S-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue

Abstract Immunohistochemical (IHC) staining in breast cancer shows both gain and loss of COX2 expression with disease risk and progression. We investigated four common COX2 antibody clones and found high specificity for purified human COX2 for three clones; however, recognition of COX2 in cell lysat...

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Autores principales:	Sonali Jindal, Nathan D. Pennock, Alex Klug, Jayasri Narasimhan, Andrea Calhoun, Michelle R. Roberts, Rulla M. Tamimi, A. Heather Eliassen, Sheila Weinmann, Virginia F. Borges, Pepper Schedin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282
Acceso en línea:	https://doaj.org/article/129419c4a8544d358cac1ef1e1e746bd
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spelling	oai:doaj.org-article:129419c4a8544d358cac1ef1e1e746bd2021-12-02T11:51:07ZS-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue10.1038/s41523-020-00204-62374-4677https://doaj.org/article/129419c4a8544d358cac1ef1e1e746bd2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41523-020-00204-6https://doaj.org/toc/2374-4677Abstract Immunohistochemical (IHC) staining in breast cancer shows both gain and loss of COX2 expression with disease risk and progression. We investigated four common COX2 antibody clones and found high specificity for purified human COX2 for three clones; however, recognition of COX2 in cell lysates was clone dependent. Biochemical characterization revealed two distinct forms of COX2, with SP21 recognizing an S-nitrosylated form, and CX229 and CX294 recognizing non-nitrosylated COX2 antigen. We found S-nitrosylated and non-nitrosylated COX2 occupy different subcellular locations in normal and breast cancer tissue, implicating distinct synthetic/trafficking pathways and function. Dual stains of ~2000 breast cancer cases show early-onset breast cancer had increased expression of both forms of COX2 compared to postmenopausal cases. Our results highlight the strengths of using multiple, highly characterized antibody clones for COX2 IHC studies and raise the prospect that S-nitrosylation of COX2 may play a role in breast cancer biology.Sonali JindalNathan D. PennockAlex KlugJayasri NarasimhanAndrea CalhounMichelle R. RobertsRulla M. TamimiA. Heather EliassenSheila WeinmannVirginia F. BorgesPepper SchedinNature PortfolioarticleNeoplasms. Tumors. Oncology. Including cancer and carcinogensRC254-282ENnpj Breast Cancer, Vol 6, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282
spellingShingle	Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282 Sonali Jindal Nathan D. Pennock Alex Klug Jayasri Narasimhan Andrea Calhoun Michelle R. Roberts Rulla M. Tamimi A. Heather Eliassen Sheila Weinmann Virginia F. Borges Pepper Schedin S-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue
description	Abstract Immunohistochemical (IHC) staining in breast cancer shows both gain and loss of COX2 expression with disease risk and progression. We investigated four common COX2 antibody clones and found high specificity for purified human COX2 for three clones; however, recognition of COX2 in cell lysates was clone dependent. Biochemical characterization revealed two distinct forms of COX2, with SP21 recognizing an S-nitrosylated form, and CX229 and CX294 recognizing non-nitrosylated COX2 antigen. We found S-nitrosylated and non-nitrosylated COX2 occupy different subcellular locations in normal and breast cancer tissue, implicating distinct synthetic/trafficking pathways and function. Dual stains of ~2000 breast cancer cases show early-onset breast cancer had increased expression of both forms of COX2 compared to postmenopausal cases. Our results highlight the strengths of using multiple, highly characterized antibody clones for COX2 IHC studies and raise the prospect that S-nitrosylation of COX2 may play a role in breast cancer biology.
format	article
author	Sonali Jindal Nathan D. Pennock Alex Klug Jayasri Narasimhan Andrea Calhoun Michelle R. Roberts Rulla M. Tamimi A. Heather Eliassen Sheila Weinmann Virginia F. Borges Pepper Schedin
author_facet	Sonali Jindal Nathan D. Pennock Alex Klug Jayasri Narasimhan Andrea Calhoun Michelle R. Roberts Rulla M. Tamimi A. Heather Eliassen Sheila Weinmann Virginia F. Borges Pepper Schedin
author_sort	Sonali Jindal
title	S-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue
title_short	S-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue
title_full	S-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue
title_fullStr	S-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue
title_full_unstemmed	S-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue
title_sort	s-nitrosylated and non-nitrosylated cox2 have differential expression and distinct subcellular localization in normal and breast cancer tissue
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/129419c4a8544d358cac1ef1e1e746bd
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S-nitrosylated and non-nitrosylated COX2 have differential expression and distinct subcellular localization in normal and breast cancer tissue

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