carbonic anhydrase/únava

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Effect of carbonic anhydrase III inhibition on substrate utilization and fatigue in rat soleus.

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Přihlášení Registrace

Carbonic anhydrase III (CA III; EC 4.2.1.1) is the most abundant cytosolic enzyme in type I skeletal muscle fibers. We have previously shown that inhibiting the CA III activity of type I muscle can influence fatigability. Our goal was to test the hypothesis that the influence on fatigability of CA

Carbonic Anhydrase III Is Expressed in Mouse Skeletal Muscles Independent of Fiber Type-Specific Myofilament Protein Isoforms and Plays a Role in Fatigue Resistance.

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Přihlášení Registrace

Carbonic anhydrase III (CAIII) is a metabolic enzyme and a regulator for intracellular pH. CAIII has been reported with high level expression in slow twitch skeletal muscles. Here we demonstrate that CAIII is expressed in multiple slow and fast twitch muscles of adult mouse independent of the

Fatigue and recovery of rat soleus muscle are influenced by inhibition of an intracellular carbonic anhydrase isoform.

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Přihlášení Registrace

Carbonic anhydrase III (CA III; EC 4.2.1.1) is the most abundant cytosolic enzyme in type I skeletal muscle fibers. Methazolamide, a specific CA inhibitor, was used to characterize the effects of inhibiting CA III on the resistance to fatigue and recovery of the rat soleus muscle using a 60-min

Reduced Expression of Carbonic Anhydrase III in Skeletal Muscles Could Be Linked to Muscle Fatigue: A Rat Muscle Fatigue Model

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Přihlášení Registrace

Background: Carbonic anhydrase III (CAIII) is expressed abundantly in slow skeletal muscles, adipocytes, and the liver. It plays a critical role in maintaining intracellular pH, antioxidation, and energy metabolism, which are further involved in fatigue. However,

Carbonic anhydrase III: the new hope for the elimination of exercise-induced muscle fatigue.

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Přihlášení Registrace

Fatigue, defined as the failure to maintain the required or expected power output, is a complex problem. Its occurrence mechanism is extremely complicated. The obvious reasons are that it is a multifactorial situation and that the limiting factors may vary with force intensity, exercise duration and

A quantitative study of bioenergetics in skeletal muscle lacking carbonic anhydrase III using 31P magnetic resonance spectroscopy.

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Přihlášení Registrace

Oxidative slow skeletal muscle contains carbonic anhydrase III in high concentration, but its primary function remains unknown. To determine whether its lack handicaps energy metabolism and/or acid elimination, we measured the intracellular pH and energy phosphates by (31)P magnetic resonance

The influence of supplemental sodium acetate on carbonic anhydrase inhibitor-induced side effects.

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A double-masked, randomly assigned, crossover trial of the effect of supplemental two-weak courses of sodium acetate (90 mEq/day) and placebo on carbonic anhydrase inhibitor (CAI)-induced side effects of malaise, fatigue, and others ("malaise symptom complex") was performed in 28 patients. Fifteen

Effect of acetazolamide and methazolamide on diaphragm and dorsiflexor fatigue: a randomized controlled trial.

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Přihlášení Registrace

Acetazolamide, a carbonic anhydrase (CA) inhibitor used clinically and to prevent acute mountain sickness, worsens skeletal muscle fatigue in animals and humans. In animals, methazolamide, a methylated analog of acetazolamide and an equally potent CA inhibitor, reportedly exacerbates fatigue less

Transgenic Expression of Carbonic Anhydrase III in Cardiac Muscle Demonstrates A Mechanism to Tolerate Acidosis.

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Přihlášení Registrace

Carbonic anhydrase III (CAIII) is abundant in liver, adipocytes, skeletal muscles, but not heart. A cytosolic enzyme that catalyzes conversions between CO₂and HCO₃^-in the regulation of intracellular pH, its physiological role in myocytes is not fully understood.

Expression and purification of TAT-fused carbonic anhydrase III and its effect on C2C12 cell apoptosis induced by hypoxia/reoxygenation.

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Přihlášení Registrace

BACKGROUND Carbonic anhydrase III (CAIII) is remarkably abundant in slow skeletal muscles. It has multiple biological activities which could dissipate or resist some fatigue-related substances. In this study, we purified trans-activating transcriptional activator (TAT) fused CAIII protein and

Metabolic and contractile influence of carbonic anhydrase III in skeletal muscle is age dependent.

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Přihlášení Registrace

Carbonic anhydrase (CA) III is very abundant in type I skeletal muscle, but its function is still debated. Our aims were to examine CA III expression during growth and determine whether the effects of CA inhibition previously observed in adult muscles could be seen in younger rats in which CA III

Carbonic anhydrase inhibitor side effects. Serum chemical analysis.

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Přihlášení Registrace

Multiple serum chemical values were examined in 92 patients with chronic glaucoma who were treated with the carbonic anhydrase inhibitors (CAIs) acetazolamide or methazolamide, seeking relationships between serum composition and symptomatic side effects. Of the 92 patients, 44 complained of a

Forearm muscle metabolism studied using (31)P-MRS during progressive exercise to fatigue after Acz administration.

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Přihlášení Registrace

The effects of acetazolamide (Acz)-induced carbonic anhydrase inhibition (CAI) on muscle intracellular thresholds (T) for intracellular pH (pH(i)) and inorganic phosphate-to-phosphate creatine ratio (P(i)/PCr) and the plasma lactate (La(-)) threshold were examined in nine adult male subjects

Carbohydrate utilization in rat soleus muscle is influenced by carbonic anhydrase III activity.

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Přihlášení Registrace

Inhibition of carbonic anhydrase III (CA III; EC 4.2.1.1) activity in type I muscle can influence resistance to fatigue and glycogen utilization. Our aim was to determine if CA III inhibition could influence muscle pH and glycolytic rate. Muscle pH, hexosemonophosphates (HMP), glycolytic

Expression of carbonic anhydrase III and skeletal muscle remodeling following selective denervation.

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Přihlášení Registrace

Carbonic anhydrase III (CAIII) is expressed selectively in type I (slow‑twitch) myofibers. To investigate the association between changes in the expression of CAIII and skeletal muscle structure following denervation, the present study stained adjacent sections of skeletal muscle for ATPase and

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