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PubMed2005

Ischemic preconditioning protects post-ischemic renal function in anesthetized dogs: role of adenosine and adenine nucleotides.

AIM: To investigate the effects of renal ischemic preconditioning (IPC) on both renal hemodynamics and the renal interstitial concentrations of adenosine and adenine nucleotides induced by ischemia-reperfusion injury. METHODS: Renal hemodynamics responses to ischemia-reperfusion injury in mongrel dog models were determined with or without multiple brief renal ischemic preconditioning treatments, as well as the adenosine A1 receptor antagonist (KW-3902), respectively. The renal interstitial concentrations of adenosine and adenine nucleotides in response to ischemia-reperfusion injury, either following 1-3 cycles of IPC or not, were measured simultaneously using microdialysis sampling technology. RESULTS: One 10-min IPC, adenosine A1 receptor antagonist (KW-3902) also shortened the recovery time of renal blood flow (RBF) and urine flow (UF), as well as mean blood pressure (BP). Advanced renal IPC attenuated the increment of adenosine and adenine nucleotides, as well as recovery time during the 60-min reperfusion which followed the 60-min renal ischemia. All of these recovery times were dependent on the cycles of 10-min IPC. The renal interstitial concentrations of adenosine and adenine nucleotides increased and decreased during renal ischemia and reperfusion, respectively. CONCLUSION: A significant relativity in dog models exists between the cycles of 10-min renal IPC and the recovery time of BP, UF, and RBF during the 60-min renal reperfusion following 60-min renal ischemia, respectively. Renal IPC can protect against ischemia-reperfusion injury and the predominant effect of endogenous adenosine induced by prolonged renal ischemia; renal adenosine A1 receptor activation during the renal ischemia-reperfusion injury is detrimental to renal function.

Adenine↗
PubMed1976

Pharmacological studies with adenine, adenosine and some phosphorylated derivatives on guinea-pig tracheal muscle.

Adenine, adenosine and three adenine nucleotides all caused relaxation of the guinea-pig trachea. The relaxation to the nucleotides was often preceded by a contraction. The response to adenosine and the nucleotides, but not adenine, was potentiated by dipyridamole. Imidazole inhibited the response to adenine alone. Propranolol has no effect on the response to any of the compounds. It is concluded that the guinea-pig trachea does not possess and a nucleotide-specific receptor as has been postulated for some other smooth muscle preparations. An alternative hypothesis postulating an adenosine-specific receptor is presented.

Adenine↗
PubMed1959

Specific action of adenine as a feedback inhibitor of purine biosynthesis.

Purines can prevent the formation of aminoimidazole precursors which are accumulated by bacterial mutants genetically blocked in purine biosynthesis. If the block does not interfere with interconversions among adenine, guanine, hypoxanthine and xanthine, then any of the purines can act as a feedback inhibitor. If conversion of the other purines to adenine is prevented, then adenine becomes a specific requirement for inhibition; this indicates that feedback control operates at a level involving adenine or one of its congeners.

Adenine↗
PubMed1972

Adenine phosphoribosyltransferase in Mycoplasma mycoides and Escherichia coli.

Some kinetic properties of the adenine phosphoribosyltransferases from Escherichia coli and Mycoplasma mycoides have been studied. For the E. coli enzyme, Michaelis constants for adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP) are 1.3 and 10 mum, respectively. Adenosine monophosphate, the most effective nucleotide inhibitor, inhibits competitively with respect to PRPP, the inhibition constant being 26 mum. The M. mycoides enzyme has more complex kinetics. The response to increasing PRPP concentration is sigmoidal, the degree of sigmoidality depending on both the concentration of adenine and the pH. At low PRPP levels, high concentrations of adenine are inhibitory. Guanosine monophosphate is the most effective inhibitor, being inhibitory at all pH values, but other nucleotides have been found to activate at pH 7 and inhibit at pH 8. The elution profile of the M. mycoides enzyme from Sephadex suggests an association of enzyme subunits in the presence of PRPP. This is consistent with the observed kinetics if the associated form has increased stability and activity.

