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  • 1
    ISSN: 1432-0428
    Keywords: Glueocorticoids ; 3′,5′-AMP phosphodiesterase ; lipolysis ; glycogen metabolism ; insulin ; lipolytic action of glucocorticoids ; glucocorticoid-interaction with insulin ; cyclic adenosine 3′,5′-monophosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Résumé Les glucocorticoïdes stimulent la lipolyse qui est réduite chez les animaux surrénalectomisés. Cette action hormonale est contrecarrée par l'insuline. L'action antilipolytique de l'insuline semble être due à une réduction de la concentration intracellulaire de 3′5′-AMP. Cette réduction peut être attribuée en partie à une accélération due à l'insuline de la dégradation du 3′5′-AMP. On a montré que l'influence stimulatrice des glucocorticoïdes sur la lipolyse est due à une réduction de l'activité de la 3′5′-AMP-phosphodiesterase (PDE), qui est accrue par la surrénalectomie. L'activité de la phosphodiesterase est également augmentée dans le foie, le muscle strié et les reins des rats surrénalectomisés, le traitement par un glucocorticoïde prévient cette augmentation.In vitro, la phosphodiesterase purifiée du coeur de boeuf est inhibée par les glucocorticoïdes à fortes concentrations (K i=1.1 · 10−3 M pour l'hémisuccinate de 6 α-méthylprednisolone, (K i=1.6 · 10−3 M pour le succinate de prednisolone).In vivo, la diminution provoquée par les glucocorticoïdes de l'activité de la phosphodiesterase qui se produit au bout de quelque temps, comme on l'a montré dans le foie, peut essentiellement être attribuée à une synthèse diminuée de l'enzyme. Des études sur l'interaction de l'insuline et des glucocorticoïdes sur l'activité de la phosphodiesterase ont été effectuées sur le foie. Chez les rats surrénalectomisés, rendus diabétiques par l'alloxane, l'insuline stimule l'activité de la phosphodiesterase qui a été supprimée par un traitement avec un glucocorticoïde, l'activité de la phosphodiesterase qui n'a pas été supprimée n'est pas augmentée par l'insuline. Par contre, l'action des glucocorticoïdes sur l'activité de la phosphodiesterase est indépendante de l'action de l'insuline.
    Abstract: Zusammenfassung Die Lipolyse, die bei adrenalektomierten Tieren vermindert ist, wird durch Glucocorticoide verstärkt. Die gegenüber Glucocorticoiden antagonistische Wirkung von Insulin, das die Lipolyse vermindert, kann durch eine Abnahme der intracellulären 3′,5′-AMP-Konzentration erklärt werden. Diese ist teilweise auf einen beschleunigten Abbau des Nucleotids zurückzuführen. — Die Lipolysesteigerung durch Glucocorticoide ist durch eine Verminderung der 3′,5′-AMP-Phosphodiesterase (PDE)-Aktivität bedingt, die bei adrenalektomierten Ratten erhöht ist. Die PDE-Aktivität adrenalektomierter Tiere ist auch in Leber, Skeletmuskulatur und Niere erhöht, die Gabe eines Glucocorticoids verhindert diesen Anstieg. Glucocorticoide hemmen aus Rinderherz isolierte PDEin vitro, jedoch sind hohe Steroidkonzentrationen erforderlich (K i=1.1 · 10−3 M für 6 α-Methylprednisolon-Hemisuceinat, (K i=1,6 · 10−3 M für Prednisolon-Succinat). Die einige Stunden nach Gabe eines Glucocorticoids einsetzende Abnahme der PDE-Aktivität kann im wesentlichen auf eine verminderte Enzymsynthese zurückgeführt werden. — Insulin steigert bei adrenalektomierten, alloxandiabetischen Ratten die PDE-Aktivität in der Leber nur, wenn die Tiere mit einem Glucocorticoid behandelt sind, nicht jedoch die erhöhte PDE-Aktivität bei Fehlen von Glucocorticoiden. Der Einfluß von Glucocorticoiden auf die PDE-Aktivität ist dagegen nicht an die Wirkung von Insulin gebunden.
