Acid Stimulation (acid + stimulation)

Distribution by Scientific Domains


Selected Abstracts


Forearm and leg amino acid metabolism in the basal state and during combined insulin and amino acid stimulation after a 3-day fast

ACTA PHYSIOLOGICA, Issue 3 2009
J. Gjedsted
Abstract Aim:, Fasting is characterized by a progressive loss of protein, but data on protein kinetics are unclear and few have studied the effects of re-feeding. The present study was designed to test the hypothesis that a combined infusion of insulin and amino acids after fasting would induce compensatory increases in protein synthesis and reductions in protein breakdown at the whole body level and in muscle. Methods:, We included 10 healthy male volunteers and studied them twice: (1) in the post-absorptive state and (2) after 72 h of fasting. Amino acid kinetics was measured using labelled phenylalanine and tyrosine, whole body energy expenditure was assessed and urea nitrogen synthesis rates were calculated. Results:, After fasting we observed an increase in arterial blood concentration of branched chain amino acids and a decrease in gluconeogenic amino acids (P < 0.05). Isotopically determined whole body, forearm and leg phenylalanine fluxes were unaltered apart from a 30% decrease in phenylalanine-to-tyrosine conversion (2.0 vs. 1.4 ,mol kg,1 h,1, P < 0.01). During infusion of insulin and amino acids, amino acid concentrations increased. Conclusion:, Our data indicate that after a 72-h fast basal and insulin/amino acid-stimulated regional phenylalanine fluxes in leg and forearm muscle are unaltered. During fasting concentrations of gluconeogenic amino acids decrease and hepatic and/or renal phenylalanine-to-tyrosine conversion decreases. Thus, as opposed to glucose and lipid metabolism, fasting does not induce insulin resistance as regards amino acid metabolism. [source]


Salivary simulation with ascorbic acid enhances sonographic diagnosis of obstructive sialadenitis

JOURNAL OF CLINICAL ULTRASOUND, Issue 6 2009
Alessandro Bozzato MD
Abstract Purpose. High-frequency ultrasound (US) is routinely used to evaluate various diseases of the salivary glands. Normally, the duct network of the submandibular and parotid glands is not visible during US assessment. In obstructive sialadenitis of the parotid and submandibular glands, localization of the obstacle is often difficult. Methods. In a case-control study, the sonographic visibility of the duct before and after stimulation with oral ascorbic acid (vitamin C) was compared with sialendoscopy as the gold standard. Twenty male and 23 female patients suffering from salivary gland diseases were included in this study and compared with 25 healthy volunteers. US examination of the parotid and submandibular glands was performed before and after oral ascorbic acid stimulation. Changes in visibility of the main excretory duct were recorded and US diagnoses were compared with results of sialendoscopy. Results. In 7 of 25 controls, the main duct became partially visible after stimulation. In the group of 43 patients, the main duct was depicted before stimulation in 27 patients (63%). After ascorbic acid stimulation, the main duct became visible in 41 patients (95%). Grading the stimulated duct dilation by measuring diameters at different points revealed no correlation with the underlying type of pathology. Conclusions. Application of ascorbic acid prior to diagnostic US examination facilitates the sonographic evaluation of obstructive salivary gland diseases. © 2009 Wiley Periodicals, Inc. J Clin Ultrasound 2009 [source]


Two-scale continuum model for simulation of wormholes in carbonate acidization

AICHE JOURNAL, Issue 12 2005
Mohan K. R. Panga
Abstract A two-scale continuum model is developed to describe transport and reaction mechanisms in reactive dissolution of a porous medium, and used to study wormhole formation during acid stimulation of carbonate cores. The model accounts for pore level physics by coupling local pore-scale phenomena to macroscopic variables (Darcy velocity, pressure and reactant cup-mixing concentration) through structure-property relationships (permeability-porosity, average pore size-porosity, and so on), and the dependence of mass transfer and dispersion coefficients on evolving pore scale variables (average pore size and local Reynolds and Schmidt numbers). The gradients in concentration at the pore level caused by flow, species diffusion and chemical reaction are described using two concentration variables and a local mass-transfer coefficient. Numerical simulations of the model on a two-dimensional (2-D) domain show that the model captures the different types of dissolution patterns observed in the experiments. A qualitative criterion for wormhole formation is developed and it is given by , , O(1), where , = . Here, keff is the effective volumetric dissolution rate constant, DeT is the transverse dispersion coefficient, and uo is the injection velocity. The model is used to examine the influence of the level of dispersion, the heterogeneities present in the core, reaction kinetics and mass transfer on wormhole formation. The model predictions are favorably compared to laboratory data. © 2005 American Institute of Chemical Engineers AIChE J, 2005 [source]


THE EPITHELIAL BRUSH BORDER Na+/H+ EXCHANGER NHE3 ASSOCIATES WITH THE ACTIN CYTOSKELETON BY BINDING TO EZRIN DIRECTLY AND VIA PDZ DOMAIN-CONTAINING Na+/H+ EXCHANGER REGULATORY FACTOR (NHERF) PROTEINS

CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY, Issue 8 2008
Boyoung Cha
SUMMARY 1The Na+/H+ exchanger NHE3 associates with the actin cytoskeleton by binding ezrin both directly and indirectly. Both types of interaction are necessary for acute regulation of NHE3. Most acute regulation of NHE3 occurs by changes in trafficking via effects on exocytosis and/or endocytosis. However, NHE3 activity can also be regulated without changing the surface expression of NHE3 (change in turnover number). 2A positive amino acid cluster in the a-helical juxtamembrane region in the COOH-terminus of NHE3 (amino acids K516, R520 and R527) is necessary for binding to the protein 4.1, ezrin, radixin, moesin (FERM) domain III of ezrin. Direct binding of NHE3 to ezrin is necessary for many aspects of basal trafficking, including basal exocytosis, delivery from the synthetic pathway and movement of NHE3 in the brush border (BB), which probably contributes to endocytosis over a prolonged period of time. 3In addition, NHE3 binds indirectly to ezrin. The PDZ domain-containing proteins Na+/H+ exchanger regulatory factor (NHERF) 1 and NHERF2, as intermediates in linking NHE3 to ezrin, are necessary for many aspects of NHE3 regulation. The binding of NHERF,ezrin/radixin/moesin to NHE3 occurs in the cytosolic domain of NHE3 between amino acids 475 and 689. This NHERF binding is involved in the formation of the NHE3 complex and restricts NHE3 mobility in the BB. However, it is dynamic; for example, changing in some cases of signalling. Furthermore, NHERF binding is necessary for lysophosphatidic acid stimulation of NHE3 and inhibition of NHE3 by Ca2+, cAMP and cGMP. [source]