Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.16.2 (PCP)
 3,761 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Poliovirus replicase- and host factor-catalyzed copying of 3'-terminal polyadenylic acid [poly(A)] of poliovirion RNA was studied. Host factor-stimulated synthesis of polyuridylic acid [poly(U)] by the replicase required ATP in addition to UTP. ATP was not required for the oligouridylic acid-primed copying of 3'-terminal poly(A) of virion RNA. GTP, CTP, and AMP-PCP (5'-adenylyl beta-gamma methylenediphosphate, an ATP analog) could not replace ATP in host factor-stimulated synthesis of poly(U). Antibodies to poliovirus genome-linked protein (VPg) specifically precipitated in vitro-synthesized poly(U) from a host factor-stimulated reaction. The poly(U) synthesized in a host factor-stimulated reaction was shown to be attached to VPg precursor polypeptide(s) via a tyrosine-phosphate bond as found in poliovirion VPg-RNA.
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PMID:ATP is required for initiation of poliovirus RNA synthesis in vitro: demonstration of tyrosine-phosphate linkage between in vitro-synthesized RNA and genome-linked protein. 632 50

Evidence in this and other reports from this laboratory suggest that adrenergic nerves in rat heart ventricle slices incubated in a Na+-deprived (choline+) medium containing Ca++ (Ch+--Ca++), transport (by a cocaine-sensitive mechanism) 3H-norepinephrine outwardly from synaptic vesicles attached or fused to the plasma membrane. The 3H-amine secretion was not inhibited by probenecid, an anion transport inhibitor which may prevent exocytosis. The 3H-amine release was rapidly inhibited by exogenous nucleotides ATP, UTP, and GTP greater than ADP greater than AMP greater than the nucleoside adenosine. Magnesium++ tended to increase and reserpine to decrease the effect of ATP. Neither increasing the [Ca++] nor [Mg++] (to compete with Ca++ for ATP) decreased the effect of 3 mM ATP. After secretion began, lowering the Ca++ concentration by ommission, or by the inclusion of either a low concentration of EDTA or the Ca++-binding, but non-energy-conserving synthetic analogs of ATP: AMP--PCP and AMP--PNP, gradually lowered the rates of secretion. By comparison, the rapid effects of the energy-conserving nucleotides suggested that their effects were at least partially independent of chelation, and were energy dependent. ATP, unlike cocaine, did not inhibit the uptake of NE in a Krebs HCO3 medium. Inhibition of (Na+ + K+)-ATPase by ouabain neither inhibited the release by Ch+--Ca++, nor antagonizes the release inhibiting effect of ATP. Hence, ATP did not increase apparent retention of NE by stimulating the uptake of released NE. The ATP-inhibited secretion was not increased by theophylline.
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PMID:The effect of exogenous adenosinetriphosphate on the choline-calcium stimulated release of 3H-norepinephrine in rat heart ventricle slices. 668 77

Intracellular ATP-dependent Ca2+-sequestration mechanisms were studied in isolated dispersed rat pancreatic acini following treatment with saponin or digitonin to disrupt their plasma membranes. In the presence of 45Ca2+ concentrations less than 10(-6) mol/liter, addition of 5 mmol/liter ATP caused a rapid increase in 45Ca2+ uptake exceeding the control by fivefold. ADP mimicked the ATP effect by 50 to 60%, whereas other nucleotides such as AMP-PNP, AMP-PCP, CTP, UTP, ITP, GTP, cAMP and cGMP did not. Maximal ATP-promoted Ca2+ uptake was obtained at 10(-5) mol/liter Ca2+. Inhibition of Ca2+ uptake by mitochondrial inhibitors was dependent on the Ca2+ concentration, indicating the presence of different Ca2+ storage systems. Whereas the apparent half-saturation constant found for mitochondrial Ca2+ uptake was approximately 4.5 X 10(-7) mol/liter, in the presence of antimycin and oligomycin (nonmitochondrial uptake) it was approximately 1.4 X 10(-8) mol/liter. In the absence of Mg2+ both ATP- and ADP-promoted Ca2+ uptake was nearly abolished. The Ca2+ ionophore and mersalyl blocked Ca2+ uptake, Electron microscopy showed electron-dense precipitates in the rough endoplasmic reticulum of saponin-treated cells in the presence of Ca2+, oxalate and ATP, which were absent in intact cells and in saponin-cells without ATP or pretreated with A23187. The data suggest the presence of mitochondrial and nonmitochondrial ATP-dependent C2+ storage systems in pancreatic acini. The latter is likely to be located in the rough endoplasmic reticulum.
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PMID:Calcium uptake into acini from rat pancreas: evidence for intracellular ATP-dependent calcium sequestration. 680 Dec 63

