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  • 11
    Electronic Resource
    Electronic Resource
    Decreased vasopressin content in brain stem of rats with spontaneous hypertension (1980)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 315 (1980), S. 83-84 
    Details
    ISSN: 1432-1912
    Keywords: Arginine vasopressin ; Brain stem ; Hypertensive rats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The content of arginine vasopressin in the brain stem and neurohypophysis of adult spontaneously hypertensive rats was measured by radioimmunoassay and the values were compared to those measured in normotensive Wistar-Kyoto rats. In the brain stem of hypertensive rats, AVP content was decreased by 77% while neurohypophyseal AVP content was increased by 26%. The results demonstrate that brain stem AVP levels and neurohypophyseal AVP levels may change differentially and they are consistent with the possibility that brain stem AVP may be involved in altering cardiovascular reflex activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504234
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  • 12
    Electronic Resource
    Electronic Resource
    Effects of the renin inhibitor pepstatin on the blood pressure on intact and nephrectomized rats (1972)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 275 (1972), S. 114-118 
    Details
    ISSN: 1432-1912
    Keywords: Pepstatin ; Renin-Angiotensin System ; Nephrectomy ; Proteinase Inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Pepstatin, an N-acylated pentapeptide isolated from culture filtrates of streptomycetes, has been shown in previous experiments to inhibit the reninsubstrate reaction in vitro. On the basis of blood-pressure measurements in the rat it is suggested that pepstatin affects the reaction of both endogenous and exogenous heterologous renin with plasma substrate. Besides this effect, pepstatin has a slight non-specific hypotensive action, as demonstrated in the nephrectomized rat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00505072
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  • 13
    Electronic Resource
    Electronic Resource
    Serum arginine-vasotocin (AVT) and afferent and central control of osmoregulation in conscious Pekin ducks (1980)
    Springer
    Pflügers Archiv 387 (1980), S. 99-106 
    Details
    ISSN: 1432-2013
    Keywords: Avian ADH ; Avian osmoregulation ; Cerebral osmosensitivity ; Hypothalamic temperature ; Vagal afferents
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In conscious Pekin ducks adapted either to fresh water or to hypertonic saline (1.9%) as drinking fluid, urinary excretion, salt gland secretion and the serum concentration of radioimmunoassayable arginine-vasotocin (AVT) were examined with regard to their afferent and central control. The experiments were carried out under conditions of water diuresis, osmotic diuresis or supraorbital salt gland secretion, which were induced by continuous infusions of appropriate solutions. Temporary bilateral vagus blockade caused rises in AVT serum concentration accompanied by antidiuresis in hydrated ducks and by inhibition of salt gland secretion in salt-stressed ducks. Rostral brainstem cooling caused decreases of AVT serum concentration and water diuresis in ducks under osmotic diuresis and reduction of AVT serum concentration and inhibition of salt gland secretion in saltstressed ducks. Cerebral osmotic stimulation in hydrated ducks by intracarotid injection or by intracerebroventricular microinfusion of hypertonic NaCl solutions caused antidiuretic reactions associated with rises of AVT serum concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00584259
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  • 14
    Electronic Resource
    Electronic Resource
    Radioimmunoassay for arginine-vasotocin (AVT) in serum of Pekin ducks: AVT concentrations after adaptation to fresh water and salt water (1980)
    Springer
    Pflügers Archiv 387 (1980), S. 91-97 
    Details
    ISSN: 1432-2013
    Keywords: Arginine-vasotocin ; Radioimmunoassay ; Avian osmoregulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A radioimmunoassay for arginine-vasotocin (AVT), the antidiuretic principle in birds, was developed using the high cross-reactivity of AVT with an AVP antiserum raised in rabbits. This assay is specific for the measurement of AVT in serum of birds. The sensitivity and precision is such that serum AVT concentrations above 0.5 fmol/ml can be measured quantitatively. A serum AVT concentration of 5.1±1.4 fmol/ml was found in normally hydrated, fresh water adapted ducks with a serum osmolality of 293.7±2.2 mosmol/kg. When the same animals were acutely hydrated, no or〈0.5 fmol/ml AVT was present at an osmolality of 289.9±2.4 mosmol/kg. In salt water adapted ducks with a serum osmolality of 333.0±7.6 mosmol/kg, a serum AVT of 22.7±3.0 fmol/ml was found. When fresh water adapted ducks were hydrated and infused with different doses of AVT, a linear relationship between serum AVT and the amount infused was obtained. During AVT infusions, serum osmolality and urine flow rate were negatively correlated and urine osmolality was positively correlated with serum AVT.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00584258
