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Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins

BACKGROUND: Proteins that selectively transport water across the membranes of cells are recognized as important in the normal functioning of the body systems of vertebrates. There are 13 known mammalian aquaporins (AQP0 to AQP12), some of which have been shown to have unexpected cellular roles beyon...

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Autores principales: Isokpehi, Raphael D, Rajnarayanan, Rajendram V, Jeffries, Cynthia D, Oyeleye, Tolulola O, Cohly, Hari HP
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2966333/
https://www.ncbi.nlm.nih.gov/pubmed/19607658
http://dx.doi.org/10.1186/1471-2164-10-S2-S7
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author Isokpehi, Raphael D
Rajnarayanan, Rajendram V
Jeffries, Cynthia D
Oyeleye, Tolulola O
Cohly, Hari HP
author_facet Isokpehi, Raphael D
Rajnarayanan, Rajendram V
Jeffries, Cynthia D
Oyeleye, Tolulola O
Cohly, Hari HP
author_sort Isokpehi, Raphael D
collection PubMed
description BACKGROUND: Proteins that selectively transport water across the membranes of cells are recognized as important in the normal functioning of the body systems of vertebrates. There are 13 known mammalian aquaporins (AQP0 to AQP12), some of which have been shown to have unexpected cellular roles beyond transmembrane water transport. The availability of non-mammalian vertebrate animal models has the potential to provide insight into the emergence of diverse function in the aquaporins. The domesticated chicken (Gallus gallus) is the premier avian model for biological research; however, only a limited number of studies have compared chicken and mammalian aquaporins. The identification of aquaporins that share functional motifs or are expressed in the same tissues in human and chicken could allow the further functional analyses of homologous aquaporins in both species. We hypothesize that integrative analyses of protein sequences and body site expression of human, mouse, rat and chicken aquaporins has the potential to yield novel biological hypotheses about the unexpected cellular roles of aquaporins beyond transmembrane water transport. RESULTS: A total of 76 aquaporin transcript models derived from 47 aquaporin genes were obtained for human, mouse, rat and chicken. Eleven body sites (brain, connective tissue, head, heart, liver, muscle, ovary, pancreas, small intestine, spleen and testis) were identified in which there is suggested expression of at least one mammalian and one chicken aquaporin. This study demonstrates that modern on-line analysis tools, a novel matrix integration technique, and the availability of the chicken genome for comparative genomics and expression analysis enables hypothesis generation in several important areas including: (i) alternative transcription and speciation effects on the conservation of functional motifs in vertebrate aquaporins; (ii) the emergence of basolateral targeting in mammalian species; (iii) the potential of the cysteine-rich AQP11 as a possible target in the pathophysiology of neurodegenerative disorders such as autism that involve Purkinje cells; and (iv) possible impairment of function of pancreas-expressed AQP12 during pancreatotropic necrosis in avian influenza virus infection. CONCLUSION: The investigation of aquaporin function in chicken and mammalian species has the potential to accelerate the discovery of novel knowledge of aquaporins in both avian and mammalian species.
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spelling pubmed-29663332010-10-29 Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins Isokpehi, Raphael D Rajnarayanan, Rajendram V Jeffries, Cynthia D Oyeleye, Tolulola O Cohly, Hari HP BMC Genomics Proceedings BACKGROUND: Proteins that selectively transport water across the membranes of cells are recognized as important in the normal functioning of the body systems of vertebrates. There are 13 known mammalian aquaporins (AQP0 to AQP12), some of which have been shown to have unexpected cellular roles beyond transmembrane water transport. The availability of non-mammalian vertebrate animal models has the potential to provide insight into the emergence of diverse function in the aquaporins. The domesticated chicken (Gallus gallus) is the premier avian model for biological research; however, only a limited number of studies have compared chicken and mammalian aquaporins. The identification of aquaporins that share functional motifs or are expressed in the same tissues in human and chicken could allow the further functional analyses of homologous aquaporins in both species. We hypothesize that integrative analyses of protein sequences and body site expression of human, mouse, rat and chicken aquaporins has the potential to yield novel biological hypotheses about the unexpected cellular roles of aquaporins beyond transmembrane water transport. RESULTS: A total of 76 aquaporin transcript models derived from 47 aquaporin genes were obtained for human, mouse, rat and chicken. Eleven body sites (brain, connective tissue, head, heart, liver, muscle, ovary, pancreas, small intestine, spleen and testis) were identified in which there is suggested expression of at least one mammalian and one chicken aquaporin. This study demonstrates that modern on-line analysis tools, a novel matrix integration technique, and the availability of the chicken genome for comparative genomics and expression analysis enables hypothesis generation in several important areas including: (i) alternative transcription and speciation effects on the conservation of functional motifs in vertebrate aquaporins; (ii) the emergence of basolateral targeting in mammalian species; (iii) the potential of the cysteine-rich AQP11 as a possible target in the pathophysiology of neurodegenerative disorders such as autism that involve Purkinje cells; and (iv) possible impairment of function of pancreas-expressed AQP12 during pancreatotropic necrosis in avian influenza virus infection. CONCLUSION: The investigation of aquaporin function in chicken and mammalian species has the potential to accelerate the discovery of novel knowledge of aquaporins in both avian and mammalian species. BioMed Central 2009-07-14 /pmc/articles/PMC2966333/ /pubmed/19607658 http://dx.doi.org/10.1186/1471-2164-10-S2-S7 Text en Copyright ©2009 Isokpehi et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Proceedings
Isokpehi, Raphael D
Rajnarayanan, Rajendram V
Jeffries, Cynthia D
Oyeleye, Tolulola O
Cohly, Hari HP
Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins
title Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins
title_full Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins
title_fullStr Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins
title_full_unstemmed Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins
title_short Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins
title_sort integrative sequence and tissue expression profiling of chicken and mammalian aquaporins
topic Proceedings
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2966333/
https://www.ncbi.nlm.nih.gov/pubmed/19607658
http://dx.doi.org/10.1186/1471-2164-10-S2-S7
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