Role of anions and carbonic anhydrase in epithelia
The existence of carbonic anhydrase (carbonate dehydratase, EC 4. 2.1.1) in blood was suspected and sought because the rates of spontaneous hydration and dehydration of CO 2 and carbonic acid were slow compared with the rates of exchange of CO 2 with blood. The existence of the enzyme in absorbing a...
Published in: | Philosophical Transactions of the Royal Society of London. B, Biological Sciences |
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Online Access: | http://dx.doi.org/10.1098/rstb.1982.0138 https://royalsocietypublishing.org/doi/pdf/10.1098/rstb.1982.0138 |
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crroyalsociety:10.1098/rstb.1982.0138 2024-06-02T08:05:13+00:00 Role of anions and carbonic anhydrase in epithelia 1982 http://dx.doi.org/10.1098/rstb.1982.0138 https://royalsocietypublishing.org/doi/pdf/10.1098/rstb.1982.0138 en eng The Royal Society https://royalsociety.org/journals/ethics-policies/data-sharing-mining/ Philosophical Transactions of the Royal Society of London. B, Biological Sciences volume 299, issue 1097, page 369-381 ISSN 0080-4622 2054-0280 journal-article 1982 crroyalsociety https://doi.org/10.1098/rstb.1982.0138 2024-05-07T14:16:59Z The existence of carbonic anhydrase (carbonate dehydratase, EC 4. 2.1.1) in blood was suspected and sought because the rates of spontaneous hydration and dehydration of CO 2 and carbonic acid were slow compared with the rates of exchange of CO 2 with blood. The existence of the enzyme in absorbing and secreting epithelial tissues has, in contrast, often been sought because its presence was required for the operations of theoretical models for the movements of H + ions or HCO - 3 into or out of epithelial cells. In addition to the HCl-secreting gastric mucosal epithelium, the enzyme was subsequently found in the rumen, in the kidney, especially those of species that produce acid urine, in salivary gland, the liver and biliary duct system, the mucosa of the small intestine, caecum and colon, the choroid plexuses and ciliary body of mammals, in toad urinary bladder and in the Cl - secreting cells of fish gill. The presence of carbonic anhydrase in exocrine pancreas does not seem to be well established. The enzyme, of molecular mass about 30 kDa and containing one zinc atom, exists in three related forms: one of high specific activity and two of low specific activity, one of which is found in red skeletal muscle. Although most, but not all, types of erythrocyte contain both varieties, epithelia usually contain only the highactivity enzyme; however, ox rumen contains large quantities of the low-activity variety as do guinea-pig caecal and colonic mucosae. Salt transport in the intestinal tract is associated with movements of HCO - 3 and of H + ions, yet although carbon dioxide stimulates solute and fluid transport in the gall bladder and jejunum, and inhibitors of carbonic anhydrase reduce fluid and ion transport across many epithelia, the role of the enzyme in epithelial transport is not clearly understood. Knowledge of the rates of hydration and dehydration of CO 2 /HCO - 3 in the fraction of the tissue water responsible for the H + -HCO - 3 movements in many secretory epithelia is currently lacking. Article in Journal/Newspaper Carbonic acid The Royal Society Philosophical Transactions of the Royal Society of London. B, Biological Sciences 299 1097 369 381 |
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The existence of carbonic anhydrase (carbonate dehydratase, EC 4. 2.1.1) in blood was suspected and sought because the rates of spontaneous hydration and dehydration of CO 2 and carbonic acid were slow compared with the rates of exchange of CO 2 with blood. The existence of the enzyme in absorbing and secreting epithelial tissues has, in contrast, often been sought because its presence was required for the operations of theoretical models for the movements of H + ions or HCO - 3 into or out of epithelial cells. In addition to the HCl-secreting gastric mucosal epithelium, the enzyme was subsequently found in the rumen, in the kidney, especially those of species that produce acid urine, in salivary gland, the liver and biliary duct system, the mucosa of the small intestine, caecum and colon, the choroid plexuses and ciliary body of mammals, in toad urinary bladder and in the Cl - secreting cells of fish gill. The presence of carbonic anhydrase in exocrine pancreas does not seem to be well established. The enzyme, of molecular mass about 30 kDa and containing one zinc atom, exists in three related forms: one of high specific activity and two of low specific activity, one of which is found in red skeletal muscle. Although most, but not all, types of erythrocyte contain both varieties, epithelia usually contain only the highactivity enzyme; however, ox rumen contains large quantities of the low-activity variety as do guinea-pig caecal and colonic mucosae. Salt transport in the intestinal tract is associated with movements of HCO - 3 and of H + ions, yet although carbon dioxide stimulates solute and fluid transport in the gall bladder and jejunum, and inhibitors of carbonic anhydrase reduce fluid and ion transport across many epithelia, the role of the enzyme in epithelial transport is not clearly understood. Knowledge of the rates of hydration and dehydration of CO 2 /HCO - 3 in the fraction of the tissue water responsible for the H + -HCO - 3 movements in many secretory epithelia is currently lacking. |
format |
Article in Journal/Newspaper |
title |
Role of anions and carbonic anhydrase in epithelia |
spellingShingle |
Role of anions and carbonic anhydrase in epithelia |
title_short |
Role of anions and carbonic anhydrase in epithelia |
title_full |
Role of anions and carbonic anhydrase in epithelia |
title_fullStr |
Role of anions and carbonic anhydrase in epithelia |
title_full_unstemmed |
Role of anions and carbonic anhydrase in epithelia |
title_sort |
role of anions and carbonic anhydrase in epithelia |
publisher |
The Royal Society |
publishDate |
1982 |
url |
http://dx.doi.org/10.1098/rstb.1982.0138 https://royalsocietypublishing.org/doi/pdf/10.1098/rstb.1982.0138 |
genre |
Carbonic acid |
genre_facet |
Carbonic acid |
op_source |
Philosophical Transactions of the Royal Society of London. B, Biological Sciences volume 299, issue 1097, page 369-381 ISSN 0080-4622 2054-0280 |
op_rights |
https://royalsociety.org/journals/ethics-policies/data-sharing-mining/ |
op_doi |
https://doi.org/10.1098/rstb.1982.0138 |
container_title |
Philosophical Transactions of the Royal Society of London. B, Biological Sciences |
container_volume |
299 |
container_issue |
1097 |
container_start_page |
369 |
op_container_end_page |
381 |
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