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Osmotin: a plant sentinel and a possible agonist of mammalian adiponectin
Osmotin is a stress responsive antifungal protein belonging to the pathogenesis-related (PR)-5 family that confers tolerance to both biotic and abiotic stresses in plants. Protective efforts of osmotin in plants range from high temperature to cold and salt to drought. It lyses the plasma membrane of...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4360817/ https://www.ncbi.nlm.nih.gov/pubmed/25852715 http://dx.doi.org/10.3389/fpls.2015.00163 |
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author | Anil Kumar, S. Hima Kumari, P. Shravan Kumar, G. Mohanalatha, C. Kavi Kishor, P. B. |
author_facet | Anil Kumar, S. Hima Kumari, P. Shravan Kumar, G. Mohanalatha, C. Kavi Kishor, P. B. |
author_sort | Anil Kumar, S. |
collection | PubMed |
description | Osmotin is a stress responsive antifungal protein belonging to the pathogenesis-related (PR)-5 family that confers tolerance to both biotic and abiotic stresses in plants. Protective efforts of osmotin in plants range from high temperature to cold and salt to drought. It lyses the plasma membrane of the pathogens. It is widely distributed in fruits and vegetables. It is a differentially expressed and developmentally regulated protein that protects the cells from osmotic stress and invading pathogens as well, by structural or metabolic alterations. During stress conditions, osmotin helps in the accumulation of the osmolyte proline, which quenches reactive oxygen species and free radicals. Osmotin expression results in the accumulation of storage reserves and increases the shelf-life of fruits. It binds to a seven-transmembrane-domain receptor-like protein and induces programmed cell death in Saccharomyces cerevisiae through RAS2/cAMP signaling pathway. Adiponectin, produced in adipose tissues of mammals, is an insulin-sensitizing hormone. Strangely, osmotin acts like the mammalian hormone adiponectin in various in vitro and in vivo models. Adiponectin and osmotin, the two receptor binding proteins do not share sequence similarity at the amino acid level, but interestingly they have a similar structural and functional properties. In experimental mice, adiponectin inhibits endothelial cell proliferation and migration, primary tumor growth, and reduces atherosclerosis. This retrospective work examines the vital role of osmotin in plant defense and as a potential targeted therapeutic drug for humans. |
format | Online Article Text |
id | pubmed-4360817 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-43608172015-04-07 Osmotin: a plant sentinel and a possible agonist of mammalian adiponectin Anil Kumar, S. Hima Kumari, P. Shravan Kumar, G. Mohanalatha, C. Kavi Kishor, P. B. Front Plant Sci Plant Science Osmotin is a stress responsive antifungal protein belonging to the pathogenesis-related (PR)-5 family that confers tolerance to both biotic and abiotic stresses in plants. Protective efforts of osmotin in plants range from high temperature to cold and salt to drought. It lyses the plasma membrane of the pathogens. It is widely distributed in fruits and vegetables. It is a differentially expressed and developmentally regulated protein that protects the cells from osmotic stress and invading pathogens as well, by structural or metabolic alterations. During stress conditions, osmotin helps in the accumulation of the osmolyte proline, which quenches reactive oxygen species and free radicals. Osmotin expression results in the accumulation of storage reserves and increases the shelf-life of fruits. It binds to a seven-transmembrane-domain receptor-like protein and induces programmed cell death in Saccharomyces cerevisiae through RAS2/cAMP signaling pathway. Adiponectin, produced in adipose tissues of mammals, is an insulin-sensitizing hormone. Strangely, osmotin acts like the mammalian hormone adiponectin in various in vitro and in vivo models. Adiponectin and osmotin, the two receptor binding proteins do not share sequence similarity at the amino acid level, but interestingly they have a similar structural and functional properties. In experimental mice, adiponectin inhibits endothelial cell proliferation and migration, primary tumor growth, and reduces atherosclerosis. This retrospective work examines the vital role of osmotin in plant defense and as a potential targeted therapeutic drug for humans. Frontiers Media S.A. 2015-03-16 /pmc/articles/PMC4360817/ /pubmed/25852715 http://dx.doi.org/10.3389/fpls.2015.00163 Text en Copyright © 2015 Anil Kumar, Hima Kumari, Shravan Kumar, Mohanalatha and Kavi Kishor. 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 | Plant Science Anil Kumar, S. Hima Kumari, P. Shravan Kumar, G. Mohanalatha, C. Kavi Kishor, P. B. Osmotin: a plant sentinel and a possible agonist of mammalian adiponectin |
title | Osmotin: a plant sentinel and a possible agonist of mammalian adiponectin |
title_full | Osmotin: a plant sentinel and a possible agonist of mammalian adiponectin |
title_fullStr | Osmotin: a plant sentinel and a possible agonist of mammalian adiponectin |
title_full_unstemmed | Osmotin: a plant sentinel and a possible agonist of mammalian adiponectin |
title_short | Osmotin: a plant sentinel and a possible agonist of mammalian adiponectin |
title_sort | osmotin: a plant sentinel and a possible agonist of mammalian adiponectin |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4360817/ https://www.ncbi.nlm.nih.gov/pubmed/25852715 http://dx.doi.org/10.3389/fpls.2015.00163 |
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