Adenine↗
PubMed2004

A DNA adenine methyltransferase of Escherichia coli that is cell cycle regulated and essential for viability.

DNA sequence analysis revealed that the putative yhdJ DNA methyltransferase gene of Escherichia coli is 55% identical to the Nostoc sp. strain PCC7120 gene encoding DNA methyltransferase AvaIII, which methylates adenine in the recognition sequence, ATGCAT. The yhdJ gene was cloned, and the enzyme was overexpressed and purified. Methylation and restriction analysis showed that the DNA methyltransferase methylates the first adenine in the sequence ATGCAT. This DNA methylation was found to be regulated during the cell cycle, and the DNA adenine methyltransferase was designated M.EcoKCcrM (for "cell cycle-regulated methyltransferase"). The CcrM DNA adenine methyltransferase is required for viability in E. coli, as a strain lacking a functional genomic copy of ccrM can be isolated only in the presence of an additional copy of ccrM supplied in trans. The cells of such a knockout strain stopped growing when expression of the inducible plasmid ccrM gene was shut off. Overexpression of M.EcoKCcrM slowed bacterial growth, and the ATGCAT sites became fully methylated throughout the cell cycle; a high proportion of cells with an anomalous size distribution and DNA content was found in this population. Thus, the temporal control of this methyltransferase may contribute to accurate cell cycle control of cell division and cellular morphology. Homologs of M.EcoKCcrM are present in other bacteria belonging to the gamma subdivision of the class Proteobacteria, suggesting that methylation at ATGCAT sites may have similar functions in other members of this group.

Amino Acid Sequence↗
PubMed1962

Biosynthesis of S-adenosylmethionine by Saccharomyces cerevisiae. I. Adenine and methionine requirments.

Yall, Irving (University of Arizona, Tucson, Ariz.). Biosynthesis of S-adenosylmethionine by Saccharomyces cerevisiae. I. Adenine and methionine requirements. J. Bacteriol. 83:1336-1340. 1962.-Both a parent strain (SC-10) and an adenineless mutant strain (SC-10-80-3-5) of Saccharomyces cerevisiae accumulated S-adenosylmethionine (AM) in the presence of "excess" l-methionine (400 mumoles/100 ml of medium). Relatively small amounts of AM were found when the organisms were grown in the absence of methionine, in the presence of "normal" amounts of l-methionine (3.35 mumoles/100 ml of medium), or in the presence of 400 mumoles of d-methionine. Adenine and hypoxanthine were equally effective in promoting cell growth and AM production in the mutant. S-adenosylmethionine permitted some cell growth. Other purines (guanine and xanthine) and nucleosides such as adenosine and methylthioadenosine did not serve as growth factors. The cell permeability to adenosine was tested by growing the parent strain in the presence of adenosine-8-C(14) and the mutant in adenine and the labeled nucleoside. Both of these experiments were performed in the absence and presence of "excess" l-methionine. Under all conditions, more than 25% of the radioactivity introduced as adenosine-8-C(14) was found in the cells. About 40% of the radioactivity taken up by the mutant cells in the prescene of "excess" l-methionine was fixed in AM. Adenine-8-C(14) was readily taken up by cells of both strains when grown in the absence and presence of "excess" l-methionine. About 17% of the radioactivity taken up by the mutant cells in the presence of "excess" l-methionine was found in the AM fraction.

Adenine↗
PubMed1964

RESPIRATORY PATHWAYS IN THE MYCOPLASMA. II. PATHWAY OF ELECTRON TRANSPORT DURING OXIDATION OF REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE BY MYCOPLASMA HOMINIS.