    Notes: Summary Glucocorticoids stimulate the rate of lipolysis which is reduced in adrenalectomized animals. This hormonal action is antagonized by insulin. The antilipolytic action of insulin appears to be mediated by a reduced intracellular concentration of 3′,5′-AMP. This reduction can partly be attributed to an insulin-induced acceleration of 3′,5′-AMP degradation. — It is shown that the stimulatory influence of glucocorticoids on lipolysis is due to a reduction of 3′,5′-AMP phosphodiesterase (PDE) activity, which is increased by adrenalectomy. PDE activity was also increased in liver, skeletal muscle and kidney of adrenalectomized rats; treatment with a glucoeorticoid prevented this increase.In vitro, PDE purified from beef heart was inhibited by glucocorticoids in high concentrations (Ki=1.1 · 10−3 M for 6 α-methylprednisolone hemisuccinate,K i=1.6 · 10−3 M for prednisolone succinate).In vivo, the glucocorticoid-induced decrease of PDE activity (with retarded onset as shown in liver), may essentially be attributed to a decreased enzyme synthesis. — Studies on the interaction of insulin and glucocorticoids on PDE activity were performed in the liver. In adrenalectomized, alloxan diabetic rats insulin stimulated PDE activity suppressed by treatment with a glucoeorticoid, unsuppressed PDE activity was not increased by insulin. In contrast, the action of glucocorticoids on PDE activity was independent of the presence or the effectiveness of insulin.
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  • 2
    ISSN: 1432-0428
    Keywords: Insulin ; 3′,5′-AMP phosphodiesterase ; glycogen metabolism ; lipolysis ; insulin secretion ; antilipolytic action of insulin ; glycogen synthesis and insulin ; cyclic adenosine 3′,5′-monophosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Résumé L'influence de l'insuline sur le métabolisme du glycogène hépatique et sur la lipolyse semble s'exercer par l'intermédiaire d'une diminution de la concentration de 3,′5′-AMP intracellulaire. Onamontré une diminution de la formation de 3′5′-AMP dans le tissu adipeux incubé avec de l'insuline. L'influence de l'insuline sur la dégradation du 3,′5′-AMP est étudiée. — L'activité de la 3,′5′-AMP-phos-phodiestérase (PDE) est diminuée dans le foie, le tissu adipeux et, de façon non-significative, dans le muscle strié des rats qui manquent d'insuline, c-à-d les rats rendus diabétiques par l'alloxane ou les rats privés de nourriture. L'injection intraveineuse d'une faible dose d'insuline (0.5 U/kg) ou la stimulation de la sécrétion d'insuline endogène par une injection de glucose provoquent une augmentation rapide de l'activité de la phosphodiestérase dans ces tissus. 15 min après l'injection d'insuline, l'activité de la phosphodiesterase du foie est augmentée. L'effet maximum est atteint après 30–45 min. L'activité de la phosphodiestérase rénale n'est pas diminuée dans le diabète alloxanique, l'injection d'insuline s'est avérée inefficace.In vitro, l'insuline cristalline a un effet activant sur la phosphodiestérase purifiée du coeur de boeuf. La concentration d'insuline requise pour doubler l'activité de l'enzyme est de l'ordre de 2 · 10−5 M. Le traitement avec actinomycin D empêche la stimulation par l'insuline de la PDE dans le foie. Ceci peut indiquer que l'action de l'insuline sur l'activité de la phosphodiestérase est essentiellement basée sur une synthèse accrue de l'enzyme. A cause de l'influence de la sécrétion d'insuline sur la concentration en 3,′5′-AMP du foie et du tissu adipeux, le métabolisme du glycogène et la lipolyse peuvent s'adapter rapidement à la prise de nourriture.
