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Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues

The enzyme spermine oxidase (SMOX) is involved in polyamine catabolism and converts spermine to spermidine. The enzymatic reaction generates reactive hydrogen peroxide and aldehydes as by-products that can damage DNA and other biomolecules. Increased expression of SMOX is frequently found in lung, p...

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Autores principales: Tepper, Armand W. J. W., Chu, Gerald, Klaren, Vincent N. A., Kalin, Jay H., Molina-Ortiz, Patricia, Impagliazzo, Antonietta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9032377/
https://www.ncbi.nlm.nih.gov/pubmed/35452470
http://dx.doi.org/10.1371/journal.pone.0267046
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author Tepper, Armand W. J. W.
Chu, Gerald
Klaren, Vincent N. A.
Kalin, Jay H.
Molina-Ortiz, Patricia
Impagliazzo, Antonietta
author_facet Tepper, Armand W. J. W.
Chu, Gerald
Klaren, Vincent N. A.
Kalin, Jay H.
Molina-Ortiz, Patricia
Impagliazzo, Antonietta
author_sort Tepper, Armand W. J. W.
collection PubMed
description The enzyme spermine oxidase (SMOX) is involved in polyamine catabolism and converts spermine to spermidine. The enzymatic reaction generates reactive hydrogen peroxide and aldehydes as by-products that can damage DNA and other biomolecules. Increased expression of SMOX is frequently found in lung, prostate, colon, stomach and liver cancer models, and the enzyme also appears to play a role in neuronal dysfunction and vascular retinopathy. Because of growing evidence that links SMOX activity with DNA damage, inflammation, and carcinogenesis, the enzyme has come into view as a potential drug target. A major challenge in cancer research is the lack of characterization of antibodies used for identification of target proteins. To overcome this limitation, we generated a panel of high-affinity rabbit monoclonal antibodies against various SMOX epitopes and selected antibodies for use in immunoblotting, SMOX quantification assays, immunofluorescence microscopy and immunohistochemistry. Immunohistochemistry analysis with the antibody SMAB10 in normal and transformed tissues confirms that SMOX is upregulated in several different cancers. Together, the panel of antibodies generated herein adds to the toolbox of high-quality reagents to study SMOX biology and to facilitate SMOX drug development.
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spelling pubmed-90323772022-04-23 Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues Tepper, Armand W. J. W. Chu, Gerald Klaren, Vincent N. A. Kalin, Jay H. Molina-Ortiz, Patricia Impagliazzo, Antonietta PLoS One Research Article The enzyme spermine oxidase (SMOX) is involved in polyamine catabolism and converts spermine to spermidine. The enzymatic reaction generates reactive hydrogen peroxide and aldehydes as by-products that can damage DNA and other biomolecules. Increased expression of SMOX is frequently found in lung, prostate, colon, stomach and liver cancer models, and the enzyme also appears to play a role in neuronal dysfunction and vascular retinopathy. Because of growing evidence that links SMOX activity with DNA damage, inflammation, and carcinogenesis, the enzyme has come into view as a potential drug target. A major challenge in cancer research is the lack of characterization of antibodies used for identification of target proteins. To overcome this limitation, we generated a panel of high-affinity rabbit monoclonal antibodies against various SMOX epitopes and selected antibodies for use in immunoblotting, SMOX quantification assays, immunofluorescence microscopy and immunohistochemistry. Immunohistochemistry analysis with the antibody SMAB10 in normal and transformed tissues confirms that SMOX is upregulated in several different cancers. Together, the panel of antibodies generated herein adds to the toolbox of high-quality reagents to study SMOX biology and to facilitate SMOX drug development. Public Library of Science 2022-04-22 /pmc/articles/PMC9032377/ /pubmed/35452470 http://dx.doi.org/10.1371/journal.pone.0267046 Text en © 2022 Tepper et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Tepper, Armand W. J. W.
Chu, Gerald
Klaren, Vincent N. A.
Kalin, Jay H.
Molina-Ortiz, Patricia
Impagliazzo, Antonietta
Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues
title Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues
title_full Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues
title_fullStr Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues
title_full_unstemmed Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues
title_short Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues
title_sort development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9032377/
https://www.ncbi.nlm.nih.gov/pubmed/35452470
http://dx.doi.org/10.1371/journal.pone.0267046
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