VanDemark, P. J. (University of South Dakota, Vermillion), and P. F. Smith. Respiratory pathways in the Mycoplasma. II. Pathway of electron transport during oxidation of reduced nicotinamide adenine dinucleotide by Mycoplasma hominis. J. Bacteriol. 88:122-129. 1964.-Unlike the flavin-terminated respiratory pathway of the fermentative Mycoplasma, the respiratory chain of the nonfermentative M. hominis strain 07 appears to be more complex, involving quinones and cytochromes in addition to flavins. In addition to reduction by reduced nicotine adenine dinucleotide (NADH) and reduced nicotine adenine dinucleotide phosphate, nonpyridine nucleotide-linked reduction of the respiratory chain of this organism occurred with succinate, lactate, and short-chained acyl coenzyme A derivatives as electron donors. Enzymes catalyzing the oxidation of NADH included an NADH oxidase, a diaphorase, a quinone reductase, and a cytochrome c reductase. The oxidation of NADH was sensitive to a variety of inhibitors, including 10(-4)m Atabrine, 10(-3)m sodium amytal, 10(-5)mp-chloromercuribenzoate, 10(-4)m antimycin A, and 10(-4)m potassium cyanide. The oxidase was resolved by the addition of 5% trichloroacetic acid and reactivated by the addition of flavin adenine dinucleotide but not flavin mononucleotide. The M. hominis sonic extract contained an NADH-coenzyme Q reductase. The oxidation of NADH was stimulated by the addition of either menadione or vitamin K(2) (C(35)). The oxidase was inactivated by extraction with ether or irradiation at 360 mmu. The ether-inactivated enzyme was partially reactivated by the addition of "lipid" extract of the enzyme and coenzyme Q(6). Difference spectra of the cell extracts revealed the presence of "b" and "a" type cytochromes. These cell extracts were found to contain a cyanide-and azide-sensitive cytochrome oxidase and catalase.

Catalase↗
PubMed2002

Solution structure of a DNA duplex containing a formamide-adenine base pair.

The N-(2-deoxy-beta3-D-erythro-pentofuranosyl) formamide residue results from a ring fragmentation product of thymine or cytosine. The presence of a formamide-adenine base pair in the sequence 5'd(AGGAACCACG).d(CGTGGFTCCT) has been studied by 1H and 31P nuclear magnetic resonance (NMR) and molecular dynamics. There are two possible isomers for the formamide side chain, either cis or trans. For each isomer, we observed an equilibrium in solution between two forms. First, a species where the formamide is intrahelical and paired with the facing adenine. For the cis isomer, the formamide is in a syn conformation and two hydrogen bonds with adenine are formed. The trans isomer is in an anti conformation and a single hydrogen bond is observed. In the second form, whatever the isomer, the formamide is rejected outside the helix, whereas the adenine remains inside.

Adenine↗
PubMed1985

Adenine nucleotide synthesis from inosine during normoxia and after ischaemia in the isolated perfused rat heart.

[14C]inosine in a range of concentrations of 20 microM to 1 mM was administered to the isolated perfused rat heart for 30 min. The incorporation of the nucleoside into myocardial adenine nucleotides increased for extracellular concentrations of the precursor up to 50 microM, reaching a plateau at 60 nmol . g-1 X 30 min-1 with concentrations ranging between 50 and 200 microM. The supply of 500 microM and 1 mM of inosine induced a further increase in cardiac adenine nucleotide synthesis to about 200 nmol . g-1 X 30 min-1. When supplied during low flow ischaemia (0.5 mL . min-1, 30 min.), 1 mM of inosine protected the heart against ATP degradation, while 100 microM of inosine was inefficacious. In the presence of 1 mM of inosine on reperfusion the adenine nucleotide content of the heart was similar to that observed in the absence of the nucleoside. The incorporation of [14C]inosine into adenine nucleotides was, in this last condition, below the value measured before ischaemia. Inosine administration was effective in protecting the heart against ischaemic breakdown of glycogen and favoured postischaemic restoration of glycogen stores.

Adenine Nucleotides↗
PubMed2003

Discrete but simultaneous release of adenine nucleotides and serotonin from mouse megakaryocytes as detected with patch- and carbon-fiber electrodes.

