Effect of Sympathectomy and Vagotomy on Carbonic Anhydrase Activity, Oxidative Phosphorylation, High Energy Phosphates Content and Electrolytes Content of the Gastric Mucosa

1958 ◽  
Vol 192 (3) ◽  
pp. 476-478 ◽  
Author(s):  
Takeshi Yakushiji ◽  
Tetsuya Kikuchi ◽  
Junichi Yamamoto ◽  
Kaname Kuriaki
Keyword(s):  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Oxidative Phosphorylation ◽  
High Energy ◽  
Carbonic Anhydrase Activity ◽  
High Energy Phosphates

Sympathectomy enhanced carbonic anhydrase activity, increased the rate of oxidative phosphorylation and the ATP and potassium contents of the canine gastric mucosa. Vagotomy was essentially without effect.

scholarly journals Impaired Cerebral Mitochondrial Oxidative Phosphorylation Function in a Rat Model of Ventricular Fibrillation and Cardiopulmonary Resuscitation

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Jun Jiang ◽  
Xiangshao Fang ◽  
Yue Fu ◽  
Wen Xu ◽  
Longyuan Jiang ◽  
...  
Keyword(s):  
Cardiac Arrest ◽  
Ventricular Fibrillation ◽  
Cardiopulmonary Resuscitation ◽  
Oxidative Phosphorylation ◽  
Mitochondrial Dysfunction ◽  
Rat Model ◽  
Mitochondrial Function ◽  
High Energy ◽  
Mitochondrial Morphology ◽  
High Energy Phosphates

Postcardiac arrest brain injury significantly contributes to mortality and morbidity in patients suffering from cardiac arrest (CA). Evidence that shows that mitochondrial dysfunction appears to be a key factor in tissue damage after ischemia/reperfusion is accumulating. However, limited data are available regarding the cerebral mitochondrial dysfunction during CA and cardiopulmonary resuscitation (CPR) and its relationship to the alterations of high-energy phosphate. Here, we sought to identify alterations of mitochondrial morphology and oxidative phosphorylation function as well as high-energy phosphates during CA and CPR in a rat model of ventricular fibrillation (VF). We found that impairment of mitochondrial respiration and partial depletion of adenosine triphosphate (ATP) and phosphocreatine (PCr) developed in the cerebral cortex and hippocampus following a prolonged cardiac arrest. Optimal CPR might ameliorate the deranged phosphorus metabolism and preserve mitochondrial function. No obvious ultrastructural abnormalities of mitochondria have been found during CA. We conclude that CA causes cerebral mitochondrial dysfunction along with decay of high-energy phosphates, which would be mitigated with CPR. This study may broaden our understanding of the pathogenic processes underlying global cerebral ischemic injury and provide a potential therapeutic strategy that aimed at preserving cerebral mitochondrial function during CA.

scholarly journals Carbonic anhydrase, ultrastructural localization in the mouse gastric mucosa and improvements in the technique.

1980 ◽  
Vol 28 (6) ◽  
pp. 511-525 ◽  
Author(s):  
N Sugai ◽  
S Ito
Keyword(s):  
Electron Microscopy ◽  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Picric Acid ◽  
Ultrastructural Localization ◽  
Carbonic Anhydrase Activity ◽  
Cobalt Sulfide ◽  
Ultrastructural Studies ◽  
Mucosal Cells ◽  
Erythrocyte Carbonic Anhydrase

The ultrastructural localization of carbonic anhydrase activity in mouse gastric mucosal cells as revealed by the cobalt bicarbonate histochemical method of Hansson has been made. In addition the effects of fixatives used for ultrastructural studies have been evaluated for reduction of carbonic anhydrase activity; exogenous erythrocyte carbonic anhydrase has been localized in tissues; acetazolamide and potassium cyanate inhibition of activity demonstrated; and an improved method for the osmication of reacted tissues for electron microscopy has been developed. The results indicate that the glutaraldehyde, formaldehyde, picric acid fixative, which retains about 5% of the original carbonic anhydrase activity, is distinctly better for histochemical studies than formaldehyde fixation, which retains about 32% activity. Acetazolamide at 10(-5) M consistently inhibits histochemical reaction, as does 20 mM KCNO, in the incubation medium. Exogenous carbonic anhydrase is readily visualized by the histochemical technique. Electron microscopy of gastric mucosa reacted for carbonic anhydrase activity indicates the focal deposition of the cobalt sulfide reaction product in the cores of microvilli lining the intracellular canaliculi, in the basal and lateral cell folds of parietal cells, and in the microvilli as well as the cytoplasm between mucous granules in the surface mucous cells. In addition, some reaction product was found in the mitochondrial cristae and in some nuclei and intercellular spaces.