    Abstract: Zusammenfassung An der Steigerung der Glykogensynthese der Leber und der Verminderung der Lipolyse durch Insulin ist eine Abnahme der 3′,5′-AMP-Konzentration wesentlich beteiligt. Die 3′,5′-AMP-Bildung ist in Fettgewebe, das mit Insulin inkubiert wird, vermindert. Insulin beeinflußt jedoch auch den 3′,5′-AMP-Abbau. -Die 3′,5′-AMP-Phosphodiesterase (PDE)-Aktivität des Fettgewebes, der Leber und, in geringerem Grade, der Skeletmuskulatur ist im Insulinmangel vermindert, d.h. bei alloxandiabetischen oder hungernden Ratten. I.v. Injektion von 0,5 E/kg Insulin oder eine erhöhte Abgabe von Insulin aus dem Pankreas nach Glucoseinjektion führen in diesen Geweben zu einem raschen Anstieg der PDE-Aktivität. Dieser ist in der Leber schon 15 min nach Insulingabe nachweisbar und erreicht nach 30–45 min sein Maximum. In der Niere ist kein Einfluß von Insulin auf die PDE-Aktivität nachweisbar. — Aus Rinderherz isolierte PDE wirdin vitro durch Insulin aktiviert, jedoch werden2 · 10−5 M zur Verdopplung der Aktivität benötigt. Actinomycin D verhindert die Steigerung der Leber-PDE-Aktivität nach Insulininjektion. So kann die Wirkung des Hormons im wesentlichen auf eine gesteigerte PDE-Synthese zurückgeführt werden. — Durch diesen Einfluß der Insulininkretion auf die 3′,5′-AMP-Konzentration in Leber und Fettgewebe können Glykogenstoffwechsel und Lipolyse rasch an die Nahrungsaufnahme angepaßt werden.
    Notes: Summary Influence of insulin on liver glycogen metabolism and on lipolysis appears to be mediated by a decreased intracellular 3′,5′-AMP concentration. Reduced formation of 3′,5′-AMP had been shown in adipose tissue incubated with insulin. The influence of insulin on 3′,5′-AMP degradation has been investigated. — 3′,5′-AMP phosphodiesterase (PDE) activity was reduced in liver, adipose tissue and, insignificantly, in skeletal muscle of insulin deficient, i.e. alloxan diabetic or starved rats. I.V. injection of a low dose of insulin (0.5 U/kg) or stimulation of endogenous insulin secretion by injection of glucose led to a rapid increase of PDE activity in these tissues. 15 min after insulin injection liver PDE activity was increased. The maximal effect occurred after 30–45 min. Renal PDE activity was not decreased in alloxan diabetes, insulin injection has been found ineffective. —In vitro, there was an activating effect of crystalline insulin on PDE purified from beef heart. Insulin concentration required for duplication of enzyme activity was of the order of 2 · 10−5 M. Treatment with actinomycin D nearly prevented stimulation of liver PDE by insulin. This may indicate that the action of insulin on PDE activity is essentially based on an increased enzyme synthesis. — Owing to the influence of insulin secretion on liver and adipose tissue 3′,5′-AMP concentration, glycogen metabolism and lipolysis can be quickly adapted to food intake.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 49 (1971), S. 1049-1058 
    ISSN: 1432-1440
    Keywords: Adenosine 3′:5′-monophosphate ; guanosine 3′:5′-monophosphate ; adenyl cyclase ; guanyl cyclase ; phosphodiesterase ; cyclic nucleotides ; intracellular second messengers ; hormone hormone actions ; glycogen metabolism ; lipolysis ; Adenosin-3′:5′-monophosphat ; Guanosin-3′:5′-monophosphat ; Adenyl-Cyclase ; Guanyl-Cyclase ; Phosphodiesterase ; cyclische Nucleotide ; intracelluläre Überträger-stoffe ; Hormonwirkungen ; Glykogen-Stoffwechsel ; Lipolyse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Hormone dienen als extracelluläre Informationsüberträger zwischen ihrem Bildungsort, einer endokrinen Drüse, und den Zellen, deren Funktion sie regulieren. Durch die Reaktion des Hormons mit den an der Zellmembran gelegenen Receptoren wird die Aktivität der mit diesen eng verknüpften Adenyl-Cyclase beeinflußt. Die meisten Hormone erhöhen in ihrem Zielorgan die Aktivität dieses Enzyms und führen hierdurch zu einem raschen Anstieg der intracellulären Konzentration von Adenosin-3′:5′-monophosphat (Ado-3′:5′-P). Dieses cyclische Nucleotid wird durch eine spezifische Phosphodiesterase zu Adenosin-5′-monophosphat abgebaut. Auch die Aktivität dieses Enzyms bestimmt die intracelluläre Ado-3′:5′-P-Konzentration, die im Vergleich zu der anderer Nucleotide sehr gering ist. Ado-3′:5′-P beeinflußt als zweiter, intracellulärer Überträgerstoff die Aktivität zahlreicher Schlüsselenzyme. Die