1. Dialysed giant axons from the squid have been used to study some of the properties of the Na+ fluxes when the Na+ pump is fully inhibited by strophanthidin. 2. In axons which had been depleted of ATP, strophanthidin had no effect on Na+ efflux. Similar negative results were obtained in axons dialysed with and without internal or external K+, and with or without 100 microM-internal Ca2+. 3. In the presence of 60 mM-internal Na+, 440 mM-external Na+ and strophanthidin, the fluxes of Na+ had the following characteristics. (i) ATP stimulated an efflux and an influx of Na+ of similar magnitude. The K1/2 for ATP, measured from its effect on Na+ efflux, was about 200 microM. (ii) The non-hydrolysable ATP analogue adenylyl(beta, gamma-methylene)-diphosphonate (AMP-PCP), at 2 mM concentration, either alone or in combination with 2 mM-internal phosphate, failed to stimulate any efflux of Na+. (iii) The ATP-dependent Na+ efflux was not affected by removal of internal or external K+, or external Mg2+ or Ca2+, and was not dependent on internal Ca2+. (iv) within the resolution of the method, all the ATP-dependent Na+ influx required internal Na+, and all the ATP-dependent Na+ efflux required external Na+. From the magnitude of the unidirectional Na+ fluxes the stoichiometry seemed to be a 1 to 1 Na+--Na+ exchange. 4. The ATP-internal Na+-dependent influx of Na+ in the presence of strophanthidin was not affected by 1 mM-vandate in the dialysis solution, a concentration which fully inhibits the Na+ efflux through the Na+ pump that is activated by external K+. 5. In the presence of external Na+, the external K+ sites of the Na+ pump are completely saturated with 100 mM-external K+. In unpoisoned axons incubated with 100 mM-external K+, replacement of external Na+ with Tris+ produced no change in the efflux of Na+. However, in axons poisoned with 50 microM-strophanthidin, replacement of external Na+ with Tris+ resulted in a reversible inhibition of Na+ efflux. This could suggest that strophanthidin poisoning might induce Na+ (cations?) fluxes which are not present in normal conditions.
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PMID:An ATP-dependent sodium-sodium exchange in strophanthidin poisoned dialysed squid giant axons. 731 Jul 19

ATP and ADP stimulated the release of specific prostaglandin products from the perfused rabbit kidney heart. The two nucleotides produced the same qualitative profile of prostaglandin products. In kidney, prostaglandin E2 was the major product, whereas in heart 6-keto prostaglandin F1 alpha and prostaglandin E2 predominated. ATP was a slightly more potent than ADP. ATP administered into the perfused heart to kidney was rapidly hydrolyzed to ADP and AMP. The prostaglandin E2 generating activity of ATP was increased 6-10 fold when ATP was given together with AMP-PCP or AMP-PNP which competitively inhibit the activity of vascular ATPase. Thus, the rapid hydrolysis of ATP reduces its agonistic activity for prostaglandin release. ATP and ADP administered together at maximal stimulating doses produced an additive response for prostaglandin E2 release. These results and the results of tachyphylaxis experiments indicate that ATP and ADP interact independently with different types of purinergic receptors.
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PMID:Evidence for different purinergic receptors for ATP and ADP in rabbit kidney and heart. 732 99

