Localization of carbonic anhydrase on pulmonary artery endothelial cells in culture

U. S. Ryan, P. L. Whitney, J. W. Ryan

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Bovine pulmonary artery endothelial cells in culture possess carbonic anhydrase activity and immunoreactivity. The intact cells and cell homogenates lower the pH of 25 mM triethanolamine sulfate buffer saturated with CO2 (starting pH 8.1). The intact cells are more reactive than the cell homogenates, and the enzymic activity is enriched in association with the plasma membrane fraction. Specific immunofluorescence is obtained when the cells are incubated with rabbit antibovine erythrocyte carbonic anhydrase B and then with goat antirabbit immunoglobulin G coupled to fluorescein. At the level of electron microscopy, antibodies to carbonic anhydrase B are reactive with sites along the plasma membrane and associated caveolae. Multivesicular bodies are the only intracellular sites labeled and appear to correspond to the globular sites of intracellular immunofluorescence. Cells maintained and propagated in culture in the absence of an exogenous source of carbonic anhydrase nonetheless possess carbonic anhydrase activity, suggesting that the cells are capable of synthesizing the enzyme. Taken together, our results indicate that pulmonary artery endothelial cells possess carbonic anhydrase situated so that the enzyme could readily catalyze the dehydration of plasma HCO3 to facilitate CO2 excretion and participate in the regulation of blood pH as central venous blood is converted into systemic arterial blood.

Original languageEnglish
Pages (from-to)914-919
Number of pages6
JournalJournal of Applied Physiology Respiratory Environmental and Exercise Physiology
Volume53
Issue number4
StatePublished - Jan 1 1982
Externally publishedYes

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Carbonic Anhydrases
Pulmonary Artery
Endothelial Cells
Cell Culture Techniques
Carbonic Anhydrase I
Fluorescent Antibody Technique
Cell Membrane
Multivesicular Bodies
Caveolae
Enzymes
Fluorescein
Dehydration
Goats
Catalytic Domain
Electron Microscopy
Buffers
Immunoglobulin G
Erythrocytes
Rabbits
Antibodies

ASJC Scopus subject areas

  • Endocrinology
  • Physiology

Cite this

Localization of carbonic anhydrase on pulmonary artery endothelial cells in culture. / Ryan, U. S.; Whitney, P. L.; Ryan, J. W.

In: Journal of Applied Physiology Respiratory Environmental and Exercise Physiology, Vol. 53, No. 4, 01.01.1982, p. 914-919.

Research output: Contribution to journalArticle

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