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1986 Fluoride Abstracts. Part 1.
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Zhonghua Bing Li Xue Za Zhi 1986 Dec;15(4):297-9
No Abstract available
[Morphology of the brain of the offspring of rats with chronic fluorosis]
[Article in Chinese]
Guan ZZ.
PMID: 2955919 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3743750&dopt=AbstractFarmaco [Sci] 1986 Aug;41(8):586-96
[Phenylethylamine fluorides. II. Synthesis and neurobiochemistry in the rat]
[Article in French]
Charlon C, Luu-Duc C, Huguet F, Gerard P, Narcisse G.
Sixteen fluorinated phenylethylamines analogous to catecholamine were obtained by fluoration from the corresponding amino-alcohols. The biological activity of the compounds was evaluated by determining their affinity for the central adrenergic receptors of rat brain membranes and by measuring the monoamine synaptosomal uptake. These compounds significantly inhibited serotonine uptake, but they showed no affinity for amphetaminergic binding sites.
PMID: 3743750 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3079758&dopt=AbstractJ Biol Chem 1986 Jan 15;261(2):631-7
The purified alpha subunits of Go and Gi from bovine brain require beta gamma for association with phospholipid vesicles.
Sternweis PC.
The purified G-proteins from bovine brain were examined for potential solubility in the absence of detergent. The isolated alpha o and alpha i subunits migrated through sucrose with rates consistent with the existence of monomeric species either in the presence or the absence of cholate. The beta gamma subunits or holo-G-proteins aggregated extensively if cholate was absent. Al3+, Mg2+, and F- prevented the aggregation of alpha o and alpha i caused by the addition of beta gamma and could also prevent the aggregation of alpha s when Gs was examined at higher temperature. The association of subunits with phospholipid vesicles was examined. Whereas beta gamma associated totally with phospholipid vesicles, purified alpha o showed little interaction. alpha o did bind to vesicles containing beta gamma (beta gamma vesicles) in a saturable fashion that indicated a stoichiometric association between the subunits. Treatment with guanosine 5'-(3-O-thio)triphosphate could partially dissociate alpha o that was bound to beta gamma vesicles. These data suggest that beta gamma may be an anchor for association of alpha subunits with membranes and that regulation by these proteins may not be limited to the plasma membrane. This possibility and its implications are discussed. The reversible association of alpha o to beta gamma vesicles may provide a very sensitive system for the study of the interactions between these subunits.
PMID: 3079758 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2875191&dopt=AbstractJ Toxicol Environ Health 1986;19(1):23-32
Acute effects of Soman, Sarin, and Tabun on cyclic nucleotide metabolism in rat striatum.
Liu DD, Watanabe HK, Ho IK, Hoskins B.
Rats were injected sc with 120 micrograms/kg Soman, 120 micrograms/kg Sarin or 240 micrograms/kg Tabun. At 15 min, 2 h, or 6 h after administration, animals were decapitated along with saline-treated controls, and striatal activities of nucleotide cyclases and phosphodiesterases and striatal cyclic nucleotide levels were determined. All three agents had two similar effects on rat striatal cyclic nucleotide systems: they all increased cyclic GMP levels 15 min after their administration, and they all decreased guanylate cyclase activity 2 h after administration. There were also some different effects elicited by these three organophosphorus compounds. Different effects of Soman and Sarin seem to be mainly due to their different potencies, which in turn influence the time course of their actions. Tabun is quite different from Soman and Sarin in several respects: it rarely causes convulsions at sub-lethal doses, it has no effects on striatal cyclic AMP levels, and it affects enzyme activities 6 h after its administration. These differences may be due to the presence of cyanide instead of fluoride in its structure: i.e., this may be responsible for the different effects of Tabun on striatal cyclic nucleotide systems, and perhaps other biochemical effects. These results also indicate that other neurotransmitter systems, in addition to the cholinergic system, may be involved in organophosphate-induced toxicity.
PMID: 2875191 [PubMed - indexed for MEDLINE]
[Note from FAN:
Definition of striatum - collective name for the caudate nucleus and putamen which together with the globus pallidus or pallidum form the striate body. - Ref: Stedman's Concise Medical Dictionary for the Health Professions. Illustrated 4th Edition. 2001.]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3526799&dopt=AbstractActa Neuropathol (Berl) 1986;70(2):142-8
Cytochemical localization of acid phosphatase in the hindbrain of dysraphic mice.
Wilson DB, Wyatt DP.
The cytochemical localization of acid phosphatase (AP) was studied at the ultrastructural level in the abnormal neuroepithelium of dysraphic loop-tail (Lp/Lp) embryos between 9 and 12 days of gestation. At 9-11 days, normal and abnormal embryos showed a positive AP reaction throughout the thickness of the neuroepithelium, i.e., in apical, intermediate, and basal zones, although many cells were unreactive. The reaction is sensitive to sodium fluoride and occurs in saccules and vesicles associated with the Golgi complex, as well as in vacuoles of varying size containing flocculent and particulate material. Gap-junctional vesicles, which are known to occur in increased numbers in abnormal brains, were AP-negative. By 12 days of gestation, the reaction in normal embryos was localized in the midventral marginal layer, where some cell processes were filled with reaction product; in abnormal embryos, these AP-positive processes were not observed. The results indicate that perturbations in lysosomal activity may not be fundamentally involved in the etiology of dysraphism in this mutant.