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  • 15
    Electronic Resource
    Electronic Resource
    Characterization of the diphtheria toxin-resistance system in Chinese hamster ovary cells (1979)
    Springer
    Somatic cell and molecular genetics 5 (1979), S. 453-468 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Variations in two general classes of diphtheria toxin-resistant mutants which may be selected from Chinese hamster ovary (CH0-K1) cells and the conditions for their selection are described. The resistance of class I mutants can be overcome with increasing concentrations of toxin. Their entire complement of EF-2 is susceptible to ADP-ribosylation by toxin. Class I includes those strains in which resistance resides at the level of the plasma membrane. The resistance of class II, translational, mutants cannot be overcome by high concentrations of toxin, as all, or a portion, of their EF-2 is insensitive to the action of diphtheria toxin and Pseudomonas exotoxin A. Adjustment of the concentration of toxin used to select resistant mutants can be used to regulate the class of mutant recovered. Metabolic cooperation between cells does not affect recovery of either class I or class II mutants. Resistance is stable in class I strains, but class IIb strains, which possess 50 % resistant and 50 % sensitive EF-2, display a transient high level of resistance which is retained for varying lengths of time following exposure to toxin. Class IIa strains, which possess 100% resistant EF-2, grow normally in saturating concentrations of toxin, but class IIb strains grow at a reduced rate. Evidence is presented which suggests that the gene for EF-2 is functionally diploid in CH0-K1 cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538880
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  • 16
    Electronic Resource
    Electronic Resource
    Codominant translational mutants of Chinese hamster ovary cells selected with diphtheria toxin (1979)
    Springer
    Somatic cell and molecular genetics 5 (1979), S. 469-480 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Diphtheria toxin-resistance markers in two translational mutants, CH-RE1.22c, possessing no toxin-sensitive EF-2 (class IIa), and CH-RE1.32, with 50% toxin-sensitive and 50% toxin-resistant EF-2 (class IIb), behaved codominantly in somatic cell hybrids. There was no complementation in hybrids formed between the two resistant mutants. The mutant parents and their hybrids, except those formed by fusion of CH-RE1.32 and wild-type cells, grew in the presence of toxin. To explain these results we suggest that CHO-K1 cells possess two functional copies of the gene for EF-2 and that CH-RE1.22c and CH-RE1.32 represent the homozygous (R/R) and heterozygous (R/S) states of resistance at the EF-2 gene locus. The failure of hybrids formed between CH-RE1.32 and wild-type cells to grow in toxin is a gene dosage effect. Codominant class IIa translational resistance is a selectable marker for the isolation of hybrids. It can be combined with a second, recessive, marker to provide a cell which is a “universal hybridizer” (10).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538881
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  • 17
    Electronic Resource
    Electronic Resource
    Zum extrahepatischen Stoffwechsel von Aldosteron (1968)
    Springer
    Clinical and experimental medicine 145 (1968), S. 270-277 
    Details
    ISSN: 1591-9528
    Keywords: Aldosterone ; Kidney ; Stop flow dog ; Aldosteron ; Niere ; Stop flow-Hund
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Mit Stop flow-Versuchen an Hunden konnten wir nach Infusion von 1,2-3H-18-Aldosteronglucuronid im Gegensatz zur Infusion von freiem 1,2-3H-Aldosteron keine proximale Sekretion von 1,2-3H-18-Aldosteronglucuronid nachweisen. Daraus kann geschlossen werden, daß in Hundenieren die proximalen Tubuluszellen wohl 18-Aldosteronglucuronid aus Aldosteron bilden und an das Tubuluslumen abgeben, während im Nierenarterienblut vorhandenes 18-Aldosteronglucuronid nur glomerulär filtriert und ausgeschieden wird.