Ado-3′:5′-P-Konzentration bestimmt hierdurch das Gleichgewicht verschiedener Stoffwechselwege zueinander und damit die Reaktion einer Zelle auf eine hormonale Stimulierung. An einer Reihe von Enzymen wird die durch Ado-3′:5′-P bedingte Aktivitäts-Änderung durch einen gleichartigen Mechanismus bewirkt. Das cyclische Nucleotid stimuliert Proteinkinasen, die eine Phosphatgruppe des ATP auf verschiedene Proteine übertragen und hierdurch deren Eigenschaften verändern können. So steigt bei Phosphorylierung durch eine Ado-3′:5′-P-stimulierbare Proteinkinase die Aktivität der Triglyceridlipase und der Glykogen-Phosphorylase-b-kinase an, dagegen nimmt die Aktivität der Glykogen-Synthetase ab; durch Phosphorylierung von Histonen kann deren Repressorcigenschaft vermindert und die Synthese von Enzymen gesteigert werden. In manchen tierischen Geweben wurde auch eine spezifisch durch Guanosin-3′:5′-monophosphat (Guo-3′:5′-P) stimulierbare Proteinkinase nachgewiesen. Dieses cyclische Nucleotid kommt wie Ado-3′:5′-P in allen Säugerorganen vor. Die Bildung von Guo-3′:5′-P aus GTP wird durch die Guanyl-Cyclase katalysiert, ein Ferment, das im Gegensatz zur Adenyl-Cyclase zum großen Teil nicht an die Zellmembranen gebunden ist. Die Konzentration von Guo-3′:5′-P in verschiedenen Geweben, im Blutplasma und im Urin wird durch Hormone beeinflußt. Es ist noch nicht bekannt, welche hormonalen Regulationen durch Guo-3′:5′-P vermittelt werden; dagegen ist bei vielen, rasch einsetzenden Hormonwirkungen die Beteiligung von Ado-3′:5′-P nachgewiesen worden.
    Notes: Summary In the extracellular space, hormones transmit informations from the endocrine glands to the target tissues. At the cell membrane the hormone reacts with specific receptors which are assumed to be a integrated part of the adenyl cyclase system. Most of the hormones provoke an increase in adenyl cyclase activity of the target cells thereby causing a rapid elevation of the intracellular concentration of adenosine 3′:5′-monophosphate (Ado-3′:5′-P). This cyclic nucleotide is degraded to adenosine 5′-monophosphate by a specific phosphodiesterase. The activity of this enzyme also influences the intracellular Ado-3′:5′-P concentration which is very low compared to the concentrations of other nucleotides. As an intracellular second messenger, Ado-3′:5′-P influences the activities of various key enzymes. Thereby, the intracellular concentration of Ado-3′:5′-P controls the relative velocities of various metabolic pathways and an alteration of the intracellular Ado-3′:5′-P concentration results in a cellular reaction to the hormonal stimulation. In various enzymes, Ado-3′:5′-P affects the activity by a similar enzymatic mechanism. Ado-3′:5′-P increases the activity of protein kinases which transfer a phosphate group from ATP to various proteins thereby altering their properties. The phosphorylation by an Ado-3′:5′-P-stimulated protein kinase causes an increase in the activities of triglyceride lipase and glycogen phosphorylase-b-kinase and a decreased glycogen synthetase activity, histones may become less effective as repressors of protein synthesis. A protein kinase stimulated by guanosine 3′:5′-monophosphate (Guo-3′:5′-P) has been detected in various tissues. Guo-3′:5′-P like Ado-3′:5′-P is found in all mammalian tissues studied. In contrast to adenyl cyclase, guanyl cyclase which enzyme catalyzes the formation of Guo-3′:5′-P from GTP, is not bound to cell membranes in many tissues. Guo-3′:5′-P concentrations in tissues, blood plasm and urine are affected by hormones. However, it is still unknown which hormonal regulations are mediated by Guo-3′:5′-P, whereas Ado-3′:5′-P has been etablished as a second messenger in the action of a great number of hormones.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 66 (1988), S. 511-523 
    ISSN: 1432-1440
