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CO2 and bicarbonate exchange in the rat liver
1Department of Medicine, Harbor-UCLA Medical Center, Torrance 90509.
Journal of Applied Physiology (Bethesda, Md. : 1985)
|December 1, 1988
Summary
Hepatocyte carbonic anhydrase (CA) activity is accessible to the plasma, facilitating CO2 and HCO3- equilibration. Inhibition studies reveal a readily accessible CA isoenzyme on hepatocyte surfaces.
Area of Science:
- Biochemistry
- Physiology
- Enzymology
Background:
- Carbonic anhydrase (CA) enzymes are present in hepatocytes, with distribution varying within the hepatic lobule.
- Sex steroid levels influence the predominant CA isoenzyme in animals.
Purpose of the Study:
- To investigate if hepatocyte CA activity is accessible to plasma for CO2 and HCO3- equilibration in isolated male rat livers.
- To determine the presence and accessibility of CA on the hepatocyte surface.
Main Methods:
- Isolated male rat livers were perfused with erythrocyte-free solutions.
- Labeled H14CO3- and 14CO2 were injected into the portal vein, and 14C emergence from the hepatic vein was monitored.
- Acetazolamide, a CA inhibitor, was infused to assess its effect on labeled compound distribution.
Main Results:
- H14CO3- emergence was slightly faster than 14CO2 emergence in control perfusions.
- Acetazolamide treatment confined H14CO3- to the extracellular space and prolonged 14CO2 outflow, indicating intracellular trapping.
- Infusion of erythrocyte CA normalized the outflow patterns of 14CO2 and H14CO3-.
Conclusions:
- A readily inhibitable CA isoenzyme is present on the hepatocyte surface, accessible to plasma HCO3- and acetazolamide.
- This surface CA facilitates the equilibration of CO2 and HCO3- during a single passage through the liver.
- An intracellular pH of 7.26 was calculated based on perfusate pH and tracer distribution.