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Molecular Identification of First Putative Aquaporins in Snails

Aquaporins (AQPs), also known as water channel proteins, are members of a large protein family termed Major Intrinsic Proteins (MIP). The mammalian AQPs have been most comprehensively described, while knowledge about AQPs in invertebrates is limited mainly to insects. Not a single AQP protein has be...

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Autores principales: Pieńkowska, Joanna R., Kosicka, Ewa, Wojtkowska, Małgorzata, Kmita, Hanna, Lesicki, Andrzej
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3930841/
https://www.ncbi.nlm.nih.gov/pubmed/24445747
http://dx.doi.org/10.1007/s00232-014-9629-0
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author Pieńkowska, Joanna R.
Kosicka, Ewa
Wojtkowska, Małgorzata
Kmita, Hanna
Lesicki, Andrzej
author_facet Pieńkowska, Joanna R.
Kosicka, Ewa
Wojtkowska, Małgorzata
Kmita, Hanna
Lesicki, Andrzej
author_sort Pieńkowska, Joanna R.
collection PubMed
description Aquaporins (AQPs), also known as water channel proteins, are members of a large protein family termed Major Intrinsic Proteins (MIP). The mammalian AQPs have been most comprehensively described, while knowledge about AQPs in invertebrates is limited mainly to insects. Not a single AQP protein has been described in snails to date. Consequently, we decided to search for the proteins in gastropod representatives, namely Lymnaea stagnalis, Catascopia occulta, and Stagnicola palustris (Mollusca; Gastropoda; Pulmonata; Lymnaeidae). Using the molecular approach, we identified L. stagnalis, C. occulta, and S. palustris open reading frames (ORFs) showing homology to AQP genes available in GenBank database, and characterized the encoded proteins, referred to as LsAQP1, CoAQP1, and SpAQP1, respectively. The putative snail aquaporins contain 299 amino acids, have a molecular mass of about 32 kDa, display the general AQP topology and three-dimensional structure congruent with orthodox AQPs, i.e., water-specific ones. Due to high levels of similarity in their characteristics, LsAQP1 was chosen for further studies, as the obtained results were supposed to be applicable for CoAQP1 and SpAQP1. Expression analysis revealed the presence of LsAQP1 transcript in the digestive tract, the cerebral ganglia, the kidney, the reproductive system, and the foot, suggesting that LsAQP1 as well as CoAQP1 and SpAQP1 are ubiquitous proteins and may play important roles in many essential water transport processes. The role appears to be confirmed by results of the yeast growth complementation assay pointing at functionality of LsAQP1. Thus, the obtained results support the AQP expression in gastropod tissues for the first time. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00232-014-9629-0) contains supplementary material, which is available to authorized users.
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spelling pubmed-39308412014-02-28 Molecular Identification of First Putative Aquaporins in Snails Pieńkowska, Joanna R. Kosicka, Ewa Wojtkowska, Małgorzata Kmita, Hanna Lesicki, Andrzej J Membr Biol Article Aquaporins (AQPs), also known as water channel proteins, are members of a large protein family termed Major Intrinsic Proteins (MIP). The mammalian AQPs have been most comprehensively described, while knowledge about AQPs in invertebrates is limited mainly to insects. Not a single AQP protein has been described in snails to date. Consequently, we decided to search for the proteins in gastropod representatives, namely Lymnaea stagnalis, Catascopia occulta, and Stagnicola palustris (Mollusca; Gastropoda; Pulmonata; Lymnaeidae). Using the molecular approach, we identified L. stagnalis, C. occulta, and S. palustris open reading frames (ORFs) showing homology to AQP genes available in GenBank database, and characterized the encoded proteins, referred to as LsAQP1, CoAQP1, and SpAQP1, respectively. The putative snail aquaporins contain 299 amino acids, have a molecular mass of about 32 kDa, display the general AQP topology and three-dimensional structure congruent with orthodox AQPs, i.e., water-specific ones. Due to high levels of similarity in their characteristics, LsAQP1 was chosen for further studies, as the obtained results were supposed to be applicable for CoAQP1 and SpAQP1. Expression analysis revealed the presence of LsAQP1 transcript in the digestive tract, the cerebral ganglia, the kidney, the reproductive system, and the foot, suggesting that LsAQP1 as well as CoAQP1 and SpAQP1 are ubiquitous proteins and may play important roles in many essential water transport processes. The role appears to be confirmed by results of the yeast growth complementation assay pointing at functionality of LsAQP1. Thus, the obtained results support the AQP expression in gastropod tissues for the first time. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00232-014-9629-0) contains supplementary material, which is available to authorized users. Springer US 2014-01-21 2014 /pmc/articles/PMC3930841/ /pubmed/24445747 http://dx.doi.org/10.1007/s00232-014-9629-0 Text en © The Author(s) 2014 https://creativecommons.org/licenses/by/2.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Article
Pieńkowska, Joanna R.
Kosicka, Ewa
Wojtkowska, Małgorzata
Kmita, Hanna
Lesicki, Andrzej
Molecular Identification of First Putative Aquaporins in Snails
title Molecular Identification of First Putative Aquaporins in Snails
title_full Molecular Identification of First Putative Aquaporins in Snails
title_fullStr Molecular Identification of First Putative Aquaporins in Snails
title_full_unstemmed Molecular Identification of First Putative Aquaporins in Snails
title_short Molecular Identification of First Putative Aquaporins in Snails
title_sort molecular identification of first putative aquaporins in snails
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3930841/
https://www.ncbi.nlm.nih.gov/pubmed/24445747
http://dx.doi.org/10.1007/s00232-014-9629-0
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