Glial cells are closely associated with synapses and are modulated by neurotransmitters released during synaptic transmission. At many synapses, ATP is released during synaptic transmission and is involved in cell-cell signaling. Since glial cells have purinoceptors, it is possible that ATP mediates synaptic neuron-glia signaling. This work aims at determining which types of purinoceptors are present on perisynaptic Schwann cells, the perisynaptic glial cells at the frog neuromuscular junction, and test their sensitivity to endogenous purines by monitoring the relative changes of intracellular Ca2+. Local application of ATP induced the release of Ca2+ from internal stores. Adenosine induced Ca2+ responses that were blocked by A1 receptor antagonists and mimicked by an A1 receptor agonist and were caused by the release of Ca2+ from internal stores via a pertussis toxin-sensitive G-protein. A2 receptor antagonists had no effect on Ca2+ responses induced by adenosine. Me-S-ATP, an ATP analog, triggered Ca2+ release from internal stores via a pertussis toxin-sensitive G-protein, consistent with the activation of P2Y receptors. L-AMP-PCP, another ATP analog, induced Ca2+ entry mainly through L-type Ca2+ channels by a pertussis toxin-insensitive mechanism, consistent with the activation of P2X receptors. Blockade of adenosine receptors did not affect glial Ca2+ responses induced by nerve evoked transmitter release. However, blockade of ATP receptors reduced the size and increased the delay of the responses. Hence, purinoceptors are present on the perisynaptic Schwann cells and are activated by endogenous ATP released during synaptic transmission.
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PMID:Purinergic receptors and their activation by endogenous purines at perisynaptic glial cells of the frog neuromuscular junction. 747 66

The present study was undertaken to observe the changes of Ryanodine receptor of cardiac junctional sarcoplasmic reticulum (SR) in relation to membrane lipid microenvironment alteration during septic shock. The results showed that the Bmax for 3H-ryanodine binding to cardiac junctional SR was decreased by 41.3% (3.9 +/- 0.1 vs. sham 6.6 +/- 0.7 pmol/mg, P < 0.01) while the Kd value was unaffected during late septic shock (CLP 18 h). Ca2+ activated 3H-ryanodine binding significantly and reached a saturation value when Ca2+ concentration was 5 x 10(-5) mol/L, while the S0.5 and the Hill coefficient values remained unchanged during septic shock. Caffeine, ATP, and AMP-PCP activated while Mg2+, ruthenium red inhibited 3H-ryanodine binding in both groups but the A0.5 (concentration requires for half maximum activation) and the IC50 (concentration requires for half-maximum inhibition) for the above mentioned activators and inhibitors, were respectively unaffected during septic shock. Digestion of cardiac SR isolated from control rats with phospholipase A2 inhibited 3H-ryanodine binding, which could be dramatically recovered by the incorporation of phosphatidylcholine (PC), or phosphatidylserine (PS), or phosphatidylethanolamine (PE) into the isolated cardiac SR. Incorporation of above phospolipids into SR isolated from septic rats reversed shock-induced inhibition of 3H-ryanodine binding. It is concluded that the mechanism responsible for the inhibition of 3H-ryanodine binding of junctional SR during septic shock may be related to modification of membrane lipid microenvironment in response to PLA2 overactivation during septic shock.
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PMID:[Altered ryanodine receptor of rat cardiac sarcoplasmic reticulum and its underlying mechanism during septic shock]. 748 76

In a laboratory experiment, effects of chemical stress (pentachlorophenol, PCP, at concentrations of 0, 50, and 500 mg/kg) and biotic interactions (nematodes in the presence or absence of collembolas and enchytraeids) on the community structure of soil animals and decomposition processes were studied. PCP was strongly adsorbed to humus that contained 65% organic matter. Numbers of fungal-feeding nematodes decreased significantly at the highest PCP concentration, while no effects were found in bacterial feeders. There were differences in the numbers of nematodes between different animal combinations, but at the highest PCP concentration, collembolas and enchytraeids had no effect on them. Numbers of collembola Willemia anophtalma were lowered at the highest PCP concentration, although PCP was not acutely toxic at this concentration. The highest PCP concentration was acutely toxic to enchytraeids, and for an unknown reason all of them died in the main experiment. Both ATP content of the soil and soil respiration were reduced at the highest PCP concentration, while no differences were found between animal treatments. Amounts of NH4-N and PO4-P in the soil increased with increasing PCP concentration. It was concluded that in the presence of simple animal communities, harmful chemicals like PCP regulate the community structure of soil animals as well as decomposition and nutrient mobilization.
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PMID:Effects of pentachlorophenol and biotic interactions on soil fauna and decomposition in humus soil. 749 64