    Keywords: Transmembranous signalling ; Guanine nucleotide-binding proteins (G-proteins) ; Receptor-effector-coupling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The vast majority of extracellular signals alters cell function by activating cell surface receptors. The transmembranous signalling process initiated by an activated receptor leads to the generation of an intracellular signal and eventually to a cellular response. In contrast to receptors that are permanently coupled to an enzyme or an ion channel representing the effector, a large number of surface receptors for hormones, neurotransmitters and receptors for exogenous chemical or physical stimuli reversibly interacts with membranous signal transduction components which, in turn, regulate intracellular messenger-generating effectors. The transducer molecules isolated so far form a family of guanine nucleotide-binding proteins (G- or N-proteins). All isolated G-proteins are composed of three different subunits (α, β, γ). The α-subunit, which is specific for the individual G-protein, binds and hydrolyzes GTP and is target of ADP-ribosylating bacterial toxins. Hormone-induced activation of a receptor causes interaction with the α-subunit of a G-protein and the exchange of bound GDP with GTP. The GTP-bound form of the α-subunit represents the active form of the G-protein, which is capable of stimulating or inhibiting the respective effector. The active state of the α-subunit is terminated by its inherent GTPase activity causing hydrolysis of bound GTP. The βγ-complexes of G-proteins are structurally very similar and functionally interchangeable; they appear to dissociate from the α-subunits during receptor activation of the G-protein. Possible functions of the βγ-complex are to anchor the non-activated G-protein in the membrane, to facilitate G-protein-receptor interaction, and to promote the inactive state of the α-subunit. G-protein-regulated effectors include enzymes, ion channels and probably transporters. The best studied G-protein-regulated enzyme is the retinal cyclic GMP-phosphodiesterase which is activated by bleached rhodopsinvia the tissue-specific G-protein, termed transducin. The ubiquitously occurring membrane-bound adenylate cyclase is under dual control by families of stimulatory and inhibitory receptors, actingvia G-proteins called Gs and Gi, respectively. Moreover, the receptor control of phospholipases A2 and C and probably of phospholipase D most likely involves G-proteins which have not yet been identified. Finally, the activity of NADPH oxidase of neutrophils and that of cyclic AMP phosphodiesterases in liver and fat cells may be regulatedvia G-proteins. Modulations of non-enzymatic effectors are reviewed elsewhere.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 66 (1988), S. 557-564 
    ISSN: 1432-1440
    Keywords: Transmembranous signalling ; Receptors ; Guanine nucleotide-binding proteins (G-proteins) ; Ion channels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary G-proteins act as transducers between cell surface receptors activated by extracellular signals and enzymatic effectors which control the concentrations of cytosolic signal molecules such as cAMP, cGMP, inositol phosphates and calcium. The receptor/G-protein-induced changes of the intracellular concentration of such signal molecules correlates with activity changes of various voltage-dependent ion channels. In some instances, cytosolic signal molecules appear to interact directly with ion channels, thereby causing an alteration of ion channel activity. In other instances, signal molecules affect the function of ion channels by activating protein kinases which, in turn, phosphorylate either proteins constituting extracellular signal- and voltage-dependent ion channels or non-identified membranous regulatory components. Recent findings suggest a third, membrane-confined mechanism which does not involve cytosolic signal molecules but a close control of voltage-dependent ion channels by G-proteins. Ion channels that are modulated by extracellular signals according to this newly discovered principle include those for calcium and potassium in neuronal, cardiac and endocrine cells. G-proteins involved in the hormonal stimulation of potassium and calcium channels belong to the family of Gi-type G-proteins which are functionally uncoupled from activating receptors by pertussis toxin. In addition, the cholera toxin-sensitive G-protein, Gs, may directly stimulate cardiac calcium channels. Hormonal inhibition of calcium channels is possibly mediated by Go which, like G-proteins of the Gi-family, is functionally impaired by pertussis toxin. Whether G-proteins act by binding directly to ion channels or whether they interact with so far unknown regulatory components of the plasma membrane remains to be clarified. Properties of G-proteins and G-protein control of enzymatic effectors have been reviewed elsewhere [60].
