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Dataset for proteomic analysis of arylamine N-acetyltransferase 1 knockout MDA-MB-231 breast cancer cells

Arylamine N-acetyltransferase 1 (NAT1) is frequently upregulated in breast cancer. An unbiased analysis of proteomes of parental MDA-MB-231 breast cancer cells and two separate NAT1 knockout (KO) cell lines were performed. Among 4,890 proteins identified, 737 and 651 proteins were found significantl...

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Autores principales: Hong, Kyung U., Gardner, Jonathan Q., Doll, Mark A., Stepp, Marcus W., Wilkey, Daniel W., Benz, Frederick W., Cai, Jian, Merchant, Michael L., Hein, David W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9679541/
https://www.ncbi.nlm.nih.gov/pubmed/36426076
http://dx.doi.org/10.1016/j.dib.2022.108634
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author Hong, Kyung U.
Gardner, Jonathan Q.
Doll, Mark A.
Stepp, Marcus W.
Wilkey, Daniel W.
Benz, Frederick W.
Cai, Jian
Merchant, Michael L.
Hein, David W.
author_facet Hong, Kyung U.
Gardner, Jonathan Q.
Doll, Mark A.
Stepp, Marcus W.
Wilkey, Daniel W.
Benz, Frederick W.
Cai, Jian
Merchant, Michael L.
Hein, David W.
author_sort Hong, Kyung U.
collection PubMed
description Arylamine N-acetyltransferase 1 (NAT1) is frequently upregulated in breast cancer. An unbiased analysis of proteomes of parental MDA-MB-231 breast cancer cells and two separate NAT1 knockout (KO) cell lines were performed. Among 4,890 proteins identified, 737 and 651 proteins were found significantly (p < 0.01) upregulated and downregulated, respectively, in NAT1 KO cells, compared to the parental cells. Each set of proteins was analyzed to identify Gene Ontology biological processes, molecular functions, and cellular components that were enriched in the set. Among the proteins upregulated in NAT1 KO cells, processes associated with MHC major histocompatibility complex I-mediated antigen presentation were significantly enriched. Multiple processes involved in mitochondrial functions were collectively downregulated in NAT1 KO cells, including multiple subunits of mitochondrial ATP synthase (Complex V of the electron transport chain). This was accompanied by a reduction in cell cycle-associated proteins and an increase in pro-apoptotic pathways in NAT1 KO cells. The current dataset contains additional representations of the biological processes and components that are differentially enriched in NAT1 KO MDA-MB-231 cells and will serve as a basis for generating novel hypotheses regarding the role of NAT1 in breast cancer. Data are available via ProteomeXchange with identifier PXD035953.
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spelling pubmed-96795412022-11-23 Dataset for proteomic analysis of arylamine N-acetyltransferase 1 knockout MDA-MB-231 breast cancer cells Hong, Kyung U. Gardner, Jonathan Q. Doll, Mark A. Stepp, Marcus W. Wilkey, Daniel W. Benz, Frederick W. Cai, Jian Merchant, Michael L. Hein, David W. Data Brief Data Article Arylamine N-acetyltransferase 1 (NAT1) is frequently upregulated in breast cancer. An unbiased analysis of proteomes of parental MDA-MB-231 breast cancer cells and two separate NAT1 knockout (KO) cell lines were performed. Among 4,890 proteins identified, 737 and 651 proteins were found significantly (p < 0.01) upregulated and downregulated, respectively, in NAT1 KO cells, compared to the parental cells. Each set of proteins was analyzed to identify Gene Ontology biological processes, molecular functions, and cellular components that were enriched in the set. Among the proteins upregulated in NAT1 KO cells, processes associated with MHC major histocompatibility complex I-mediated antigen presentation were significantly enriched. Multiple processes involved in mitochondrial functions were collectively downregulated in NAT1 KO cells, including multiple subunits of mitochondrial ATP synthase (Complex V of the electron transport chain). This was accompanied by a reduction in cell cycle-associated proteins and an increase in pro-apoptotic pathways in NAT1 KO cells. The current dataset contains additional representations of the biological processes and components that are differentially enriched in NAT1 KO MDA-MB-231 cells and will serve as a basis for generating novel hypotheses regarding the role of NAT1 in breast cancer. Data are available via ProteomeXchange with identifier PXD035953. Elsevier 2022-09-24 /pmc/articles/PMC9679541/ /pubmed/36426076 http://dx.doi.org/10.1016/j.dib.2022.108634 Text en © 2022 The Author(s). Published by Elsevier Inc. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Data Article
Hong, Kyung U.
Gardner, Jonathan Q.
Doll, Mark A.
Stepp, Marcus W.
Wilkey, Daniel W.
Benz, Frederick W.
Cai, Jian
Merchant, Michael L.
Hein, David W.
Dataset for proteomic analysis of arylamine N-acetyltransferase 1 knockout MDA-MB-231 breast cancer cells
title Dataset for proteomic analysis of arylamine N-acetyltransferase 1 knockout MDA-MB-231 breast cancer cells
title_full Dataset for proteomic analysis of arylamine N-acetyltransferase 1 knockout MDA-MB-231 breast cancer cells
title_fullStr Dataset for proteomic analysis of arylamine N-acetyltransferase 1 knockout MDA-MB-231 breast cancer cells
title_full_unstemmed Dataset for proteomic analysis of arylamine N-acetyltransferase 1 knockout MDA-MB-231 breast cancer cells
title_short Dataset for proteomic analysis of arylamine N-acetyltransferase 1 knockout MDA-MB-231 breast cancer cells
title_sort dataset for proteomic analysis of arylamine n-acetyltransferase 1 knockout mda-mb-231 breast cancer cells
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9679541/
https://www.ncbi.nlm.nih.gov/pubmed/36426076
http://dx.doi.org/10.1016/j.dib.2022.108634
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