PMID: 3526799 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3756485&dopt=AbstractBrain Res 1986 Aug 20;380(2):336-40
Acetate and fluoroacetate as possible markers for glial metabolism in vivo.
Muir D, Berl S, Clarke DD.
[3H]Acetate has been shown by light autoradiographic methods to label the neuropil but not the perikarya in brain and retina. [3H]Fluoroacetate behaves similarly. The study provides anatomical data which support the concept of metabolic compartmentation of glutamic acid and associated metabolites previously derived from biochemical studies. It is suggested that these may be markers of non-neuronal metabolism, probably mostly glial, and may be used to develop procedures which will provide complementary data to that obtained with 2-deoxyglucose on regional metabolism in brain.
PMID: 3756485 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3795054&dopt=AbstractJ Pharmacol Exp Ther 1986 Dec;239(3):952-8
Regional modulation of [3H]forskolin binding in the rat brain by guanylyl-5'-imidodiphosphate and sodium fluoride: comparison with the distribution of guanine nucleotide binding sites.
Gehlert DR.
Hormone-sensitive adenylate cyclase is believed to exist as a complex consisting of a catalytic subunit, guanine nucleotide binding regulatory unit and a hormone or neurotransmitter receptor. The diterpene compound, forskolin, is a potent stimulator of adenylate cyclase activity presumably interacting with a site directly on the catalytic subunit. Guanine nucleotides and sodium fluoride stimulate adenylate cyclase through a stimulatory guanine nucleotide binding regulatory subunit. In order to examine the role of the forskolin binding site in the rat brain, the distribution of [3H]forskolin binding sites has been compared with those of a radiolabeled guanine nucleotide analog. [3H]Forskolin densely labeled a few discrete brain regions including the caudate-putamen, nucleus accumbens, olfactory tubercle, globus pallidus and substantia nigra. Specific [3H]guanylyl-5'-imidodiphosphate ([3H]Gpp(NH)p) binding sites were found in high densities in not only these areas but also in the cerebral cortex, thalamus, hypothalamus and midbrain regions. In the hippocampal formation, guanine nucleotide binding sites were seen in the stratum oriens, stratum radiatum, stratum lacunosum molecular and the molecular layer of the dentate gyrus. On the other hand, forskolin labeled the hilus and the pyramidal cell layer of CA3 and CA4 with high density, a region where guanine nucleotide binding was relatively low. Sodium fluoride and Gpp(NH)p were found to enhance forskolin binding in regions in which [3H]Gpp(NH)p binding sites were present. These results indicate that most, but not all forskolin binding sites in the brain, are allosterically coupled with the stimulatory guanine nucleotide binding protein. Conversely, it has also been demonstrated that some forskolin binding sites in the hippocampus are probably not guanine nucleotide regulated.
PMID: 3795054 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3822255&dopt=AbstractNeurotoxicology 1986 Fall;7(3):137-56
Neurobehavioral evaluation of soil and structural fumigators using methyl bromide and sulfuryl fluoride.
Anger WK, Moody L, Burg J, Brightwell WS, Taylor BJ, Russo JM, Dickerson N, Setzer JV, Johnson BL, Hicks K.
Neurobehavioral functions affected by methyl bromide exposure were evaluated in California structural and soil fumigators using methyl bromide and sulfuryl fluoride. Sampling data revealed that structural fumigators are exposed for up to 1.5 hrs/day to 0-2.2 ppm methyl bromide and/or 10-200 ppm sulfuryl fluoride, and soil fumigators can be exposed to 2.3 ppm methyl bromide over an 8-hr day. Subjects were grouped for statistical analysis on the basis of exposure history: Those exposed primarily (80% or more of the work period with exposure potential) to methyl bromide (N = 32), primarily to sulfuryl fluoride (24), or to a combination of methyl bromide and sulfuryl fluoride (40-60% of each) for a minimum of one year (18), and those not exposed to high concentrations of any chemicals (29 Referents). Fumigators using methyl bromide reported a significantly higher prevalence of 18 symptoms consistent with methyl bromide toxicity than did Referents. Methyl bromide fumigators did not perform as well as Referents on 23 of 27 behavioral tests (chosen to reflect methyl bromide effects), and were significantly lower on one test of finger sensitivity and one of cognitive performance. These consistent differences suggest that even the low levels of methyl bromide found in fumigation today may produce slight neurotoxic effects. found in fumigation today may produce slight neurotoxic effects. The greater number of symptoms and reduced performance on all cognitive tests in sulfuryl fluoride fumigators compared to the Reference Group plus the absence of published research on this compound suggest that the data base for sulfuryl fluoride is inadequate.