Four cDNA-encoding G-activated inwardly rectifying K+ channels have been cloned recently (Kubo, Y., Reuveny, E., Slesinger, P. A., Jan, Y. N., and Jan, L. Y. (1993) Nature 364, 802-806; Lesage, F., Duprat, F., Fink, M., Guillemare, E., Coppola, T., Lazdunski, M., and Hugnot, J. P. (1994) FEBS Lett. 353, 37-42; Krapivinsky, G., Gordon, E. A., Wickman, K., Velimirovic, B., Krapivinsky, L., and Clapham, D. E. (1995) Nature 374, 135-141). We report the cloning of a mouse GIRK2 splice variant, noted mGIRK2A. Both channel proteins are functionally expressed in Xenopus oocytes upon injection of their cRNA, alone or in combination with the GIRK1 cRNA. Three GIRK channels, mGIRK1-3, are shown to be present in the brain. Colocalization in the same neurons of mGIRK1 and mGIRK2 supports the hypothesis that native channels are made by an heteromeric subunit assembly. GIRK3 channels have not been expressed successfully, even in the presence of the other types of subunits. However, GIRK3 chimeras with the amino- and carboxyl-terminal of GIRK2 are functionally expressed in the presence of GIRK1. The expressed mGIRK2 and mGIRK1, -2 currents are blocked by Ba2+ and Cs+ ions. They are not regulated by protein kinase A and protein kinase C. Channel activity runs down in inside-out excised patches, and ATP is required to prevent this rundown. Since the nonhydrolyzable ATP analog AMP-PCP is also active and since addition of kinases A and C as well as alkaline phosphatase does not modify the ATP effect, it is concluded that ATP hydrolysis is not required. An ATP binding process appears to be essential for maintaining a functional state of the neuronal inward rectifier K+ channel. A Na+ binding site on the cytoplasmic face of the membrane acts in synergy with the ATP binding site to stabilize channel activity.
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PMID:Molecular properties of neuronal G-protein-activated inwardly rectifying K+ channels. 749 85

Mitochondrial gene expression in kinetoplastid organisms such as Trypanosoma, Leishmania and Crithidia requires a posttranscriptional RNA processing event known as kRNA editing. During editing, uridine nucleotides get inserted and deleted into pre-mRNAs directed by small, metabolically stable RNAs, termed guide RNAs. Although the precise mechanism of the reaction is not understood, the accepted working model describes the formation of extended anti-parallel RNA helices between gRNA molecules with pre- and partially edited mRNAs as intermediates. These duplex structures must be separated to ensure the sequential action of multiple gRNAs in a 3' to 5' polarity on the mRNA molecule. In spite of this fact, no unwinding activity has heretofore been identified in kinetoplastid mitochondria. We report the characterisation of a RNA helicase activity within Trypanosoma brucei mitochondrial extracts. The activity unwinds 25- and 48 bp, tailed RNA duplex structures but fails to separate DNA strands. It can be destroyed by heat denaturation as well as by proteinase K treatment. The activity requires magnesium cations and acts in a NTP/dNTP dependent manner. Hydrolysis of a nucleoside triphosphate is required rather than mere NTP binding as deduced from a comparison of unwinding in the presence of ATP and AMP-PCP. RNA duplexes mimicking presumed kRNA editing intermediates are substrates of the unwinding activity and therefore, we address the possible involvement of a RNA helicase activity during kRNA editing.
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PMID:Trypanosoma brucei mitochondria contain RNA helicase activity. 752 33


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