Biomarkers for ragwort poisoning in horses: identification of protein targets

<p>Abstract</p> <p>Background</p> <p>Ingestion of the poisonous weed ragwort (<it>Senecio jacobea</it>) by horses leads to irreversible liver damage. The principal toxins of ragwort are the pyrrolizidine alkaloids that are rapidly metabolised to highly react...

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Main Authors: Beynon Robert J, Matthews Jacqueline B, Knottenbelt Derek, Moore Rowan E, Whitfield Phillip D
Format: Article
Language:English
Published: BMC 2008-08-01
Series:BMC Veterinary Research
Online Access:http://www.biomedcentral.com/1746-6148/4/30
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spelling doaj-8a1922d49dd04c1da96e44795f49a5582020-11-24T21:42:57ZengBMCBMC Veterinary Research1746-61482008-08-01413010.1186/1746-6148-4-30Biomarkers for ragwort poisoning in horses: identification of protein targetsBeynon Robert JMatthews Jacqueline BKnottenbelt DerekMoore Rowan EWhitfield Phillip D<p>Abstract</p> <p>Background</p> <p>Ingestion of the poisonous weed ragwort (<it>Senecio jacobea</it>) by horses leads to irreversible liver damage. The principal toxins of ragwort are the pyrrolizidine alkaloids that are rapidly metabolised to highly reactive and cytotoxic pyrroles, which can escape into the circulation and bind to proteins. In this study a non-invasive <it>in vitro </it>model system has been developed to investigate whether pyrrole toxins induce specific modifications of equine blood proteins that are detectable by proteomic methods.</p> <p>Results</p> <p>One dimensional gel electrophoresis revealed a significant alteration in the equine plasma protein profile following pyrrole exposure and the formation of a high molecular weight protein aggregate. Using mass spectrometry and confirmation by western blotting the major components of this aggregate were identified as fibrinogen, serum albumin and transferrin.</p> <p>Conclusion</p> <p>These findings demonstrate that pyrrolic metabolites can modify equine plasma proteins. The high molecular weight aggregate may result from extensive inter- and intra-molecular cross-linking of fibrinogen with the pyrrole. This model has the potential to form the basis of a novel proteomic strategy aimed at identifying surrogate protein biomarkers of ragwort exposure in horses and other livestock.</p> http://www.biomedcentral.com/1746-6148/4/30
collection DOAJ
language English
format Article
sources DOAJ
author Beynon Robert J
Matthews Jacqueline B
Knottenbelt Derek
Moore Rowan E
Whitfield Phillip D
spellingShingle Beynon Robert J
Matthews Jacqueline B
Knottenbelt Derek
Moore Rowan E
Whitfield Phillip D
Biomarkers for ragwort poisoning in horses: identification of protein targets
BMC Veterinary Research
author_facet Beynon Robert J
Matthews Jacqueline B
Knottenbelt Derek
Moore Rowan E
Whitfield Phillip D
author_sort Beynon Robert J
title Biomarkers for ragwort poisoning in horses: identification of protein targets
title_short Biomarkers for ragwort poisoning in horses: identification of protein targets
title_full Biomarkers for ragwort poisoning in horses: identification of protein targets
title_fullStr Biomarkers for ragwort poisoning in horses: identification of protein targets
title_full_unstemmed Biomarkers for ragwort poisoning in horses: identification of protein targets
title_sort biomarkers for ragwort poisoning in horses: identification of protein targets
publisher BMC
series BMC Veterinary Research
issn 1746-6148
publishDate 2008-08-01
description <p>Abstract</p> <p>Background</p> <p>Ingestion of the poisonous weed ragwort (<it>Senecio jacobea</it>) by horses leads to irreversible liver damage. The principal toxins of ragwort are the pyrrolizidine alkaloids that are rapidly metabolised to highly reactive and cytotoxic pyrroles, which can escape into the circulation and bind to proteins. In this study a non-invasive <it>in vitro </it>model system has been developed to investigate whether pyrrole toxins induce specific modifications of equine blood proteins that are detectable by proteomic methods.</p> <p>Results</p> <p>One dimensional gel electrophoresis revealed a significant alteration in the equine plasma protein profile following pyrrole exposure and the formation of a high molecular weight protein aggregate. Using mass spectrometry and confirmation by western blotting the major components of this aggregate were identified as fibrinogen, serum albumin and transferrin.</p> <p>Conclusion</p> <p>These findings demonstrate that pyrrolic metabolites can modify equine plasma proteins. The high molecular weight aggregate may result from extensive inter- and intra-molecular cross-linking of fibrinogen with the pyrrole. This model has the potential to form the basis of a novel proteomic strategy aimed at identifying surrogate protein biomarkers of ragwort exposure in horses and other livestock.</p>
url http://www.biomedcentral.com/1746-6148/4/30
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