PMID: 3822255 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3726876&dopt=AbstractToxicol Appl Pharmacol 1986 Jul;84(3):561-6
The inhibition of rat and guinea pig cholinesterases by anionic hydrolysis products of methylphosphonic difluoride (difluoro).
Dahl AR, Hobbs CH, Marshall TC.
Methylphosphonic difluoride (difluoro) and its hydrolysis products, methylphosphonofluoridate (MF) and fluoride, were examined for cholinesterase-inhibiting ability in rats and guinea pigs by both inhalation and intraperitoneal exposure routes. In vivo inhibition was compared to in vitro inhibition. In the whole animal, MF was the active chemical, but in vitro under special conditions, difluoro was more potent than MF and fluoride. Rat and guinea pig blood cholinesterase were equally sensitive to inhibition by MF, but only the guinea pig displayed cholinergic signs leading to death from MF toxicity. Data imply that MF is responsible for the cholinesterase inhibition resulting from exposure to DF vapor. MF may be the first example of a moderately strong acid shown to inhibit cholinesterase and cause death from cholinergic effects.
PMID: 3726876 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3333272&dopt=AbstractMutagenesis 1986 Mar;1(2):157-67
The mutagenicity of sodium fluoride to L5178Y [wild-type and TK+/- (3.7.2c)] mouse lymphoma cells.
Cole J, Muriel WJ, Bridges BA.
MRC Cell Mutation Unit, University of Sussex, Brighton, UK.
L5178Y wild-type and TK+/- (3.7.2c) cells were treated with sodium fluoride over a range of concentrations (10-500 micrograms ml-1) and treatment times (4, 16 and 48 h) covering less than 10-100% survival. The mutant frequency at five genetic loci (resistance to ouabain, 6-thioguanine, excess thymidine, methotrexate and 1-beta-D-arabinofuranosyl cytosine) was assayed in wild-type cells and trifluorothymidine in TK+/- cells. No significant induced mutation at any locus was observed after 4 h of treatment. Sixteen hours of treatment with high concentrations of sodium fluoride did not induce resistance to ouabain, but resulted in some significant induction of 6-thioguanine, 1-beta-D-arabinofuranosyl cytosine and methotrexate resistance, although the results were variable between experiments and no dose-response was observed. At the thymidine kinase locus, a dose-related increase in mutant frequency to excess thymidine and trifluorothymidine resistance was observed. The maximum induction was approximately eight times the control frequency after TK+/- cells were treated with the highly toxic concentration of 500 micrograms ml-1 of sodium fluoride for 16 h. These observations, and an analysis of the colony size of trifluorothymidine-resistant mutants in TK+/- cells, suggest that sodium fluoride is clastogenic to dividing cultured mammalian cells at high, toxic concentrations. Further work is desirable to investigate the mechanism by which chromosomes are damaged at high concentrations of fluoride, since without such a mechanistic understanding, extrapolation of our data to the human situation must be insecure. Nevertheless, the knowledge available at present gives no reason to expect any genotoxic effects in human tissues at levels of fluoride ions to which they are currently exposed in the general population.
PMID: 3333272 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3008868&dopt=AbstractBiol Reprod 1986 Apr;34(3):518-26
Dolichol kinase activity in the developing rat testis.
Berkowitz L, Nyquist SE.
Dolichyl phosphate concentrations, a primary factor in regulating the rate of N-glycosidically linked glycoprotein synthesis, are dependent upon a cytidine triphosphate (CTP)-dependent dolichol kinase. This study examines dolichol kinase in rat testicular microsomes and defines assay conditions. As with dolichol kinases from other tissues, addition of 2-mercaptoethanol increased activity 60%. Inclusion of NaF, an inhibitor of testicular dolichyl phosphate phosphatase activity, also resulted in a 38% increase in activity. Triton X-100 was necessary for phosphorylation of both endogenous and exogenous dolichol; however, concentrations of detergent in excess of 0.25-0.35% were inhibitory. A 2- to 5-fold stimulation of kinase activity was obtained by addition of 50-100 microM exogenous dolichol. The high level of nucleoside triphosphatase activity in testicular microsomes mandated the inclusion of high levels of uridine triphosphate (UTP) to protect the [gamma-32 P] CTP. Increasing UTP concentrations up to 50 mM resulted in increased product formation. A clear requirement for divalent cations was observed; 5 mM ethylenediaminetetraacetate (EDTA) abolished activity. The following order of cation effectiveness was observed: Mn greater than or equal to Ca greater than Cd greater than Zn much greater than Mg. Ten mM optima were established for Ca2+ and Mn2+; the presence of UTP, however, results in significantly reduced concentrations of free Ca2+. Ion combination studies demonstrated interactive inhibitory effects between Ca2+ and other stimulatory divalent cations. Addition of 2 microM brain calmodulin, in the presence of 10 mM Ca2+, resulted in a 75-100% stimulation of activity.(ABSTRACT TRUNCATED AT 250 WORDS)
PMID: 3008868 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3082670&dopt=Abstract
FEBS Lett 1986 Mar 17;198(1):164-8Creutzfeldt-Jakob infection increases adenylate cyclase activity in specific regions of guinea pig brain.
