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Insectivorous Bats Digest Chitin in the Stomach Using Acidic Mammalian Chitinase

The gastrointestinal tract of animals is adapted to their primary source of food to optimize resource use and energy intake. Temperate bat species mainly feed on arthropods. These contain the energy-rich carbohydrate chitin, which is indigestible for the endogenous enzymes of a typical mammalian gas...

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Autores principales: Strobel, Sara, Roswag, Anna, Becker, Nina I., Trenczek, Tina E., Encarnação, Jorge A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3760910/
https://www.ncbi.nlm.nih.gov/pubmed/24019876
http://dx.doi.org/10.1371/journal.pone.0072770
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author Strobel, Sara
Roswag, Anna
Becker, Nina I.
Trenczek, Tina E.
Encarnação, Jorge A.
author_facet Strobel, Sara
Roswag, Anna
Becker, Nina I.
Trenczek, Tina E.
Encarnação, Jorge A.
author_sort Strobel, Sara
collection PubMed
description The gastrointestinal tract of animals is adapted to their primary source of food to optimize resource use and energy intake. Temperate bat species mainly feed on arthropods. These contain the energy-rich carbohydrate chitin, which is indigestible for the endogenous enzymes of a typical mammalian gastrointestinal tract. However, the gastrointestinal tract of bat species should be adapted to their diet and be able to digest chitin. We hypothesized that (i) European vespertilionid bat species have the digestive enzyme chitinase and that (ii) the chitinolytic activity is located in the intestine, as has been found for North American bat species. The gastrointestinal tracts of seven bat species (Pipistrellus pipistrellus, Plecotus auritus, Myotis bechsteinii, Myotis nattereri, Myotis daubentonii, Myotis myotis, and Nyctalus leisleri) were tested for chitinolytic activity by diffusion assay. Gastrointestinal tracts of P. pipistrellus, P. auritus, M. nattereri, M. myotis, and N. leisleri were examined for acidic mammalian chitinase by western blot analysis. Tissue sections of the gastrointestinal tract of P. pipistrellus were immunohistochemically analyzed to locate the acidic mammalian chitinase. Chitinolytic activity was detected in the stomachs of all bat species. Western blot analysis confirmed the acidic mammalian chitinase in stomach samples. Immunohistochemistry of the P. pipistrellus gastrointestinal tract indicated that acidic mammalian chitinase is located in the stomach chief cells at the base of the gastric glands. In conclusion, European vespertilionid bat species have acidic mammalian chitinase that is produced in the gastric glands of the stomach. Therefore, the gastrointestinal tracts of insectivorous bat species evolved an enzymatic adaptation to their diet.
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spelling pubmed-37609102013-09-09 Insectivorous Bats Digest Chitin in the Stomach Using Acidic Mammalian Chitinase Strobel, Sara Roswag, Anna Becker, Nina I. Trenczek, Tina E. Encarnação, Jorge A. PLoS One Research Article The gastrointestinal tract of animals is adapted to their primary source of food to optimize resource use and energy intake. Temperate bat species mainly feed on arthropods. These contain the energy-rich carbohydrate chitin, which is indigestible for the endogenous enzymes of a typical mammalian gastrointestinal tract. However, the gastrointestinal tract of bat species should be adapted to their diet and be able to digest chitin. We hypothesized that (i) European vespertilionid bat species have the digestive enzyme chitinase and that (ii) the chitinolytic activity is located in the intestine, as has been found for North American bat species. The gastrointestinal tracts of seven bat species (Pipistrellus pipistrellus, Plecotus auritus, Myotis bechsteinii, Myotis nattereri, Myotis daubentonii, Myotis myotis, and Nyctalus leisleri) were tested for chitinolytic activity by diffusion assay. Gastrointestinal tracts of P. pipistrellus, P. auritus, M. nattereri, M. myotis, and N. leisleri were examined for acidic mammalian chitinase by western blot analysis. Tissue sections of the gastrointestinal tract of P. pipistrellus were immunohistochemically analyzed to locate the acidic mammalian chitinase. Chitinolytic activity was detected in the stomachs of all bat species. Western blot analysis confirmed the acidic mammalian chitinase in stomach samples. Immunohistochemistry of the P. pipistrellus gastrointestinal tract indicated that acidic mammalian chitinase is located in the stomach chief cells at the base of the gastric glands. In conclusion, European vespertilionid bat species have acidic mammalian chitinase that is produced in the gastric glands of the stomach. Therefore, the gastrointestinal tracts of insectivorous bat species evolved an enzymatic adaptation to their diet. Public Library of Science 2013-09-03 /pmc/articles/PMC3760910/ /pubmed/24019876 http://dx.doi.org/10.1371/journal.pone.0072770 Text en © 2013 Strobel et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Strobel, Sara
Roswag, Anna
Becker, Nina I.
Trenczek, Tina E.
Encarnação, Jorge A.
Insectivorous Bats Digest Chitin in the Stomach Using Acidic Mammalian Chitinase
title Insectivorous Bats Digest Chitin in the Stomach Using Acidic Mammalian Chitinase
title_full Insectivorous Bats Digest Chitin in the Stomach Using Acidic Mammalian Chitinase
title_fullStr Insectivorous Bats Digest Chitin in the Stomach Using Acidic Mammalian Chitinase
title_full_unstemmed Insectivorous Bats Digest Chitin in the Stomach Using Acidic Mammalian Chitinase
title_short Insectivorous Bats Digest Chitin in the Stomach Using Acidic Mammalian Chitinase
title_sort insectivorous bats digest chitin in the stomach using acidic mammalian chitinase
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3760910/
https://www.ncbi.nlm.nih.gov/pubmed/24019876
http://dx.doi.org/10.1371/journal.pone.0072770
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