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Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders

Plant proteases play a crucial role in many different biological processes along the plant life cycle. One of the most determinant stages in which proteases are key protagonists is the plant germination through the hydrolysis and mobilization of other proteins accumulated in seeds and cereal grains....

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Autores principales: Martinez, Manuel, Gómez-Cabellos, Sara, Giménez, María José, Barro, Francisco, Diaz, Isabel, Diaz-Mendoza, Mercedes
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6548828/
https://www.ncbi.nlm.nih.gov/pubmed/31191594
http://dx.doi.org/10.3389/fpls.2019.00721
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author Martinez, Manuel
Gómez-Cabellos, Sara
Giménez, María José
Barro, Francisco
Diaz, Isabel
Diaz-Mendoza, Mercedes
author_facet Martinez, Manuel
Gómez-Cabellos, Sara
Giménez, María José
Barro, Francisco
Diaz, Isabel
Diaz-Mendoza, Mercedes
author_sort Martinez, Manuel
collection PubMed
description Plant proteases play a crucial role in many different biological processes along the plant life cycle. One of the most determinant stages in which proteases are key protagonists is the plant germination through the hydrolysis and mobilization of other proteins accumulated in seeds and cereal grains. The most represented proteases in charge of this are the cysteine proteases group, including the C1A family known as papain-like and the C13 family also called legumains. In cereal species such as wheat, oat or rye, gluten is a very complex mixture of grain storage proteins, which may affect the health of sensitive consumers like celiac patients. Since gluten proteins are suitable targets for plant proteases, the knowledge of the proteases involved in storage protein mobilization could be employed to manipulate the amount of gluten in the grain. Some proteases have been previously found to exhibit promising properties for their application in the degradation of known toxic peptides from gluten. To explore the variability in gluten-degrading capacities, we have now analyzed the degradation of gluten from different wheat cultivars using several cysteine proteases from barley. The wide variability showed highlights the possibility to select the protease with the highest potential to alter grain composition reducing the gluten content. Consequently, new avenues could be explored combining genetic manipulation of proteolytic processes with silencing techniques to be used as biotechnological tools against gluten-related disorders.
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spelling pubmed-65488282019-06-12 Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders Martinez, Manuel Gómez-Cabellos, Sara Giménez, María José Barro, Francisco Diaz, Isabel Diaz-Mendoza, Mercedes Front Plant Sci Plant Science Plant proteases play a crucial role in many different biological processes along the plant life cycle. One of the most determinant stages in which proteases are key protagonists is the plant germination through the hydrolysis and mobilization of other proteins accumulated in seeds and cereal grains. The most represented proteases in charge of this are the cysteine proteases group, including the C1A family known as papain-like and the C13 family also called legumains. In cereal species such as wheat, oat or rye, gluten is a very complex mixture of grain storage proteins, which may affect the health of sensitive consumers like celiac patients. Since gluten proteins are suitable targets for plant proteases, the knowledge of the proteases involved in storage protein mobilization could be employed to manipulate the amount of gluten in the grain. Some proteases have been previously found to exhibit promising properties for their application in the degradation of known toxic peptides from gluten. To explore the variability in gluten-degrading capacities, we have now analyzed the degradation of gluten from different wheat cultivars using several cysteine proteases from barley. The wide variability showed highlights the possibility to select the protease with the highest potential to alter grain composition reducing the gluten content. Consequently, new avenues could be explored combining genetic manipulation of proteolytic processes with silencing techniques to be used as biotechnological tools against gluten-related disorders. Frontiers Media S.A. 2019-05-29 /pmc/articles/PMC6548828/ /pubmed/31191594 http://dx.doi.org/10.3389/fpls.2019.00721 Text en Copyright © 2019 Martinez, Gómez-Cabellos, Giménez, Barro, Diaz and Diaz-Mendoza. 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 Plant Science
Martinez, Manuel
Gómez-Cabellos, Sara
Giménez, María José
Barro, Francisco
Diaz, Isabel
Diaz-Mendoza, Mercedes
Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders
title Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders
title_full Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders
title_fullStr Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders
title_full_unstemmed Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders
title_short Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders
title_sort plant proteases: from key enzymes in germination to allies for fighting human gluten-related disorders
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6548828/
https://www.ncbi.nlm.nih.gov/pubmed/31191594
http://dx.doi.org/10.3389/fpls.2019.00721
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