    Notes: Summary In stop flow experiments during infusion of 1,2-3H-18-aldosterone glucuronide there was no proximal tubular secretion of this metabolite in contrary to experiments during infusion of 1,2-3H-aldosterone. The discrepancy must be explained by formation of 1,2-3H-aldosterone glucuronide out of3H-aldosterone in proximal tubular cells, while the 1,2-3H-18-aldosterone glucuronide in the plasma of the renal artery blood is only filtered in the glomerulum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02044618
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  • 18
    Electronic Resource
    Electronic Resource
    Zum extrahepatischen Stoffwechsel von Aldosteron (1968)
    Springer
    Clinical and experimental medicine 146 (1968), S. 329-335 
    Details
    ISSN: 1591-9528
    Keywords: Aldosterone ; Metabolism ; Protein-binding ; Renal clearance ; Aldosteron ; Stoffwechsel ; Eiwei\bindung ; Nierenclearance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Im menschlichen Blutplasma wurde vermittels äquilibriumDialyse die Eiwei\bindung für Tetrahydroaldosteronglucuronid mit 35–39% und diejenige für 18-Aldosteronglucuronid mit 54–57% bestimmt. Auf Grund dieser Werte und der früher mitgeteilten renalen Clearance dieser beiden Aldosteronmetaboliten, welche die Eiwei\bindung nicht berücksichtigte [13], ergibt sich für das Tetrahydroaldosteronglucuronid eine renale Clearance im Bereich derjenigen des Inulins und für das 18-Aldosteronglucuronid eine solche im Bereich der PAHClearance.
    Notes: Summary In equilibrium dialysis with human blood plasma and human albumin the protein binding of tetrahydroaldosterone glucuronide was 35 to 39% and the protein binding of 18-aldosterone glucuronide was 54 to 57%. The “uncorrected” renal clearance values of these two aldosterone metabolites, as published bySiegenthaler et al. [13], were “corrected” for protein binding. So the renal clearance of tetrahydroaldosterone glucuronide is similar to the renal clearance of inulin, whereas the renal clearance of 18-aldosterone glucuronide lies in the range of the PAH clearance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02045931
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  • 19
    Electronic Resource
    Electronic Resource
    Zum extrahepatischen Stoffwechsel von Aldosteron (1968)
    Springer
    Clinical and experimental medicine 146 (1968), S. 336-345 
    Details
    ISSN: 1591-9528
    Keywords: Aldosterone ; Kidney ; Man ; Aldosteron ; Niere ; Mensch
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Auf Grund eines Vergleiches der Verhältnisse von 1,2-3HTetrahydroaldosteronglucuronid zu 1,2-3H-18-Aldosteronglucuronid im Plasma von drei Normalpersonen und zwei nephrektomierten Patienten nach einer Injektion von 1,2-3H-Aldosteron haben wir folgende Schlüsse in Betracht gezogen: 1. Das im Blutplasma vorhandene 1,2-3H-18-Aldosteronglucuronid wird nur glomerular filtriert. 2. Die renale Clearance von 18-Aldosteronglucuronid, die etwa das Fünffache der Inulinclearance beträgt [13, 15], mu\ zu vier Fünfteln auf Bildung von 18-Aldosteronglucuronid durch die proximalen [15] Tubuluszellen zurückgeführt werden. 3. Das Ausma\ der renalen Bildung von 18-Aldosteronglucuronid liegt in einer Grö\enordnung von 80% der Gesamtmenge 18-Aldosteronglucuronid im 24 StdUrin.
    Notes: Summary After an intravenous injection of 1,2-3H-aldosterone the ratios of 1,23H-tetrahydroaldosterone glucuronide to 1,2-3H-aldosterone glucuronide in the blood plasma of three normal and two nephrectomized persons were compared. In the three normal persons the ratios were of the same magnitude as in the two nephrectomized persons. On the basis of glomerular filtration of tetrahydroaldosterone glucuronide, as previously demonstrated by renal clearance studies in man [13, 15] and stop flow experiments in dogs [6], we made the following deductions: 1. 18aldosterone glucuronide in blood plasma is only filtered in the glomerulum. 2. The renal clearance of 18-aldosterone glucuronide, as investigated during aldosterone infusion in man [13, 15], therefore must be explained by glomerular filtration of only one fifth and by formation of four fifth of 18-aldosterone glucuronide by proximal [15] tubular cells. 3. This means that about 80% of 18-aldosterone glucuronide excreted in urine is formed by the kidneys.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02045932
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