Effects of gastric acid stimulants and inhibitors on the activities of HCO3−-stimulated, Mg2+-dependent ATPase and carbonic anhydrase in rat gastric mucosa

Narumi, Shigehiko; Kanno, Morio

doi:10.1016/0005-2736(73)90256-3

Cited by 39 publications

(7 citation statements)

References 11 publications

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“…T h e carbonic anhydrase is present in the gastric mucosa at higher concentrations than in any other tissue (Maren 1967). Narumi and Kanno (1973) suggested a correlation between the stimulation of gastric acid seretion and the activity of the carbonic anhydrase, since subcutaneous administration of carbachol, tetragastrin or histamine increased both gastric secretion and carbonic anhydrase activity in rat gastric mucosa. Pretreatment with atropine or acetazolamide decreased this stimulation.…”

Section: Discussionmentioning

confidence: 99%

Distribution of carbonic anhydrase in cells and membranes isolated from pig gastric mucosa

Vega¹,

Olaisson²,

Mårdh³

1985

Acta Physiologica Scandinavica

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Mucosal cells were isolated from pig stomachs and then fractionated on linear density gradients of Percoll. Different types of cells were identified by their typical staining and morphology. In disrupted cell fractions, hydration of CO2 by carbonic anhydrase was measured by means of pH-stat technique. Localization of carbonic anhydrase to certain cell fractions was also studied by histochemical staining. Both parietal cells and carbonic anhydrase were confined to the low and intermediate density fractions of the gradients. Purified membranes from pig gastric mucosa, which contained the acid pump of the stomach, the H,K-ATPase, also contained a firmly bound carbonic anhydrase of high activity. The enzyme activity in the membranes was inhibited by acetazolamide, furosemide and KSCN. The molecular mass of the carbonic anhydrase was 33 kDA as estimated by its binding of [14C]furosemide followed by polyacrylamide gel electrophoresis. Previous suggestions of a role of carbonic anhydrase as a supplier of H+ in the secretion of acid are supported by its high activity and its localization to the same membrane as the acid pump of the stomach.

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Section: Discussionmentioning

confidence: 99%

Distribution of carbonic anhydrase in cells and membranes isolated from pig gastric mucosa

Vega¹,

Olaisson²,

Mårdh³

1985

Acta Physiologica Scandinavica

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“…So fand man eine Zunahme der Enzym-Aktivitit im Magen nach subkutaner Gabe von bekannten Sekretagoga wie Histamin, Carbachol und Tetragastrim Nach subkutaner Vorbehandlung mit Hemmstoffen der Siuresekretion wie Atropin und Acetazolamid (Diamox®) konnte die Zunahme der Enzymaktivit/it verhindert werden [22]. So fand man eine Zunahme der Enzym-Aktivitit im Magen nach subkutaner Gabe von bekannten Sekretagoga wie Histamin, Carbachol und Tetragastrim Nach subkutaner Vorbehandlung mit Hemmstoffen der Siuresekretion wie Atropin und Acetazolamid (Diamox®) konnte die Zunahme der Enzymaktivit/it verhindert werden [22].…”

Section: Ad B) Parallete ]Lnderungen Des" Transportes Und Der Enzymakunclassified

“…Entsprechende Untersuchungen tiber Aktivit/its-/inderungen der H C O 3 -A T P a s e und )~nderungen der Sekretion von H + / H C O 3 stehen noch in den Anf/ingen [22,51,52]. Der Grund hierffir liegt darin, dab der Nachweis des Transportenzyms in den Puffer-transportierenden Organen erst in den letzten Jahren gelungen ist.…”

Section: Pathophysiologie Des Puffertransportesunclassified

“…Diese Forderung ist ftir den Na+-Transport und die (Na+-K+)-ATPase weitgehend erffillt [4,10,18,31]. Nach den ersten vorliegenden Befunden ist dies auch ffir die HCO~-ATPase der Fall [22,51,52]. Im folgenden m6chten wir die bisher erhobenen Befunde fiber Vorkommen und Eigenschaften der HCO;--ATPase zusammenstellen und die pathophysiologische Relevanz dieses Transportenzyms ffir weitere Untersuchungen aufzeigen.…”

Section: Introductionunclassified

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Die Bedeutung der HCO 3 ? -ATPase in der H+/HCO 3 ? -Sekretion

Simon

Knauf

1976

Klin Wochenschr

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Active buffer transport, e.g. H+ -secretion by stomach and kidney and HCO3--secretion by pancreas and salivary glands, is linked with the presence of a HCO3-stimulated ATP-Phosphohydrolase. In contrast to (Na+ -k+)-ATPase which is considered to be equivalent to the Na+ pump, the HCO3--ATPase requires only one ion for activation and is insensitive to ouabain. The HCO3--ATPase is found in the plasma membrane of the epithelia, but in contrast to the (Na+ -k+)-ATPase it is located in the luminal cell border. The activity of the HCO3--ATPase changes in parallel along with the rate of active buffer transport, a finding which underlines its importance as a transport enzyme. Several disorders of buffer transport are described which are possibly associated with a defect of the HCO3--ATPase system.

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“…Endometrial carbonic anhydrase (CA) activity in nonpregnant rabbits can be increased by administration of gonadotropin (Lutwak-Mann, 1955). Injection of histamine, cyclic AMP, gastrin, or other gastric acid stimulants has been shown to increase the CA activity of rat stomach (Bersimbaev et al, 1971; Salganik et al, 1972;Narumi and Kanno, 1973). Narumi and Miyamqto (1974) showed activation in the presence of added protein kinase, ATP, Mg2+, and cyclic AMP of one of two isozymes prepared from commercial bovine erythrocyte CA.…”

mentioning

confidence: 99%

Stimulation of Carbonic Anhydrase Activity and Phosphorylation in Primary Astroglial Cultures by Norepinephrine

Church

Kimelberg

Sapirstein

1980

Journal of Neurochemistry

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The carbonic anhydrase activity of 3‐week‐old primary astroglial cultures started from the dissociated cerebral hemispheres of neonatal rats was increased up to twofold after treatment of the cultures with 0.1 mM‐norepinephrine or histamine. Stimulation due to addition of norepinephrine was inhibited by propranolol. The carbonic anhydrase activity of primary cultures derived from the cerebellum plus brain stem regions was about fourfold greater than the activity of primary cultures started from cerebral hemispheres, but in contrast was not stimulated by norepinephrine. Treatment of the cerebral cultures with norepinephrine in the presence of 32P resulted in a two‐ to threefold increased incorporation of 32P into carbonic anhydrase purified from the same cultures, and this increased incorporation was inhibited by propranolol. It is suggested that one of the consequences of the stimulation of 3′,5′‐cyclic AMP levels in brain by norepinephrine is activation of astroglial carbonic anhydrase activity due to 3′5′‐cyclic AMP‐stimulated phosphorylation of the enzyme.

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Effects of gastric acid stimulants and inhibitors on the activities of HCO3−-stimulated, Mg2+-dependent ATPase and carbonic anhydrase in rat gastric mucosa

Cited by 39 publications

References 11 publications

Distribution of carbonic anhydrase in cells and membranes isolated from pig gastric mucosa

Distribution of carbonic anhydrase in cells and membranes isolated from pig gastric mucosa

Die Bedeutung der HCO 3 ? -ATPase in der H+/HCO 3 ? -Sekretion

Stimulation of Carbonic Anhydrase Activity and Phosphorylation in Primary Astroglial Cultures by Norepinephrine

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