Using patch- and carbon-fiber electrodes, we studied release phenomena of adenine nucleotides and serotonin from megakaryocytes isolated from the bone marrow of the mouse. Megakaryocytes express ionotropic purinergic receptors on their surfaces. Under the condition of whole cell recording, the cells showed spikelike spontaneous inward currents. The spontaneous currents were carried by cations and had amplitudes of 30-800 pA at -43 mV and durations of 0.1-0.3 s. Pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid (PPADS; 100 microM) and suramin (100 microM), purinoceptor-blocking agents, depressed the currents reversibly. It is thought that the receptor involved was the P2X1 subtype on the cell and that the currents were due to activation of the P2X1 receptor by adenine nucleotides released from the cell. The currents showed a skewed amplitude distribution, suggesting variation of vesicular contents and/or distinct localization or varied density of receptors on the cell. Frequency of the spontaneous inward currents was enhanced by external application of platelet-activating substances, thrombin (0.4 U/ml), phorbol ester (100 nM), and ADP (2 microM), at low concentrations. With a carbon-fiber electrode, which can detect oxidizable substances including serotonin, spikelike oxidation currents from the external surface of the megakaryocyte were detected. The frequency of the oxidation currents increased remarkably after the application of thrombin (10 U/ml). The majority of the oxidation currents coincided with the rising phase of the whole cell currents, suggesting corelease of serotonin and adenine nucleotide from the same vesicle. We concluded that megakaryocytes store adenine nucleotides and serotonin in the same vesicle and release them simultaneously in a discrete manner.

Adenine Nucleotides↗
PubMed1991

Adenine nucleotide synthesis in exercising and endurance-trained skeletal muscle.

Strenuous exercise leads to increased efflux of purine nucleoside and base that should necessitate recovery of adenine nucleotides by either the de novo synthesis or salvage pathway. De novo synthesis of adenine nucleotide was measured in quiescent and contracting muscle of sedentary and exercise-trained rats using an isolated perfused hindquarter preparation. Synthesis rates were assessed by measuring the incorporation of [1-14C]glycine into adenine nucleotide in muscles of both resting and stimulated hindlimbs after 1 h of either low- or high-energy demand isometric contractions. In nonstimulated sedentary and trained muscles, rates of de novo synthesis were similar. The effect of muscle contractions on de novo synthesis varied among muscle fiber types. Contracting, nonfatigued fast-twitch muscle sections showed significant declines in de novo synthesis in both sedentary and trained groups. Rates in slow-twitch red fibers and fatigued fast-twitch white fiber sections were not different from rest. Supplementing the perfusate with 5 mM ribose caused de novo synthesis to rise three- to fourfold in each of the fiber sections. However, the response in synthesis rates due to exercise was similar with or without ribose supplementation. De novo synthesis does not increase during exercise but exhibits an unchanged or reduced rate depending on the expected energy balance within the cell. This would occur if the energy state of muscle exerts significant control over de novo synthesis of adenine nucleotide.

Adenine Nucleotides↗
PubMed1998

Intracellular Mg2+ regulates ADP phosphorylation and adenine nucleotide synthesis in human erythrocytes.

13C- and 31P-NMR were used in methylene blue-treated human erythrocytes to determine the dependence on intracellular Mg2+ concentration ([Mg2+]i) of the pentose phosphate pathway (PPP), the glycolytic pathway, and adenine nucleotide synthesis. The PPP flux had an [Mg2+]i at half-maximal velocity ([Mg2+]i,0.5) of 0.02 mM, well below the physiological range (0.2-0.7 mM). Flux through the PPP was reduced at higher [Mg2+]i as flux through phosphofructokinase was increased ([Mg2+]i,0.5 = 0.16 mM). [Mg2+]i,0.5 of phosphoglycerate kinase flux, which equals net ADP phosphorylation rate, was 0.27 mM, well within the physiological [Mg2+]i range. The rate of adenine nucleotide synthesis from [2-13C]glucose-derived ribose 5-phosphate and exogenous adenine also exhibited dependence on [Mg2+]i but was not saturable up to 1.6 mM. Therefore, net flux through the PPP and glycolytic pathways in erythrocytes is not strongly dependent on [Mg2+]i at physiological ion concentrations, but both ADP phosphorylation and adenine nucleotide synthesis are likely to be regulated by normal fluctuations in [Mg2+]i.