Rasenick MM, Valley S, Manuelidis EE, Manuelidis L.
Creutzfeldt-Jakob disease is a slow, infectious, progressive neurological disorder which results in human dementia. Synaptic membranes from various brain regions of guinea pigs infected with Creutzfeldt-Jakob disease show increased guanyl nucleotide- or 5-hydroxytryptamine-mediated activation of adenylate cyclase. This increased enzyme activity appears due, primarily, to facilitated 'coupling' between the GTP-binding protein which stimulates adenylate cyclase (GNs) and the catalytic moiety of that enzyme rather than increased sensitivity to 5-hydroxytryptamine. It is possible that this phenomenon is due to direct effects of the Creutzfeldt-Jakob infectious agent, or a pathological product resulting from that agent, upon synaptic membrane adenylate cyclase.
PMID: 3082670 [PubMed - indexed for MEDLINE]
Fluoride 1986; 19(4):157-165Fluoride-induced tetrazolium dye reduction by rabbit neutrophils
JGR Elferink
Department of Medical Biochemistry, Sylvius Laboratories, University of Leiden, The Netherlands
Summary: In rabbit neutrophils sodium fluoride (20 mM) induces a strong increase in reduction of the tetrazolium dye iodonitrotetrazolium (INT) indicating an activation of the metabolic burst. This occurs in the absence of extracellular Ca2+; fluoride-induced INT reduction is little influenced by the presence or absence of Ca2+, Mg2+ or Sr2+, but it is strongly inhibited by Co2+, Ni2+, Mn2+ and La3+. In the presence of Ca2+ or La3+ cell damage occurs. Fluoride-induced INT reductionis characterized by a lag time of about 10 min, and is strongly inhbited by Ca2+ -complexing and Ca2+ -antagonistic drugs. The results suggest the involvement of intracellular Ca2+ in fluroide-activation of the metabolic burst. The involvement of phospholipase A2 in the activation is questionable because inhibitors of this enzyme gave divergent results. There is synergism between fluoride and some activators of the metabolic burst, especially phorbol myristate acette, with regard to activtion of INT reduction.
Excerpt: The neutrophil is the first line of defence of the organism against microbial invaders; these are phagocytized and killed by products released by degranulation, and by toxic oxygen products produced during the metabolic burst. The metabolic burst comprises a series of processes, eventually resulting in the enhanced production of toxic oxygen metabolites. Exposure of neutrophils in vitro to certain soluble activators may result in degranulation and a metabolic burst, which enables the study of these processes in the absence of phagocytosis (1).
(1) Klebanoff SJ, Clark RA (1978). The neutrophil: function and clinical disorders. North Holland Publishing Co., Amsterdam.
Fluoride 1986; 19(2):78-79Effect of fluoride and mercury upon the activity of aminotransferases
H Miszta * and Z Dabrowski
* Department of Animal Physiology, Division of Experimental Hematology and Toxicology, Institute of Zoology, Jagiellonian University, Krakow, Poland
Summary: The authors carried out experiments, using blood serum of Wistar rats, to study the synergistic effect of fluoride and mercury upon the activity of aspartate ainotransferase and alanine aminotransferase. When sodium fluroide and mercury chloride were combined enzymatic activity apparently increased in comparison to controls (AspAT - p<0.01 and A1AT - p<0.01). A more conspicuous increase in activities of the studied enzymes was obtained compared to controls, following administration of mercury chloride and sodium fluroide separately (HgCl2 - AspAT - p<0.001 and A1AT - p<0.05, NaF - AspAt - p<0.001 and A1AT - p<0.001).
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3085719&dopt=AbstractBiochim Biophys Acta 1986 May 21;876(3):474-85
Anion effects on the reaction of lecithin-cholesterol acyltransferase with discoidal complexes of phosphatidylcholines . apolipoprotein A-I . cholesterol.
Jonas A, Daehler JL, Wilson ER.
Discoidal complexes of phosphatidylcholine (PC) . apolipoprotein A-I . cholesterol were prepared with egg PC, palmitoyloleoylPC, dipalmitoylPC, or dimyristoylPC, and were used as substrates of purified lecithin-cholesterol acyltransferase to investigate the effects of neutral salts on the enzymatic reaction. Sodium fluoride, chloride and bromide concentrations up to 1 M, did not affect the properties of the substrate particles, but caused marked and distinct changes in the activity of the enzyme with the various PC particles. The effects of salts were largely due to the anions, which followed the order of the lyotropic series in their inactivating capacity: F- less than Cl- less than Br- less than NO3- less than I- less than SCN-. Sodium salts (F-, Cl-, and Br-) produced a very large increase in the pH optimum of the enzymatic reaction (7.4 to at least 8.5) essentially obliterating the ionization of a functional group with pK of 8.1. The kinetics of the enzymatic reaction revealed major differences among the PC particles, and different responses of their kinetic parameters with increasing salt concentrations. The conclusions reached in this work are the following:
(1) The relative reactivity of PC substrates, in discoidal particles, with lecithin-cholesterol acyltransferase depends strongly on the concentration and type of salts in the medium.
