Carbonic Anhydrase in the Human Fetal Lung
- 1 June 1982
- journal article
- research article
- Published by Springer Nature in Pediatric Research
- Vol. 16 (6) , 407-411
- https://doi.org/10.1203/00006450-198206000-00002
Abstract
Summary: Lung tissue from human fetuses, with gestational ages ranging between 14–26 wk, was studied by histochemical and biochemical methods. The findings were similar in all tissues tested, without apparent correlation to gestational age. Staining that indicated carbonic anhydrase activity was found in the capillary endothelium and in the epithelium of some segments of the peripheral airways. The ciliated epithelium of the central airways was unstained. The distribution of the enzyme in the human fetal lung differed clearly from that in the adult human lung, where little or no enzyme has been found in the airway epithelium. The mean carbonic anhydrase activity in whole homogenates of fetal lung tissue was 24 enzyme units per g wet weight of tissue. Ninety % of this activity was recovered in the supernatant fraction. Assay of this fraction by a radioimmunosorbent technique showed the presence of the carbonic anhydrase isoenzyme HCA-C corresponding to 380 ng enzyme per mg tissue protein. Small amounts of HCA-B were also found but are thought to be attributable to contaminating erythrocytes; thus, the data suggest that both the capillary endothelium and the lung epithelium contain HCA-C, an isoenzyme of carbonic anhydrase known to be involved in electrolyte transport in many tissues. Speculation: Carbonic anhydrase is probably involved in lung liquid secretion in the fetal lamb. The present data suggest that this enzyme plays a similar role in the human fetal lung.This publication has 15 references indexed in Scilit:
- Carbonic anhydrase in rat liver and rabbit skeletal muscle: further evidence for the specificity of the histochemical cobalt-phosphate method of Hansson.Journal of Histochemistry & Cytochemistry, 1980
- EVIDENCE OF A HIGH-ACTIVITY C-TYPE OF CARBONIC-ANHYDRASE IN HUMAN CILIARY PROCESSES1979
- On the lack of specificity of the cobalt-bicarbonate method for carbonic anhydrase.Journal of Histochemistry & Cytochemistry, 1977
- Intracellular Localization of Carbonic Anhydrase in the Frog NephronActa Physiologica Scandinavica, 1976
- Immunologic and kinetic properties of carbonic anhydrases from various tissuesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1968
- Histochemical demonstration of carbonic anhydrase activityHistochemistry and Cell Biology, 1967
- Standardization of hemoglobinometry II. The hemiglobincyanide methodClinica Chimica Acta; International Journal of Clinical Chemistry, 1961
- Carbonic Anhydrase Activity in Fetal and Young Rhesus Monkeys.Experimental Biology and Medicine, 1961
- CARBONIC ANHYDRASE INHIBITION .5. N-5-SUBSTITUTED 2 - ACETYLAMINO - 1,3,4 - THIADIAZOLE - 5 - SULFONAMIDES - METABOLIC CONVERSION AND USE AS CONTROL SUBSTANCES1956
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951