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1.
Actas Urol Esp ; 29(7): 708-10, 2005.
Article in Spanish | MEDLINE | ID: mdl-16180324

ABSTRACT

High-flow priapism is an infrequent pathology in Urology, specially long-term cases as the one we present. Literature is scarce and both diagnostic methods and treatment have remained unchanged for many years We present a high flow priapism case that has lasted for 30 years, but which is well tolerated and even desired by the "patient". Furthermore, we propose a new diagnostic algorithm and treatment.


Subject(s)
Priapism/diagnosis , Adult , Blood Flow Velocity , Humans , Magnetic Resonance Angiography , Male , Penis/physiopathology , Priapism/physiopathology , Treatment Outcome
2.
Actas urol. esp ; 29(7): 708-710, jul.-ago. 2005. ilus
Article in Es | IBECS | ID: ibc-039317

ABSTRACT

El priapismo de alto flujo representa una patología infrecuente en el campo de la urología y mucho más los casos de larga evolución como el que presentamos. La bibliografía es escasa y los métodos de diagnóstico y tratamiento no han evolucionado en muchos años. Presentamos un caso de priapismo de alto flujo de 30 años de evolución, bien tolerado, y hasta deseado por el “paciente” y proponemos un nuevo algoritmo de diagnóstico y tratamiento (AU)


High-flow priapism is an infrequent pathology in Urology, specially long term cases as the one we present. Literature is scarce and both diagnostic methods and treatment have remained unchanged for many years. We present a high flow priapism case that has lasted for 30 years, but which is well tolerated and even desired by the “patient”. Furthermore, we propose a new diagnostic algorithm and treatment (AU)


Subject(s)
Male , Adult , Humans , Priapism/physiopathology , Priapism/classification , Priapism/etiology , Magnetic Resonance Imaging , Circumcision, Male/adverse effects
3.
Am J Physiol Cell Physiol ; 278(1): C17-25, 2000 Jan.
Article in English | MEDLINE | ID: mdl-10644507

ABSTRACT

Some amphipathic bitter tastants and non-sugar sweeteners are direct activators of G proteins and stimulate transduction pathways in cells not related to taste. We demonstrate that the amphipathic bitter tastants quinine and cyclo(Leu-Trp) and the non-sugar sweetener saccharin translocate rapidly through multilamellar liposomes. Furthermore, when rat circumvallate (CV) taste buds were incubated with the above tastants for 30 s, their intracellular concentrations increased by 3.5- to 7-fold relative to their extracellular concentrations. The time course of this dramatic accumulation was also monitored in situ in rat single CV taste buds under a confocal laser-scanning microscope. Tastants were clearly localized to the taste cell cytosol. It is proposed that, due to their rapid permeation into taste cells, these amphipathic tastants may be available for activation of signal transduction components (e. g., G proteins) directly within the time course of taste sensation. Such activation may occur in addition to the action of these tastants on putative G protein-coupled receptors. This phenomenon may be related to the slow taste onset and lingering aftertaste typically produced by many bitter tastants and non-sugar sweeteners.


Subject(s)
Chemoreceptor Cells/physiology , Liposomes/metabolism , Signal Transduction/physiology , Taste/physiology , Animals , Antimalarials/pharmacokinetics , Biological Transport/physiology , Diffusion , Epithelial Cells/metabolism , Fluorescent Dyes , GTP-Binding Proteins/metabolism , Male , Membrane Proteins/metabolism , Piperazines/pharmacokinetics , Quinine/pharmacokinetics , Rats , Rats, Sprague-Dawley , Receptors, Cell Surface , Saccharin/pharmacokinetics
4.
J Dairy Sci ; 76(3): 742-51, 1993 Mar.
Article in English | MEDLINE | ID: mdl-8463486

ABSTRACT

Fifteen Holstein heifers that were 175 +/- 4.0 d old and at BW of 175 +/- 4.9 kg were used to determine the effect of three feeding regimens from 6 to 12 mo of age on growth, blood concentration of several hormones, and milk production during first lactation. The feeding regimens consisted of two periods, the first lasting for 4 mo and the other for the subsequent 2 mo. For group A (restricted) heifers, the diet during period 1 was restricted to 85% of NRC (1988) recommendations (a daily BW gain of .7 kg); during period 2, a high energy, high protein diet was provided for ad libitum intake. Group B (control) heifers received a diet that corresponded to 100 and 90% of the NRC (1988) recommendations in periods 1 and 2, respectively. Group C (ad libitum) intake heifers received a high energy, high protein diet throughout both periods. Daily BW gains of heifers of groups A, B, and C were, respectively, .625, .768, and 1.100 kg for period 1 and 1.162, .705, and .797 kg for period 2. The different feeding regimens influenced the age at which the heifers achieved puberty but did not affect BW at puberty. Milk production during 250 d of lactation was 7056, 6070, and 5975 kg for groups A, B, and C, respectively. A statistical model that included serum derived mitogenic activity and serum prolactin of period 2 accounted for 63% of the difference in milk production at first lactation.