(2) Anions (in lyotropic series) rather than cations affect the enzymatic reaction.
(3) There are functional groups with pK of 8.1 which are affected markedly in their ionization behavior by anion binding.
(4) The active site of lecithin-cholesterol acyltransferase and its interaction with anions are affected by the exact nature of the PC-apolipoprotein interface.
PMID: 3085719 [PubMed - indexed for MEDLINE]
ttp://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3019547&dopt=AbstractCardiovasc Res 1986 May;20(5):331-6
Beta adrenoceptor density and adenylate cyclase response in right atrial and left ventricular myocardium of patients with mitral valve disease.
Golf S, Andersen D, Hansson V.
Beta adrenoceptor density, measured by radioligand binding techniques, is reportedly much higher in atrial than in ventricular myocardium of patients with mitral valve disease. In the present study adenylate cyclase activity, both basal and in response to beta adrenergic agonists and sodium fluoride, in biopsy preparations from these same patients was significantly lower in atrial than in ventricular tissue when stimulated with either isoproterenol, noradrenaline, isoproterenol combined with terbutaline, or sodium fluoride. Terbutaline stimulated and basal adenylate cyclase activity was not significantly different in the two cardiac regions. The ratios of receptor density to isoproterenol stimulated and to sodium fluoride stimulated adenylate cyclase activity were 4-5 times higher in atrial than in ventricular biopsy specimens. Thus ventricular beta receptors, although present in comparatively low concentrations, are coupled to considerably more catalytic moieties of the receptor-adenylate cyclase complex than their atrial counterparts. The reason for this is probably a relative lack of coupling proteins (N components) in atrial tissue. A weak positive correlation between receptor density and isoproterenol stimulated adenylate cyclase activity was found in atrial but not in ventricular tissue. This may indicate individual variation in receptor-adenylate cyclase coupling. Furthermore, no correlation was found between atrial and ventricular values for any variable. One reason for this may be the different haemodynamic stresses in the two cardiac chambers.
PMID: 3019547 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3011769&dopt=AbstractJ Biochem (Tokyo) 1986 Apr;99(4):1277-80
Dissociation of Ca2+ mobilization from breakdown of phosphatidylinositol 4,5-bisphosphate in activated human platelets.
Kito M, Narita H, Takamura H, Park HJ, Matsuura T, Tanaka K.
The early breakdown of phosphatidylinositol 4,5-bisphosphate in human platelets stimulated by a threshold concentration of either collagen or thrombin was inhibited by 5 mM NaF through its inhibition of phospholipase C activity. However, 5 mM NaF did not inhibit Ca2+ mobilization due to the stimuli from internal stores, but it did inhibit the influx of extracellular Ca2+ through its suppression of thromboxane A2 formation.
PMID: 3011769 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3005508&dopt=AbstractJ Neurochem 1986 Apr;46(4):1180-5
Forskolin potentiates the stimulation of rat striatal adenylate cyclase mediated by D-1 dopamine receptors, guanine nucleotides, and sodium fluoride.
Battaglia G, Norman AB, Hess EJ, Creese I.
We report here that forskolin acts in a synergistic manner with dopaminergic agonists, guanine nucleotides, or sodium fluoride to potentiate the stimulation of rat striatal adenylate cyclase mediated by these reagents. In the presence of 100 microM GTP, 100 microM guanyl-5'-yl imidodiphosphate [Gpp(NH)p], or 10 mM NaF, there is a greater than additive increase in forskolin-stimulated enzyme activity as well as a concomitant decrease (two- to fourfold) in the EC50 value for forskolin stimulation of striatal enzyme activity. In the presence of various concentrations of forskolin (10 nM-100 microM), the stimulation of adenylate cyclase elicited by GTP, Gpp(NH)p, and NaF is potentiated 194-1,825%, 122-1,141%, and 208-938%, respectively, compared with the stimulation by these agents above basal activity in the absence of forskolin. With respect to 3,4-dihydroxyphenylethylamine (dopamine) receptor-mediated stimulation of striatal enzyme activity, the stimulation of enzyme activity by dopaminergic agonists, in the absence or presence of forskolin, was GTP-dependent and could be antagonized by the selective D-1 antagonist SCH23390 (100 nM), indicating that these effects are mediated by D-1 dopamine receptors. In the presence of 100 microM GTP, forskolin at various concentrations markedly potentiates the stimulation elicited by submaximal as well as a maximally effective concentrations of dopamine (100 microM) and SKF38393 (1 microM). At higher concentrations of forskolin (10-100 microM) the stimulation elicited by the partial agonist SKF38393 is comparable to that of the full agonist dopamine.(ABSTRACT TRUNCATED AT 250 WORDS)
PMID: 3005508 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2871554&dopt=AbstractProc Natl Acad Sci U S A 1986 Apr;83(8):2738-42
An unconventional response of adenylate cyclase to morphine and naloxone in the chicken during early development.
Sakellaridis N, Vernadakis A.
