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Immunolocalization of Arthropsin in the Onychophoran Euperipatoides rowelli (Peripatopsidae)
Opsins are light-sensitive proteins that play a key role in animal vision and are related to the ancient photoreceptive molecule rhodopsin found in unicellular organisms. In general, opsins involved in vision comprise two major groups: the rhabdomeric (r-opsins) and the ciliary opsins (c-opsins). Th...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4972820/ https://www.ncbi.nlm.nih.gov/pubmed/27540356 http://dx.doi.org/10.3389/fnana.2016.00080 |
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author | Schumann, Isabell Hering, Lars Mayer, Georg |
author_facet | Schumann, Isabell Hering, Lars Mayer, Georg |
author_sort | Schumann, Isabell |
collection | PubMed |
description | Opsins are light-sensitive proteins that play a key role in animal vision and are related to the ancient photoreceptive molecule rhodopsin found in unicellular organisms. In general, opsins involved in vision comprise two major groups: the rhabdomeric (r-opsins) and the ciliary opsins (c-opsins). The functionality of opsins, which is dependent on their protein structure, may have changed during evolution. In arthropods, typically r-opsins are responsible for vision, whereas in vertebrates c-opsins are components of visual photoreceptors. Recently, an enigmatic r-opsin-like protein called arthropsin has been identified in various bilaterian taxa, including arthropods, lophotrochozoans, and chordates, by performing transcriptomic and genomic analyses. Since the role of arthropsin and its distribution within the body are unknown, we immunolocalized this protein in a representative of Onychophora – Euperipatoides rowelli – an ecdysozoan taxon which is regarded as one of the closest relatives of Arthropoda. Our data show that arthropsin is expressed in the central nervous system of E. rowelli, including the brain and the ventral nerve cords, but not in the eyes. These findings are consistent with previous results based on reverse transcription PCR in a closely related onychophoran species and suggest that arthropsin is a non-visual protein. Based on its distribution in the central brain region and the mushroom bodies, we speculate that the onychophoran arthropsin might be either a photosensitive molecule playing a role in the circadian clock, or a non-photosensitive protein involved in olfactory pathways, or both. |
format | Online Article Text |
id | pubmed-4972820 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-49728202016-08-18 Immunolocalization of Arthropsin in the Onychophoran Euperipatoides rowelli (Peripatopsidae) Schumann, Isabell Hering, Lars Mayer, Georg Front Neuroanat Neuroanatomy Opsins are light-sensitive proteins that play a key role in animal vision and are related to the ancient photoreceptive molecule rhodopsin found in unicellular organisms. In general, opsins involved in vision comprise two major groups: the rhabdomeric (r-opsins) and the ciliary opsins (c-opsins). The functionality of opsins, which is dependent on their protein structure, may have changed during evolution. In arthropods, typically r-opsins are responsible for vision, whereas in vertebrates c-opsins are components of visual photoreceptors. Recently, an enigmatic r-opsin-like protein called arthropsin has been identified in various bilaterian taxa, including arthropods, lophotrochozoans, and chordates, by performing transcriptomic and genomic analyses. Since the role of arthropsin and its distribution within the body are unknown, we immunolocalized this protein in a representative of Onychophora – Euperipatoides rowelli – an ecdysozoan taxon which is regarded as one of the closest relatives of Arthropoda. Our data show that arthropsin is expressed in the central nervous system of E. rowelli, including the brain and the ventral nerve cords, but not in the eyes. These findings are consistent with previous results based on reverse transcription PCR in a closely related onychophoran species and suggest that arthropsin is a non-visual protein. Based on its distribution in the central brain region and the mushroom bodies, we speculate that the onychophoran arthropsin might be either a photosensitive molecule playing a role in the circadian clock, or a non-photosensitive protein involved in olfactory pathways, or both. Frontiers Media S.A. 2016-08-04 /pmc/articles/PMC4972820/ /pubmed/27540356 http://dx.doi.org/10.3389/fnana.2016.00080 Text en Copyright © 2016 Schumann, Hering and Mayer. 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 | Neuroanatomy Schumann, Isabell Hering, Lars Mayer, Georg Immunolocalization of Arthropsin in the Onychophoran Euperipatoides rowelli (Peripatopsidae) |
title | Immunolocalization of Arthropsin in the Onychophoran Euperipatoides rowelli (Peripatopsidae) |
title_full | Immunolocalization of Arthropsin in the Onychophoran Euperipatoides rowelli (Peripatopsidae) |
title_fullStr | Immunolocalization of Arthropsin in the Onychophoran Euperipatoides rowelli (Peripatopsidae) |
title_full_unstemmed | Immunolocalization of Arthropsin in the Onychophoran Euperipatoides rowelli (Peripatopsidae) |
title_short | Immunolocalization of Arthropsin in the Onychophoran Euperipatoides rowelli (Peripatopsidae) |
title_sort | immunolocalization of arthropsin in the onychophoran euperipatoides rowelli (peripatopsidae) |
topic | Neuroanatomy |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4972820/ https://www.ncbi.nlm.nih.gov/pubmed/27540356 http://dx.doi.org/10.3389/fnana.2016.00080 |
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