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Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions

This essay reviews the discoveries, synthesis, and biological significance of prostaglandins (PGs) and other eicosanoids in insect biology. It presents the most current – and growing – understanding of the insect mechanism of PG biosynthesis, provides an updated treatment of known insect phospholipa...

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Autores principales: Stanley, David, Kim, Yonggyun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6375067/
https://www.ncbi.nlm.nih.gov/pubmed/30792667
http://dx.doi.org/10.3389/fphys.2018.01927
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author Stanley, David
Kim, Yonggyun
author_facet Stanley, David
Kim, Yonggyun
author_sort Stanley, David
collection PubMed
description This essay reviews the discoveries, synthesis, and biological significance of prostaglandins (PGs) and other eicosanoids in insect biology. It presents the most current – and growing – understanding of the insect mechanism of PG biosynthesis, provides an updated treatment of known insect phospholipase A(2) (PLA(2)), and details contemporary findings on the biological roles of PGs and other eicosanoids in insect physiology, including reproduction, fluid secretion, hormone actions in fat body, immunity and eicosanoid signaling and cross-talk in immunity. It completes the essay with a prospectus meant to illuminate research opportunities for interested readers. In more detail, cellular and secretory types of PLA(2), similar to those known on the biomedical background, have been identified in insects and their roles in eicosanoid biosynthesis documented. It highlights recent findings showing that eicosanoid biosynthetic pathway in insects is not identical to the solidly established biomedical picture. The relatively low concentrations of arachidonic acid (AA) present in insect phospholipids (PLs) (< 0.1% in some species) indicate that PLA(2) may hydrolyze linoleic acid (LA) as a precursor of eicosanoid biosynthesis. The free LA is desaturated and elongated into AA. Unlike vertebrates, AA is not oxidized by cyclooxygenase, but by a specific peroxidase called peroxinectin to produce PGH(2), which is then isomerized into cell-specific PGs. In particular, PGE(2) synthase recently identified converts PGH(2) into PGE(2). In the cross-talks with other immune mediators, eicosanoids act as downstream signals because any inhibition of eicosanoid signaling leads to significant immunosuppression. Because host immunosuppression favors pathogens and parasitoids, some entomopathogens evolved a PLA(2) inhibitory strategy activity to express their virulence.
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spelling pubmed-63750672019-02-21 Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions Stanley, David Kim, Yonggyun Front Physiol Physiology This essay reviews the discoveries, synthesis, and biological significance of prostaglandins (PGs) and other eicosanoids in insect biology. It presents the most current – and growing – understanding of the insect mechanism of PG biosynthesis, provides an updated treatment of known insect phospholipase A(2) (PLA(2)), and details contemporary findings on the biological roles of PGs and other eicosanoids in insect physiology, including reproduction, fluid secretion, hormone actions in fat body, immunity and eicosanoid signaling and cross-talk in immunity. It completes the essay with a prospectus meant to illuminate research opportunities for interested readers. In more detail, cellular and secretory types of PLA(2), similar to those known on the biomedical background, have been identified in insects and their roles in eicosanoid biosynthesis documented. It highlights recent findings showing that eicosanoid biosynthetic pathway in insects is not identical to the solidly established biomedical picture. The relatively low concentrations of arachidonic acid (AA) present in insect phospholipids (PLs) (< 0.1% in some species) indicate that PLA(2) may hydrolyze linoleic acid (LA) as a precursor of eicosanoid biosynthesis. The free LA is desaturated and elongated into AA. Unlike vertebrates, AA is not oxidized by cyclooxygenase, but by a specific peroxidase called peroxinectin to produce PGH(2), which is then isomerized into cell-specific PGs. In particular, PGE(2) synthase recently identified converts PGH(2) into PGE(2). In the cross-talks with other immune mediators, eicosanoids act as downstream signals because any inhibition of eicosanoid signaling leads to significant immunosuppression. Because host immunosuppression favors pathogens and parasitoids, some entomopathogens evolved a PLA(2) inhibitory strategy activity to express their virulence. Frontiers Media S.A. 2019-02-07 /pmc/articles/PMC6375067/ /pubmed/30792667 http://dx.doi.org/10.3389/fphys.2018.01927 Text en Copyright © 2019 Stanley and Kim. 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) and the copyright owner(s) 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
Stanley, David
Kim, Yonggyun
Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions
title Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions
title_full Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions
title_fullStr Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions
title_full_unstemmed Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions
title_short Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions
title_sort prostaglandins and other eicosanoids in insects: biosynthesis and biological actions
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6375067/
https://www.ncbi.nlm.nih.gov/pubmed/30792667
http://dx.doi.org/10.3389/fphys.2018.01927
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