The developmental profile of basal, NaF- and forskolin-stimulated adenylate cyclase [ATP-pyrophosphatelyase (cyclizing), EC 4.6.1.1] activity was established throughout the 21-day embryonic age of the chicken. The highest activities were observed from day 6 to day 8. Morphine inhibited NaF- and forskolin-stimulated brain adenylate cyclase activities only at days 6-8. The inhibition was not reversed by the antagonist naloxone, which also inhibited the enzyme during the same embryonic period and had no inhibitory effect thereafter. Thus, this action of morphine is not mediated through the conventional opiate receptor-adenylate cyclase system. We propose that the temporal specificity of this effect of morphine may play a role in the development of prenatal opiate effects.
PMID: 2871554 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3949884&dopt=AbstractJ Cell Biol 1986 Mar;102(3):959-66
The effects of basic substances and acidic ionophores on the digestion of exogenous and endogenous proteins in mouse peritoneal macrophages.
Ohkuma S, Chudzik J, Poole B.
Basic substances and acidic ionophores that increase the lysosomal pH in cultured macrophages (Ohkuma, S., and B. Poole, 1978, Proc. Natl. Acad. Sci. USA., 75:3327-3331; Poole, B., and S. Ohkuma, 1981, J. Cell Biol., 90:665-669) inhibited the digestion of heat-denatured acetylated bovine serum albumin (BSA) taken up by the cells. For several substances, the shift in pH sufficed to explain the inhibition of proteolysis. Additional effects, presumably on enzyme activities, have to be postulated for tributylamine, amantadine, and chloroquine. Sodium fluoride (10 mM) had no significant effect on the breakdown of BSA by macrophages. The breakdown of endogenous macrophage proteins, whether short lived or long lived, was inhibited approximately 40% by 10 mM NaF and 30%, or sometimes less in the case of long-lived proteins, by 100 microM chloroquine. When the cells were supplied with BSA, a mixture of cell proteins, or even inert endocytosible materials, the breakdown of endogenous long-lived proteins and the inhibitory effect of chloroquine on this process were selectively reduced. Inhibition of endocytosis by cytochalasins B or D did not affect the chloroquine-sensitive breakdown of endogenous proteins, indicating that the proteins degraded by this process were truly endogenous and not taken in from the outside by cellular cannibalism. On the other hand, when macrophage proteins were supplied extracellularly, their breakdown occurred at the same rate for short-lived and long-lived proteins, and it was strongly inhibited by chloroquine and not by NaF. It is concluded from these results that the breakdown of endogenous proteins, both short-lived and long-lived, probably takes place partly (approximately 30%) in lysosomes and partly through one or more nonlysosomal mechanism(s) unaffected by chloroquine and presumably susceptible to inhibition by fluoride. A difference must exist between short-lived and long-lived proteins in the manner in which they reach lysosomes or are handled by these organelles; this difference would account for the selective effect of the supply of endocytosible materials on the lysosomal processing of long-lived proteins.
PMID: 3949884 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3010521&dopt=AbstractUkr Biokhim Zh 1986 Mar-Apr;58(2):34-41
[Influence of effectors of hormone-sensitive adenylate cyclase on the activation system of photostimulated cyclic nucleotide phosphodiesterase from outer rod segments]
[Article in Russian]
Kalinina SN, Etingof RN.
The effect of preincubation of preparations of the outer segments of optic rods with the nonhydrolyzed analog GTP-guanilyl-5'-imidodiphosphate (Gpp(NH)p) and NaF, the combined effect of these agents as well as the action of (NH4)2SO4 (10-800 mM), MgSO4 (2-50 mM) and induction of peroxide oxidation of lipids are studied as applied to the catalytic activity of phosphodiesterase of cyclic nucleotides. Gpp(NH)p and NaF are shown to be tightly bound to GTP-binding proteins (G-proteins) of outer segments of optic rods, additional activation of phosphodiesterase in the presence of Gpp(NH)p being observed after preincubation with NaF and subsequent washing of the membrane. A problem on different binding sites of the ion F and Gpp(NH)p on G-proteins is discussed. It is found that (NH4)2SO4 does not affect the basal activity of phosphodiesterase but inhibits the activating effect of Gpp(NH)p and NaF on the enzyme. Induction of peroxide oxidation of lipids prevented by the addition of ionol (antioxidant) in a dose of 5.10(-4) M has the same effect. Changes in the concentration of Mg2+ in the medium influence insignificantly the basal activity of phosphodiesterase but are necessary for manifestation of the activating effect of Gpp(NH)p and NaF.
PMID: 3010521 [PubMed - indexed for MEDLINE
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3005391&dopt=AbstractJ Histochem Cytochem 1986 Mar;34(3):363-71
Thiamine monophosphatase: a genuine marker for transganglionic regulation of primary sensory neurons.
Knyihar-Csillik E, Bezzegh A, Boti S, Csillik B.