Adenine Nucleotides↗
PubMed1977

Metabolism of adenine nucleotides in the cultured fetal mouse heart.

Intact beating fetal mouse hearts in organ culture were deprived of oxygen and glucose for up to 4 h, resulting in loss of beating, an 80% fall in ATP, reduction of energy charge from 0.85 to 0.48, and doubling of total nucleoside concentration. Radiolabeled adenine nucleotides were degraded to hypoxanthine and inosine, which were lost from the hearts into the medium during the deprivation period. Adenosine and adenine also appeared in the medium when adenosine deaminase was inhibited. After 24 h of O2 and glucose resupply, ATP returned to 60% of control, and energy charge rose to 0.76. Labeled nucleosides and bases remaining in the heart or exogenous labeled adenine were utilized to resynthesize ATP. [14C]glycine was rapidly taken up by recovering hearts but was not used for de novo adenine nucleotide synthesis. Ability to recover ATP and spontaneous contraction appear related to residual nucleotide and nucleoside content rather than to energy charge.

Adenine Nucleotides↗
PubMed1981

Adenine nucleotide transport during cardiac ischemia.

The suggestion that long-chain acyl coenzyme A (CoA) derivatives may inhibit mitochondrial adenine nucleotide transport in heart cells during ischemia has been reevaluated. The effectiveness of media palmitoyl-CoA as an inhibitor is a function of mitochondrial protein and media adenine nucleotide concentrations. Extrapolation to the protein and adenine nucleotide levels of the cardiac cell suggest that physiological concentrations of cytosolic long-chain acyl-CoA would not inhibit adenosine 5'-triphosphate (ATP) transport. Palmitoyl-CoA was varied in the mitochondrial matrix by incubating the isolated mitochondria with and without palmitoyl carnitine. Intramitochondrial nucleotides were depleted by incubating the isolated mitochondria for various periods of time with arsenite and phosphate. Even at low substrate (matrix ATP) concentrations, no palmitoyl-CoA inhibition of ATP transport could be demonstrated. Further experiments showed that endogenous nucleotide levels are significantly depleted in mitochondria isolated from hearts made ischemic for 30-90 min. Since mitochondrial adenine nucleotide transport occurs by an exchange mechanism, this depletion of the internal pool of nucleotides from ischemic heart mitochondria may result in an irreversible diminution of ATP transport.

Acyl Coenzyme A↗
PubMed1985

Phosphate-induced efflux of adenine nucleotides from heart mitochondria.

Adenine nucleotide efflux from isolated rat heart mitochondria was studied. Inorganic phosphate induced efflux of adenine nucleotides from the mitochondria. This efflux was inhibited by carboxyatractyloside and atractyloside. The rate of efflux showed saturation kinetics with respect to extramitochondrial phosphate (Km, 9.5 mM). Lowering the pH from 7.4 to 6.8 had little or no effect on the rate of efflux. Deenergizing the mitochondria enhanced carboxyatractyloside-insensitive efflux, but it did not affect carboxyatractyloside-sensitive efflux. Extramitochondrial ATP (200 microM) or AMP (200 microM) prevented efflux when the phosphate concentration was 10 mM. AMP (200 microM) did not inhibit efflux when the phosphate concentration was 40 mM. Atractyloside inhibited efflux noncompetitively with respect to inorganic phosphate. Mersalyl (10 nmol/mg protein) did not inhibit efflux. Phenylsuccinate (20 mM) totally inhibited phosphate-induced efflux. The results of this study indicate that under conditions found in the ischemic heart cell (low ATP, high phosphate), adenine nucleotides may be lost from the mitochondria via the adenine nucleotide translocase. Phosphate does not induce this efflux by interacting with the translocase or the phosphate-hydroxyl carrier. The site of action of phosphate may be the dicarboxylate carrier.

Adenine Nucleotides↗
PubMed1986

Verapamil preserves adenine nucleotide pool in cardiomyopathic Syrian hamster.

