partially or totally reversed. It was concluded that dissociation between (decreased) tissue P content and (increased) P uptake indicates decreased P (absorption and) deposition as the main mechanisms of tissue P depletion during prolonged HK.

Animals↗
PubMed1990

Sequence of a cDNA that specifies the uridine diphosphate N-acetyl-D-glucosamine:dolichol phosphate N-acetylglucosamine-1-phosphate transferase from Chinese hamster ovary cells.

We have isolated a portion of the uridine diphosphate N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-glucosamine-1-phosphate transferase gene (GTR2) from the genome of a tunicamycin-resistant clonal Chinese hamster ovary cell line, 3E11. The genomic fragment was selected by its hybridization to the yeast ALG-7 gene at low stringency. A 2.46-kilobase cDNA was isolated from a library prepared from 3E11 mRNA and probed with GTR2. The cDNA contained an open reading frame that encodes a protein of 408 amino acids with a molecular mass of 44.9 kDa. This protein was 43% identical in amino acid sequence to the protein of 448 amino acids encoded by the ALG-7 gene. The GTR2 gene fragment contained sequences for four exons coding for the carboxyl-terminal half of the protein. Transferase DNA sequences in 3E11 cells were 12-fold elevated over wild-type cells and 25-fold elevated when 3E11 cells were grown in the presence of tunicamycin. Transferase RNA levels in 3E11 cells were also elevated over wild-type levels but appeared unchanged by the presence of tunicamycin in the medium.

Amino Acid Sequence↗