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PubMed1998

Effect of acetazolamide on cation concentration in the endolymph of the endolymphatic sac.

Acetazolamide (ACTZ), a carbonic anhydrase inhibitor, has been reported to decrease the endolymphatic sac (ES) DC potential (ESP) in the guinea pig. To assess the involvement of cation transport in the ESP change by ACTZ we examined the effect of ACTZ upon the K+ and Na+ activities of the ES endolymph in the guinea pig using ion-sensitive microelectrode. ACTZ (10 mg/kg), a dose that produces the ESP maximum reduction, produced a significant increase in Na+ activity of the ES endolymph with no change in K+ activity. The results suggest that Na+ transport may be directly or indirectly involved in ESP reduction by ACTZ, and that a Na(+)-H+ exchanger may be involved in Na+ influx pathway from endolymph to the ES epithelial cells.

Acetazolamide↗
PubMed1998

Resting and acetazolamide-challenged technetium-99m-ECD SPECT in transient global amnesia.

Regional resting cerebral blood flow and vascular reserve in a patient with transient global amnesia (TGA) were evaluated during and after a TGA episode using 99mTc-ethyl cysteinate dimer (ECD). The patient had consecutive SPECT studies before and after acetazolamide (ACZ) administration with adjunctive radionuclide angiography using equal-volume-split 99mTc-ECD. SPECT study during TGA episode showed poor vasodilatory reactivity to ACZ in the left medial temporal region involving the hippocampus and resting hypoperfusion in the regions bilaterally. The resting hypoperfusion with reserved vasodilatory reactivity to ACZ also was seen in the bilateral thalami. Abnormal findings in these regions disappeared on the follow-up SPECT study 15 days after the onset. No previous SPECT evaluation of regional abnormalities of both hemodynamic reserve and resting perfusion during and after an episode of TGA has been reported.

Acetazolamide↗
PubMed2001

The inhibition of the carbon concentrating mechanism of the green alga Chlorella saccharophila by acetazolamide.

The effects of the carbonic anhydrase (CA) inhibitors acetazolamide (AZ) and dextran-bound sulfonamide (DBS) on HCO3--dependent O2 evolution in Chlorella saccharophila were evaluated. Addition of 4 µM AZ or 0.4 mg ml-1 DBS to photosynthesizing cells reduced the O2 evolution rate at low dissolved inorganic carbon (DIC) concentration, decreased the size of the intracellular acid-labile carbon pool, and decreased the apparent affinity of the cells for DIC. Measurement of the whole-cell affinity of cells for CO2 and HCO3- in the presence and absence of inhibitors indicated that active HCO3- transport was inhibited by AZ and DBS. The inhibition of HCO3- transport was independent of the inhibition of external and internal CA. These results suggest that the active uptake of HCO3- occurs initially by the interaction of HCO3- and a CA-like transporter.

Journal Article↗
PubMed1990

Properties of a Mutant from Synechocystis PCC6803 Resistant to Acetazolamide, an Inhibitor of Carbonic Anhydrase.

A spontaneous mutant of the cyanobacterium Synechocystis PCC6803 was isolated for its resistance to acetazolamide, an inhibitor of carbonic anhydrase. The mutant showed a deficiency in oxygen exchange between CO(2) and H(2)O, a lower level of stable internal CO(2) pool and a decreased capacity to adapt its photosynthetic affinity under limited inorganic carbon regime. The initial rate of uptake of inorganic carbon was identical to that of wild-type cells. It is demonstrated that the mutation affects the carbonic anhydrase activity. This could result from either of two impairments: a deficiency in the enzyme activity detectable by mass spectrometric determinations, or a modification of the cellular compartment in which the enzyme is located, preventing its activity.

Journal Article↗