There is a decrease in total adenine nucleotides, cyclic AMP (cAMP), ATP/total ADP, and phosphocreatine (PCr)/creatine (Cr) both in situ and in the perfused heart in the heart failure stage of the cardiomyopathic Syrian hamster. There were decreases in developed pressure, dP/dt, and O2 consumption associated with the decrease in total adenine nucleotides and cAMP. Cardiomyopathic Syrian hamsters (180-240 days old) with congestive heart failure were given water with the calcium entry blocker, verapamil, as an additive 2 mo before death. In the cardiomyopathic group given verapamil the adenine nucleotides, cAMP, and high-energy phosphates were preserved and cardiac performance was not significantly different from that of the verapamil-treated healthy hamsters at the time of death. Pretreatment of cardiomyopathic animals with verapamil (6.6 mg verapamil/ml water consumed by drinking) resulted in significantly higher ATP/total ADP and PCr/Cr compared with nontreated cardiomyopathic hamsters. This is the first report demonstrating that a calcium entry blocker may improve cardiac performance and preserve total adenine nucleotides during the heart failure stage of the cardiomyopathic hamster.

Adenine Nucleotides↗
PubMed1992

Prolonged adenine nucleotide resynthesis and reperfusion injury in postischemic skeletal muscle.

Skeletal muscle ischemia results in energy depletion and intracellular acidosis. Reperfusion is associated with impaired adenine nucleotide resynthesis, edema formation, and myocyte necrosis. The purpose of these studies was to define the time course of cellular injury and adenine nucleotide depletion and resynthesis in postischemic skeletal muscle during prolonged reperfusion in vivo. The isolated canine gracilis muscle model was used. After 5 h of ischemia, muscles were reperfused for either 1 or 48 h. Lactate and creatine phosphokinase (CPK) release during reperfusion was calculated from arteriovenous differences and blood flow. Adenine nucleotides, nucleosides, bases, and creatine phosphate were quantified by high-performance liquid chromatography, and muscle necrosis was assessed by nitroblue tetrazolium staining. Reperfusion resulted in a rapid release of lactate, which paralleled the increase in blood flow, and a delayed but prolonged release of CPK. Edema formation and muscle necrosis increased between 1 and 48 h of reperfusion (P less than 0.05). Recovery of energy stores during reperfusion was related to the extent of postischemic necrosis, which correlated with the extent of nucleotide dephosphorylation during ischemia (r = 0.88, P less than 0.001). These results suggest that both adenine nucleotide resynthesis and myocyte necrosis, which are protracted processes in reperfusing skeletal muscle, are related to the extent of nucleotide dephosphorylation during ischemia.

Adenine Nucleotides↗
PubMed1998

Chronic renal failure in a mouse model of human adenine phosphoribosyltransferase deficiency.

In humans, adenine phosphoribosyltransferase (APRT, EC 2.4.2.7) deficiency can manifest as nephrolithiasis, interstitial nephritis, and chronic renal failure. APRT catalyzes synthesis of AMP from adenine and 5-phosphoribosyl-1-pyrophosphate. In the absence of APRT, 2,8-dihydroxyadenine (DHA) is produced from adenine by xanthine dehydrogenase (XDH) and can precipitate in the renal interstitium, resulting in kidney disease. Treatment with allopurinol controls formation of DHA stones by inhibiting XDH activity. Kidney disease in APRT-deficient mice resembles that seen in humans. By age 12 wk, APRT-deficient male mice are, on average, mildly anemic and smaller than normal males. They have extensive renal interstitial damage (assessed by image analysis) and elevated blood urea nitrogen (BUN), and their creatinine clearance rates, which measure excretion of infused creatinine as an estimate of glomerular filtration rate (GFR), are about half that of wild-type males. APRT-deficient males treated with allopurinol in the drinking water had normal BUN and less extensive visible renal damage, but creatinine clearance remained low. Throughout their lifespans, homozygous null female mice manifested significantly less renal damage than homozygous null males of the same age. APRT-deficient females showed no significant impairment of GFR at age 12 wk. Consequences of APRT deficiency in male mice are more pronounced than in females, possibly due to differences in rates of adenine or DHA synthesis or to sex-determined responses of the kidneys.

Adenine Phosphoribosyltransferase↗