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 73 (1995), S. 121-122 
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 73 (1995), S. 123-132 
    ISSN: 1432-1440
    Keywords: Cellular effectors ; Cellular signaling ; G protein ; Heptahelical receptor ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Seven-transmembrane receptors signal through nucleotide-binding proteins (G proteins) into the cell. G proteins are membrane-associated proteins composed of three subunits termed α, β and γ, of which the Gα subunit classifies the heterotrimer. So far, 23 different mammalian Gα subunits are known, which are grouped in four subfamilies (Gs, Gi, Gq, G12) on the basis of their amino acid similarity. They carry an endogenous GTPase activity allowing reversible functional coupling between ligand-bound receptors and effectors such as enzymes and ion channels. In addition, five Gβ and seven Gγ subunits have been identified which form tightly associated βγ heterodimers. Upon activation by a ligand-bound receptor the G protein dissociates into Gα and Gβγ, which both transmit signal by interacting with effectors. On the G protein level, specificity and selectivity of the incoming signal is accomplished by G protein trimers composed of distinct subunits. On the other hand, many receptors have been shown to activate different G proteins, thereby regulating diverse signal transduction pathways.
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  • 8
    ISSN: 0992-7689
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract During solar flares and coronal mass ejections, nuclei and electrons accelerated to high energies are injected into interplanetary space. These accelerated particles can be detected at the SOHO satellite by the ERNE instrument. From the data produced by the instrument, it is possible to identify the particles and to calculate their energy and direction of propagation. Depending on variable coronal/interplanetary conditions, different kinds of effects on the energetic particle transport can be predicted. The problems of interest include, for example, the effects of particle properties (mass, charge, energy, and propagation direction) on the particle transport, the particle energy changes in the transport process, and the effects the energetic particles have on the solar-wind plasma. The evolution of the distribution function of the energetic particles can be measured with ERNE to a better accuracy than ever before. This gives us the opportunity to contribute significantly to the modeling of interplanetary transport and acceleration. Once the acceleration/transport bias has been removed, the acceleration-site abundance of elements and their isotopes can be studied in detail and compared with spectroscopic observations.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 763 (1995), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Ground water 38 (2000), S. 0 
    ISSN: 1745-6584
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Geosciences
    Notes: Electromagnetic surveys of a young, wholly sedimentary, strip barrier island (St. George Island) on Florida's Gulf Coast reveal a Dupuit-Ghyben-Herzberg fresh water lens with the thickest part located close to the ocean side of the island at both undeveloped and developed sites. This result is at odds with those obtained on other barrier beaches, where the lens is either approximately symmetric or skewed toward the lagoon side due to higher sea level and greater upper beach storage on the ocean side. The inferred morphology of the fresh water lens on St. George Island can be attributed to variations in hydrogeologic (e.g., hydraulic conductivity, presence of semipermeable confining layer) and/or boundary conditions (e.g., recharge, higher sea level on the lagoon side), but the effects of variations in these factors on the shape of the lens are not separable. We therefore use independent constraints on hydraulic conductivity (from tidal pumping analyses), hydrofacies distribution, and recharge patterns to assess the plausibility that lateral variations in various physical parameters produce the observed lens shape. Dune ridge topography, which may constitute a significant portion of the width of a narrow island, perturbs recharge and shallow ground water flow patterns and may contribute to the development of a thick fresh water lens on an island's ocean side. However, topographic variations alone cannot account for the anomalous form of the island's fresh water lens.
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