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Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders
Amine oxidases (AOs) are ubiquitous enzymes involved in the metabolism of biogenic amines. Copper AOs (Cu-AOs) catalyze the oxidative deamination of primary amine groups of several biogenic amines, such as putrescine, cadaverine, and histamine. In the present review, the effects of a plant amine oxi...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
TheScientificWorldJOURNAL
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5901317/ https://www.ncbi.nlm.nih.gov/pubmed/17619775 http://dx.doi.org/10.1100/tsw.2007.139 |
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author | Masini, Emanuela Bani, Danielle Marzocca, Cosimo Mateescu, Mircea Alexandru Mannaioni, Pier Francesco Federico, Rodolfo Mondovì, Bruno |
author_facet | Masini, Emanuela Bani, Danielle Marzocca, Cosimo Mateescu, Mircea Alexandru Mannaioni, Pier Francesco Federico, Rodolfo Mondovì, Bruno |
author_sort | Masini, Emanuela |
collection | PubMed |
description | Amine oxidases (AOs) are ubiquitous enzymes involved in the metabolism of biogenic amines. Copper AOs (Cu-AOs) catalyze the oxidative deamination of primary amine groups of several biogenic amines, such as putrescine, cadaverine, and histamine. In the present review, the effects of a plant amine oxidase (Cu-AO, histaminase, EC1.4.3.6) purified from pea seedlings in the modulation of IgE-mediated allergic reactions, and in the prevention of cardiac and splachnic postischemic reperfusion damage are reported. |
format | Online Article Text |
id | pubmed-5901317 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | TheScientificWorldJOURNAL |
record_format | MEDLINE/PubMed |
spelling | pubmed-59013172018-06-03 Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders Masini, Emanuela Bani, Danielle Marzocca, Cosimo Mateescu, Mircea Alexandru Mannaioni, Pier Francesco Federico, Rodolfo Mondovì, Bruno ScientificWorldJournal Review Article Amine oxidases (AOs) are ubiquitous enzymes involved in the metabolism of biogenic amines. Copper AOs (Cu-AOs) catalyze the oxidative deamination of primary amine groups of several biogenic amines, such as putrescine, cadaverine, and histamine. In the present review, the effects of a plant amine oxidase (Cu-AO, histaminase, EC1.4.3.6) purified from pea seedlings in the modulation of IgE-mediated allergic reactions, and in the prevention of cardiac and splachnic postischemic reperfusion damage are reported. TheScientificWorldJOURNAL 2007-06-12 /pmc/articles/PMC5901317/ /pubmed/17619775 http://dx.doi.org/10.1100/tsw.2007.139 Text en Copyright © 2007 Emanuela Masini et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Masini, Emanuela Bani, Danielle Marzocca, Cosimo Mateescu, Mircea Alexandru Mannaioni, Pier Francesco Federico, Rodolfo Mondovì, Bruno Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders |
title | Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders |
title_full | Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders |
title_fullStr | Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders |
title_full_unstemmed | Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders |
title_short | Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders |
title_sort | pea seedling histaminase as a novel therapeutic approach to anaphylactic and inflammatory disorders |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5901317/ https://www.ncbi.nlm.nih.gov/pubmed/17619775 http://dx.doi.org/10.1100/tsw.2007.139 |
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