Subject(s)
Cattle/physiology , Diet , Hormones/blood , Lactation , Animal Feed , Animals , Cattle/blood , Energy Intake , Female , Weight Gain
5.
Cell Biol Int Rep ; 16(4): 359-68, 1992 Apr.
Article in English | MEDLINE | ID: mdl-1525835

ABSTRACT

Insulin-like growth factors (IGFs) I and II (IGF-I, IGF-II) and Des-3-IGF-I at physiological concentrations are potent mitogens of bovine undifferentiated mammary epithelial cells cultured in collagen in a serum-free medium. Des-3-IGF-I was found to be as potent as IGF-I, while IGF-II was significantly less active. All three factors acted either synergistically or additively with epidermal growth factor (EGF), cholera toxin and fetal calf serum (FCS). Indirect evidence indicates that despite its lower mitogenic activity the action of IGF-II is mediated through IGF-I receptors. The galactopoietic activity of Des-3-IGF-I and IGF-II was studied in an organ culture of bovine lactating mammary glands using lactogen-responsive fat synthesis as a test. Neither Des-3-IGF-I nor IGF-II exhibited galactopoietic activity nor did they affect the galactopoietic activity of prolactin.


Subject(s)
DNA/biosynthesis , Lipids/biosynthesis , Mammary Glands, Animal/drug effects , Somatomedins/pharmacology , Animals , Cattle , Cells, Cultured , Cholera Toxin/pharmacology , Female , Insulin-Like Growth Factor I/pharmacology , Insulin-Like Growth Factor II/pharmacology , Lactation , Mammary Glands, Animal/cytology , Mammary Glands, Animal/metabolism , Organ Culture Techniques , Peptide Fragments/pharmacology , Prolactin/pharmacology
6.
Arch Biochem Biophys ; 278(1): 106-12, 1990 Apr.
Article in English | MEDLINE | ID: mdl-2321951

ABSTRACT

The synthesis and uptake of intracellular organic osmolytes (compatible solutes) were studied with the aid of natural abundance 13C NMR spectroscopy in two unrelated, moderately halophilic eubacteria: Ba1 and Vibrio costicola. In minimal media containing 1 M NaCl, both microorganisms synthesized the cyclic amino acid, 1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid (trivial name, ectoine) as the predominant compatible solute, provided that no glycine betaine was present in the growth medium. When, however, the minimal medium was supplemented with glycine betaine or the latter was a component of a complex medium, it was transported into the cells and the accumulating glycine betaine replaced the ectoine. In Ba1, grown in a defined medium containing glucose as the single carbon source, ectoine could only be detected if the NaCl concentration in the medium was higher than 0.6 M; the ectoine content increased with the external salt concentration. At NaCl concentrations below 0.6 M, alpha,alpha-trehalose was the major organic osmolyte. The concentration of ectoine reached its peak during the exponential phase and declined subsequently. In contrast, the accumulation of glycine betaine continued during the stationary phase. The results presented here indicate that, at least in the two microorganisms studied, ectoine plays an important role in haloadaptation.


Subject(s)
Eubacterium/metabolism , Vibrio/metabolism , Carbon Isotopes , Culture Media , Eubacterium/drug effects , Eubacterium/growth & development , Magnetic Resonance Spectroscopy/methods , Sodium Chloride/pharmacology , Solutions , Vibrio/drug effects , Vibrio/growth & development
7.
Lipids ; 11(8): 604-9, 1976 Aug.
Article in English | MEDLINE | ID: mdl-9555

ABSTRACT

Some properties of the pure, soluble phospholipase D (phosphatidycholine phosphatido hydrolase, EC 3.1.4.4) interactions with phosphatidyl choline (1,2 diacyl-sn-glycerol-3-phosphoryl choline) in a system also containing dodecylsulfate and Ca2+ ions were studied. Concentrations of Ca2+ greater than 50 mM were necessary both for activity and adsorption of the enzyme to the "supersubstrate." Ethylenediamine tetraacetic acid caused inhibition of activity, greater than one would expect from its chelating capacity. A nonlinear increase in activity with the increase of enzyme protein was observed, suggesting a subunit aggregation into a higher mol wt protein, catalytically more active. Upon centrifugation of the supersubstrate-enzyme complex at 4.5 X 10(5) g-min at 30 C, most of the substrate molecules sedimented regardless of the pH. The reverse was true when centrifugation was done at 1 C. Phospholipase D hydrolyzed phosphatidylcholine molecules present in the supersubstrate at temperatures around 0 C at a rate 1/5 that of a maximal value measured at 30 C. The Arrhenius plot was linear in the range from 0 to 30 C, and at that temperature the curve broke with a smaller slope. Activation energy of 9.1 Kcal/mol, below 30 C, was calculated. Adsorption of the enzyme to the sedimentable supersubstrate occurred at pH 8.0, regardless of temperature. At pH 5.6, a considerable portion of phosphatidylcholine was degraded at 30 C, thus minimizing the capacity of the supersubstrate to adsorb the enzyme. Although Mg2+ could replace Ca2+ in the formation of sedimentable supersubstrate, it neither assists in adsorption of the enzyme nor in activation of the phosphatidylcholine hydrolysis.


Subject(s)
Calcium , Phospholipases , Sodium Dodecyl Sulfate , Binding Sites , Calcium/pharmacology , Hydrogen-Ion Concentration , Kinetics , Lanthanum/pharmacology , Magnesium/pharmacology , Manganese/pharmacology , Phospholipases/metabolism , Protein Binding
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