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      Plant Serine Protease Inhibitors: Biotechnology Application in Agriculture and Molecular Farming

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          Abstract

          The serine protease inhibitors (SPIs) are widely distributed in living organisms like bacteria, fungi, plants, and humans. The main function of SPIs as protease enzymes is to regulate the proteolytic activity. In plants, most of the studies of SPIs have been focused on their physiological role. The initial studies carried out in plants showed that SPIs participate in the regulation of endogenous proteolytic processes, as the regulation of proteases in seeds. Besides, it was observed that SPIs also participate in the regulation of cell death during plant development and senescence. On the other hand, plant SPIs have an important role in plant defense against pests and phytopathogenic microorganisms. In the last 20 years, several transgenic plants over-expressing SPIs have been produced and tested in order to achieve the increase of the resistance against pathogenic insects. Finally, in molecular farming, SPIs have been employed to minimize the proteolysis of recombinant proteins expressed in plants. The present review discusses the potential biotechnological applications of plant SPIs in the agriculture field.

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          Most cited references134

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          Twenty years of the MEROPS database of proteolytic enzymes, their substrates and inhibitors

          The MEROPS database (http://merops.sanger.ac.uk) is an integrated source of information about peptidases, their substrates and inhibitors, which are of great relevance to biology, medicine and biotechnology. The hierarchical classification of the database is as follows: homologous sets of sequences are grouped into a protein species; protein species are grouped into a family; families are grouped into clans. There is a type example for each protein species (known as a ‘holotype’), family and clan, and each protein species, family and clan has its own unique identifier. Pages to show the involvement of peptidases and peptidase inhibitors in biological pathways have been created. Each page shows the peptidases and peptidase inhibitors involved in the pathway, along with the known substrate cleavages and peptidase-inhibitor interactions, and a link to the KEGG database of biological pathways. Links have also been established with the IUPHAR Guide to Pharmacology. A new service has been set up to allow the submission of identified substrate cleavages so that conservation of the cleavage site can be assessed. This should help establish whether or not a cleavage site is physiologically relevant on the basis that such a cleavage site is likely to be conserved.
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            Protease Inhibitors in Plants: Genes for Improving Defenses Against Insects and Pathogens

            C Ryan (1990)
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              Plant proteases: from phenotypes to molecular mechanisms.

              J A Harten (2007)
              Plant genomes encode hundreds of proteases, which represent dozens of unrelated families. The biological role of these proteases is mostly unknown, but mutant alleles, gene silencing, and overexpression studies have provided phenotypes for a growing number of proteases. The aim of this review is to show the diversity of the processes that are regulated by proteases, and to summarize the current knowledge of the underlying molecular mechanisms. The emerging picture is that plant proteases are key regulators of a striking variety of biological processes, including meiosis, gametophyte survival, embryogenesis, seed coat formation, cuticle deposition, epidermal cell fate, stomata development, chloroplast biogenesis, and local and systemic defense responses. The functional diversity correlates with the molecular data: Proteases are specifically expressed in time and space and accumulate in different subcellular compartments. Their substrates and activation mechanisms are elusive, however, and represent a challenging topic for further research.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                17 March 2019
                March 2019
                : 20
                : 6
                : 1345
                Affiliations
                Instituto Tecnológico Chascomús (INTECH), UNSAM-CONICET, Chascomús, Provincia de Buenos Aires B7130, Argentina; marianacorigliano@ 123456intech.gov.ar (M.G.C.); sebapariani@ 123456hotmail.com (S.A.P.); esanchez@ 123456intech.gov.ar (E.F.S.-L.); valeriasander@ 123456intech.gov.ar (V.A.S.); varamosd@ 123456intech.gov.ar (V.A.R.-D.)
                Author notes
                Author information
                https://orcid.org/0000-0002-0804-1910
                Article
                ijms-20-01345
                10.3390/ijms20061345
                6471620
                30884891
                069c45de-fe2b-45d6-9930-c7e814eeeee5
                © 2019 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 12 January 2019
                : 18 February 2019
                Categories
                Review

                Molecular biology
                serine protease inhibitors,plants,pathogen resistance,molecular farming
                Molecular biology
                serine protease inhibitors, plants, pathogen resistance, molecular farming

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