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Expression pattern of arenicins—the antimicrobial peptides of polychaete Arenicola marina
Immune responses of invertebrate animals are mediated through innate mechanisms, among which production of antimicrobial peptides play an important role. Although evolutionary Polychaetes represent an interesting group closely related to a putative common ancestor of other coelomates, their immune m...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4271772/ https://www.ncbi.nlm.nih.gov/pubmed/25566093 http://dx.doi.org/10.3389/fphys.2014.00497 |
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author | Maltseva, Arina L. Kotenko, Olga N. Kokryakov, Vladimir N. Starunov, Viktor V. Krasnodembskaya, Anna D. |
author_facet | Maltseva, Arina L. Kotenko, Olga N. Kokryakov, Vladimir N. Starunov, Viktor V. Krasnodembskaya, Anna D. |
author_sort | Maltseva, Arina L. |
collection | PubMed |
description | Immune responses of invertebrate animals are mediated through innate mechanisms, among which production of antimicrobial peptides play an important role. Although evolutionary Polychaetes represent an interesting group closely related to a putative common ancestor of other coelomates, their immune mechanisms still remain scarcely investigated. Previously our group has identified arenicins—new antimicrobial peptides of the lugworm Arenicola marina, since then these peptides were thoroughly characterized in terms of their structure and inhibitory potential. In the present study we addressed the question of the physiological functions of arenicins in the lugworm body. Using molecular and immunocytochemical methods we demonstrated that arencins are expressed in the wide range of the lugworm tissues—coelomocytes, body wall, extravasal tissue and the gut. The expression of arenicins is constitutive and does not depend on stimulation of various infectious stimuli. Most intensively arenicins are produced by mature coelomocytes where they function as killing agents inside the phagolysosome. In the gut and the body wall epithelia arenicins are released from producing cells via secretion as they are found both inside the epithelial cells and in the contents of the cuticle. Collectively our study showed that arenicins are found in different body compartments responsible for providing a first line of defense against infections, which implies their important role as key components of both epithelial and systemic branches of host defense. |
format | Online Article Text |
id | pubmed-4271772 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-42717722015-01-06 Expression pattern of arenicins—the antimicrobial peptides of polychaete Arenicola marina Maltseva, Arina L. Kotenko, Olga N. Kokryakov, Vladimir N. Starunov, Viktor V. Krasnodembskaya, Anna D. Front Physiol Physiology Immune responses of invertebrate animals are mediated through innate mechanisms, among which production of antimicrobial peptides play an important role. Although evolutionary Polychaetes represent an interesting group closely related to a putative common ancestor of other coelomates, their immune mechanisms still remain scarcely investigated. Previously our group has identified arenicins—new antimicrobial peptides of the lugworm Arenicola marina, since then these peptides were thoroughly characterized in terms of their structure and inhibitory potential. In the present study we addressed the question of the physiological functions of arenicins in the lugworm body. Using molecular and immunocytochemical methods we demonstrated that arencins are expressed in the wide range of the lugworm tissues—coelomocytes, body wall, extravasal tissue and the gut. The expression of arenicins is constitutive and does not depend on stimulation of various infectious stimuli. Most intensively arenicins are produced by mature coelomocytes where they function as killing agents inside the phagolysosome. In the gut and the body wall epithelia arenicins are released from producing cells via secretion as they are found both inside the epithelial cells and in the contents of the cuticle. Collectively our study showed that arenicins are found in different body compartments responsible for providing a first line of defense against infections, which implies their important role as key components of both epithelial and systemic branches of host defense. Frontiers Media S.A. 2014-12-19 /pmc/articles/PMC4271772/ /pubmed/25566093 http://dx.doi.org/10.3389/fphys.2014.00497 Text en Copyright © 2014 Maltseva, Kotenko, Kokryakov, Starunov and Krasnodembskaya. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Physiology Maltseva, Arina L. Kotenko, Olga N. Kokryakov, Vladimir N. Starunov, Viktor V. Krasnodembskaya, Anna D. Expression pattern of arenicins—the antimicrobial peptides of polychaete Arenicola marina |
title | Expression pattern of arenicins—the antimicrobial peptides of polychaete Arenicola marina |
title_full | Expression pattern of arenicins—the antimicrobial peptides of polychaete Arenicola marina |
title_fullStr | Expression pattern of arenicins—the antimicrobial peptides of polychaete Arenicola marina |
title_full_unstemmed | Expression pattern of arenicins—the antimicrobial peptides of polychaete Arenicola marina |
title_short | Expression pattern of arenicins—the antimicrobial peptides of polychaete Arenicola marina |
title_sort | expression pattern of arenicins—the antimicrobial peptides of polychaete arenicola marina |
topic | Physiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4271772/ https://www.ncbi.nlm.nih.gov/pubmed/25566093 http://dx.doi.org/10.3389/fphys.2014.00497 |
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