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pmid:33195772

Dataset of a comparative proteomics experiment in a methylmalonyl-CoA mutase knockout HEK 293 cell model.

Michele Costanzo · Marianna Caterino · Armando Cevenini · Vincent Jung · Cerina Chhuon · Joanna Lipecka · Roberta Fedele · Ida Chiara Guerrera · Margherita Ruoppolo

Data in brief · 2020 doi:10.1016/j.dib.2020.106453

Paper

complete

Experiment

complete

Data

partial

Analysis

partial

Execution

absent

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Dataset of a comparative proteomics experiment in a methylmalonyl-CoA mutase knockout HEK 293 cell model.
doi
10.1016/j.dib.2020.106453
pmid
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Michele Costanzo
[1]
Marianna Caterino
[2]
Armando Cevenini
[3]
Vincent Jung
[4]
Cerina Chhuon
[5]
Joanna Lipecka
[6]
Roberta Fedele
[7]
Ida Chiara Guerrera
[8]
Margherita Ruoppolo
journal
Data in brief
year
2020
abstract
Methylmalonic acidemia is a rare inborn error of metabolism with severe clinical complications and poor outcome. The present data article is related to a proteomic investigation conducted on a HEK 293 cell line which has been genetically modified using CRISPR-CAS9 system to knockout the methylmalonyl-CoA mutase enzyme (MUT-KO). Thus, the generated cell model for methylmalonic acidemia was used for a proteomic comparison with respect to HEK 293 wild type cells performing a label-free quantification (LFQ) experiment. A comparison between FASP and S-Trap digestion methods was performed on protein extracts before to proceed with the proteomic analysis of the samples. Four biological replicates were employed for LC-MS/MS analysis and each was run in technical triplicates. MaxQuant and Perseus platforms were used to perform the LFQ of the proteomes and carry out statistical analysis, respectively. Globally, 4341 proteins were identified, and 243 as differentially regulated, of which 150 down-regulated and 93 up-regulated in the MUT-KO condition. MS proteomics data have been deposited to the ProteomeXchange Consortium with the dataset identifier PXD017977. The information provided in this dataset shed new light on the cellular mechanisms altered in this rare metabolic disorder, highlighting quantitative unbalances in proteins acting in cell structure and architecture organization and response to the stress. This article can be used as a new source of protein actors to be validated and a starting point for the identification of clinically relevant therapeutic targets.
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Total proteins were extracted from two different HEK 293 cell lines. One was a wild type (WT) cell line. The second one was a cell line developed as cellular model for methylmalonic acidemia after knockout of methylmalonyl-CoA mutase enzyme (MUT-KO).
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Costanzo M, Caterino M, Cevenini A, Jung V, Chhuon C, Lipecka J, Fedele R, Guerrera IC, Ruoppolo M. Proteomics Reveals that Methylmalonyl-CoA Mutase Modulates Cell Architecture and Increases Susceptibility to Stress. Int J Mol Sci. 2020 Jul 15;21(14):E4998. https://doi.org/10.3390/ijms21144998
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Complete file
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The present data article is related to a proteomic investigation conducted on a HEK 293 cell line which has been genetically modified using CRISPR-CAS9 system to knockout the methylmalonyl-CoA mutase enzyme (MUT-KO). Thus, the generated cell model for methylmalonic acidemia was used for a proteomic comparison with respect to HEK 293 wild type cells performing a label-free quantification (LFQ) experiment. A comparison between FASP and S-Trap digestion methods was performed on protein extracts before to proceed with the proteomic analysis of the samples. Four biological replicates were employed for LC-MS/MS analysis and each was run in technical triplicates. MaxQuant and Perseus platforms were used to perform the LFQ of the proteomes and carry out statistical analysis, respectively. Globally, 4341 proteins were identified, and 243 as differentially regulated, of which 150 down-regulated and 93 up-regulated in the MUT-KO condition. 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Proteomics Reveals that Methylmalonyl-CoA Mutase Modulates Cell Architecture and Increases Susceptibility to Stress. 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