Cyclooxygenase-2 selective inhibition meloxicam-induced is correlated with gastric mucosa carbonic anhydrase activity

2000 ◽  
Vol 118 (4) ◽  
pp. A1296-A1297
Author(s):  
Ioan Puscas ◽  
Adrian Maghiar ◽  
Marcela Coltau ◽  
Teodor Maghiar ◽  
Ioan I. Puscas ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Selective Inhibition ◽  
Carbonic Anhydrase Activity ◽  
Cyclooxygenase 2

Cellular localization of gastric intrinsic factor in the rat

1964 ◽  
Vol 206 (4) ◽  
pp. 783-786 ◽  
Author(s):  
Agna Boass ◽  
T. Hastings Wilson
Keyword(s):  
Gastric Mucosa ◽  
Carbonic Anhydrase ◽  
Cellular Localization ◽  
Tumor Tissue ◽  
Intrinsic Factor ◽  
Close Correlation ◽  
Carbonic Anhydrase Activity ◽  
Frozen Sections ◽  
Gastric Glands ◽  
Rat Gastric Mucosa

The distribution of carbonic anhydrase, pepsinogen, and intrinsic factor (IF) was studied in frozen sections of rat gastric mucosa using the method of Holter and Linderstrøm-Lang. Carbonic anhydrase activity was greatest in the sections nearest to the surface of the mucosa and less in the deeper regions of the glands. In contrast, the levels of both IF and pepsinogen were low at the surface and continued to increase to a maximum at the base of the gastric glands. The close correlation between the distribution of the concentrations of pepsinogen and IF suggests that the chief (zymogenic) cell may be the source of IF in the stomach of the rat. No IF was detected in human carcinoid tumor tissue. This absence of IF is consistent with the view that the argentaffine cell is not the source of IF.

Relation among regional O2 consumption, high-energy phosphates, and substrate uptake in porcine right ventricle

1994 ◽  
Vol 266 (2) ◽  
pp. H521-H530 ◽  
Author(s):  
G. G. Schwartz ◽  
C. R. Greyson ◽  
J. A. Wisneski ◽  
J. Garcia ◽  
S. Steinman
Keyword(s):  
Oxidative Phosphorylation ◽  
Myocardial Oxygen Consumption ◽  
High Energy ◽  
Substrate Uptake ◽  
High Energy Phosphates ◽  
The Right ◽  
Pulmonary Artery Constriction ◽  
Isoproterenol Infusion ◽  
Alternative Stimulus

Changes in phosphate metabolites may play a role in the regulation of myocardial oxidative phosphorylation in vivo. We tested the hypothesis that changes in phosphate metabolites with increased myocardial oxygen consumption (MVO2) depend on the mechanism by which MVO2 is increased. In 17 open-chest pigs, regional MVO2 of the right ventricular (RV) free wall was increased from control by isoproterenol infusion (Iso) and by pulmonary artery constriction (PAC). The phosphocreatine-to-ATP ratio (PCr/ATP), which is inversely related to free ADP concentration ([ADP]), was determined by 31P-nuclear magnetic resonance (NMR) spectroscopy. Regional MVO2 and lactate, glucose, and free fatty acid (FFA) uptake were determined in the myocardium directly beneath the NMR coil. Iso and PAC increased MVO2 nearly equally, to approximately twice control, but produced directionally opposite changes in PCr/ATP: a significant decrease with PAC (control 1.52 +/- 0.06, PAC 1.35 +/- 0.06, means +/- SE) but a significant increase with Iso (to 1.72 +/- 0.07). Thus increased [ADP] may have stimulated oxidative phosphorylation during PAC but could not have done so during Iso. With Iso, uptake of FFA was more than three times that with PAC, and the sum of the oxygen extraction ratios for lactate, glucose, and FFA was more than double that with PAC. Enhanced substrate uptake during Iso may have increased mitochondrial NADH, which in turn may have provided an alternative stimulus to the rate of oxidative phosphorylation. These results support multifactorial control of RV oxidative phosphorylation in vivo.

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