Thiamine monophosphatase (TMPase) has been selectively localized in small dorsal root ganglion cells and in their central and peripheral terminals. Light microscopic localization of TMPase, and its alterations due to transganglionic effects, are identical with those of fluoride-resistant acid phosphatase (FRAP), but are not contaminated by the ubiquitous lysosomal reaction inevitable in trivial acid phosphatase-stained sections. TMPase is inhibited by 0.1 mM NaF, which is slightly less than the concentration needed to inhibit FRAP (0.2-0.4 mM). It is assumed that TMPase and FRAP are identical enzymes. In the perikaryon of small dorsal root ganglion cells, TMPase is located in the cisterns of the endoplasmic reticulum and in the Golgi apparatus. The central terminals of these cells are scalloped (sinusoid) axon terminals, surrounded by membrane-bound TMPase activity. Central terminals outline substantia gelatinosa Rolandi throughout the spinal cord, as well as the analogous nucleus spinalis trigemini in the medulla. TMPase-active central terminals outline "faisceau de la corne posterieure" in the sacral cord, as well as Lissauer's tract in the thoracic, upper lumbar, and sacral segments, and the paratrigeminal nucleus and the terminal (sensory) nucleus of the ala cinerea in the brainstem. Peripheral terminals displaying TMPase activity are fine nerve plexuses of C fibers. The TMPase activity of the central terminals disappears after dorsal rhizotomy in the course of Wallerian degeneration, and is depleted in the course of transganglionic degenerative atrophy (after transection of the related peripheral sensory nerve). TMPase is an outstanding genuine marker for the study of transganglionic regulation in Muridae.
PMID: 3005391 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3632976&dopt=AbstractJ Biol Chem 1986 Feb 5;261(4):1562-9
Interactions between diphtheria toxin entry and anion transport in vero cells. III. Effect on toxin binding and anion transport of tumor-promoting phorbol esters, vanadate, fluoride, and salicylate.
Olsnes S, Carvajal E, Sandvig K.
When Vero cells were incubated with TPA (12-O-tetradecanoylphorbol 13-acetate) and related tumor promoters, their ability to bind diphtheria toxin in a functional way was rapidly reduced to less than 1% of the normal value. Upon further incubation with TPA, the cells recovered their ability to bind the toxin, apparently because they became resistant to TPA. Treatment with Na3VO4 reduced the ability of the cells to bind diphtheria toxin to approximately the same extent as treatment with TPA, but the reduction required longer time to develop and it persisted upon prolonged incubation with Na3VO4. ATP depletion of the cells prevented the reduction in binding capability. Such treatment also prevented the reduction in toxin binding induced by treatment with salicylate or fluoride. Treatment with TPA, fluoride, vanadate, and salicylate altered the ability of the cells to carry out anion transport and interfered with their ability to regulate the transport. The results indicate that the binding sites for diphtheria toxin on Vero cells are modulated by TPA, Na3VO4, salicylate, and fluoride by a process which requires ATP. The possibility is discussed that the modulation consists in phosphorylation of the toxin binding sites, which may be identical with, or closely linked to, the anion antiporter in the cells.
PMID: 3632976 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3001042&dopt=AbstractJ Biol Chem 1986 Jan 5;261(1):101-7
Aluminum ions are required for stabilization and inhibition of hepatic microsomal glucose-6-phosphatase by sodium fluoride.
Lange AJ, Arion WJ, Burchell A, Burchell B.
Stabilization and inhibition of hepatic microsomal glucose-6-P phosphohydrolase (EC 3.1.3.9) by F- requires the presence of Al3+ ions. At millimolar concentrations, reagent grade NaF inhibited glucose-6-P hydrolysis and protected the enzyme against inactivation induced by heat in the presence of 0.025% (w/v) Triton X-100 or by reaction of the catalytic site with the histidine-specific reagent, diethyl pyrocarbonate. The presence of millimolar EDTA in all test systems abolished the effectiveness of NaF, yet EDTA by itself was without significant influence on the kinetics of phosphohydrolase reaction, the thermal stability of the enzyme or its reactivity with diethyl pyrocarbonate. Although ultrapure NaF was ineffectual in all test systems, its potency as a competitive inhibitor or protective agent was markedly increased by micromolar AlCl3 or when assays were carried out in flint glass test tubes. The latter response is explained by the well documented ability of fluoride solutions to extract Al3+ from glass at neutral pH. Our analysis indicates that the effectiveness of fluoride in all test systems derives from the formation of a specific complex with Al3+, most likely Al(F)4-. The apparent dissociation constant for interaction of the enzyme and Al(F)4- is 0.1 microM. The combination of NaF and AlCl3 holds promise as an unusually effective and versatile means to stabilize this notoriously labile enzyme during efforts to purify it.
PMID: 3001042 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3729335&dopt=AbstractAntimicrob Agents Chemother 1986 Jan;29(1):58-61
Role of the cell membrane in pH-dependent fluoride inhibition of glucose uptake by Streptococcus mutans.
Germaine GR, Tellefson LM.
The effect of pH on the fluoride sensitivity of glucose uptake by whole cells and glucose transport by permeabilized cells of Streptococcus mutans was compared. Whole cells exhibited a marked pH-dependent sensitivity to fluoride over the pH range 7.0 to 5.0. As the pH was decreased, fluoride sensitivity increased. In contrast, no significant effect of pH on the fluoride sensitivity of glucose transport (e.g., phosphorylation) by permeabilized cells energized with 2-phosphoglycerate was noted. The relative effect of pH on the fluoride sensitivity of whole cell glucose uptake and fermentation was similar. These data are consistent with the notion that the cell membrane is impermeable to the fluoride anion and that intracellular accumulation of fluoride depends on translocation of hydrogen fluoride across the membrane.
PMID: 3729335 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3038162&dopt=AbstractPol Arch Weter 1986;26(1-2):73-80
[Demonstration and classification of heterogeneity of phosphoprotein phosphohydrolase in swine spleen extracts based on sodium fluoride inhibition]
[Article in Polish]
Mierzejewski T.
The heterogeneity of phosphoprotein phosphohydrolase--Fpf in cellular free spleen extracts of pigs may be determined by sodium fluoride inhibition. NaF concentration of 5 X 10(-3) mol/l divides Fpf into 3 groups and shows a wide inhibition range from 15 to 85% of the initial activity of the enzyme. Naf concentration of 5 X 10(-4)mol/l stops Fpf activity in the range from 10 to 65% and divides it into two groups. To classify the studied material into Fpf phenotypes, fluoride quotient index--WIF has been proposed which expresses the relationship between the percentage of the inhibition caused by NaF at a concentration 5 X 10(-3) mol/l and that of the inhibition caused by NaF at a concentration of 5 X 10(-4) mol/l in the reaction mixture and in the measurement conditions described in the methods. Five groups with the following numerical values of WIF have been distinguished: 1.15 less than or equal to WIF less than 1.40-44%--group I; 1.50 less than or equal to WIF less than 1.80-20%--group II; 1.90 less than or equal to WIF less than 2.10-16%--group III; 2.20 less than or equal to WIF less than 2.50-16%--group IV; and WIF = 3-4%--group V.
PMID: 3038162 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3028102&dopt=AbstractNo Abstract available
Agents Actions Suppl 1986;20:175-80
On the role of guanine nucleotide binding regulatory proteins (G-proteins) in signal transduction in human platelets: studies with sodium fluoride (NaF).
Kienast J, Arnout J, Deckmyn H, Pfliegler G, Hoet B, Vermylen J.
PMID: 3028102 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2427040&dopt=AbstractArch Dermatol Res 1986;278(4):293-7
Receptor-linked adenylate cyclase in the membranes of cultured human epidermal keratinocytes.
Cavey MT, Cavey D, Shroot B, Reichert U, Gazith J.
The beta-adrenergic receptors, previously shown to be present on the membranes of cultured human epidermal keratinocytes, were found to be functionally coupled to membrane-bound adenylate cyclase. Using membrane preparations, the enzyme could be activated by guanosine triphosphate (GTP), the stable GTP analog GPP(HN)p, and NaF, all of which are known to activate the adenylate cyclase without interacting with membrane receptors. Binding of catecholamine agonists (epinephrine, norepinephrine, and isoproterenol) to the beta-adrenergic receptors is followed by an increase in the activity of adenylate cyclase. This activation could be reversed (or prevented) by beta-adrenergic antagonists, but was unaffect by the presence of alpha-adrenergic ligands (either agonists or antagonists). The activation by catecholamines appears to be directly related to receptor occupancy, since the activation constant (Ka) of adenylate cyclase for the three catecholamines was found to be very similar to the equilibrium dissociation constant (Kd) determined from competition binding experiments. The activation of adenylate cyclase under these conditions appears to be restricted to the catecholamine agonists only. The non-catecholamine beta-adrenergic agonists (salbutamol, terbutaline) did not show any measurable activation of adenylate cyclase, even though these agonists were shown previously to bind to the beta-adrenergic receptors on keratinocyte membranes with the expected affinities.
PMID: 2427040 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3014731&dopt=AbstractVision Res 1986;26(3):383-9
Effect of fluoride on the phosphodiesterase of bovine photoreceptors.
Bignetti E, Sorbi RT, Tirindelli R.
In the absence of the specific hormone, fluoride is able to activate the adenylate cyclase because it interacts with the GTP-binding protein. It has been reported that fluoride activates also the phosphodiesterase of the light-sensitive enzymatic cascade in dark-adapted retinal rod outer segments, but there is no indication that the GTP-binding protein is involved in this process or not. We show here that also in the photoreceptor system fluoride does interact with the GTP-binding protein in order to activate the phosphodiesterase in the dark. Further, we show evidences that fluoride solubilizes the GTP-binding protein in the dark and that the resulting complex activates the phosphodiesterase in dark-adapted rod outer segment membranes.
PMID: 3014731 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3719146&dopt=AbstractNo Abstract available
Bull Environ Contam Toxicol 1986 Jul;37(1):70-6
Fluoride and lipid peroxidation: a comparative study in different rat tissues.
Shayiq RM, Raza H, Kidwai AM.
PMID: 3719146 [PubMed - indexed for MEDLINE]
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