NDLI: Quantitative MS‐Based Proteomics: Comparing the MCF‐7 Cellular Response to Hypoxia and a 2‐Oxoglutarate Analogue

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Quantitative MS‐Based Proteomics: Comparing the MCF‐7 Cellular Response to Hypoxia and a 2‐Oxoglutarate Analogue

Content Provider	Scilit
Author	Bush, Jacob T. Chan, Mun Chiang Mohammed, Shabaz Schofield, Christopher J.
Copyright Year	2020
Description	Journal: ChemBioChem The hypoxia‐inducible factors (HIFs) are key transcription factors in determining cellular responses involving alterations in protein levels in response to limiting oxygen availability in animal cells. 2‐Oxoglurate dependent oxygenases play key roles in regulating HIF levels and its transcriptional activity. We describe MS‐based proteomics studies employing a lysine demethylation‐based approach in which we compared the results of treating human breast cancer MCF‐7 cells with hypoxia or a cell‐penetrating derivative (dimethyl N‐oxalylglycine) of the stable 2OG analogue N‐oxalylglycine. The proteomic results are consistent with reported transcriptomic analyses and support the proposed key roles of 2OG dependent HIF prolyl‐ and asparaginyl‐hydroxylases in the hypoxic response. Differences between the data sets for hypoxia and DMOG may reflect context‐dependent effects or HIF‐independent effects of DMOG
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7317498/pdf
Ending Page	1655
Page Count	9
Starting Page	1647
e-ISSN	14397633
DOI	10.1002/cbic.201900719
Journal	ChemBioChem
Issue Number	11
Volume Number	21
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2020-01-10
Access Restriction	Open
Subject Keyword	Journal: ChemBioChem Biochemical Research Α‐ketoglutarate Oxygenases Hypoxia Inducible Factor (hif) Prolyl- and Asparaginyl-hydroxylases Factor Inhibiting Hif(fih)
Content Type	Text
Resource Type	Article

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Tuning the Transcriptional Response to Hypoxia by Inhibiting Hypoxia-inducible Factor (HIF) Prolyl and Asparaginyl Hydroxylases

Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.

Tuning the Transcriptional Response to Hypoxia by Inhibiting Hypoxia-inducible Factor (HIF) Prolyl and Asparaginyl Hydroxylases

Factor inhibiting HIF can catalyze two asparaginyl hydroxylations in VNVN motifs of ankyrin fold proteins.

Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (fih) substrates indicates widespread asparaginyl.

HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O2 levels

Biochemical and biophysical analyses of hypoxia sensing prolyl hydroxylases from Dictyostelium discoideum and Toxoplasma gondii.

Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing

Factor Inhibiting HIF (FIH) Recognizes Distinct Molecular Features within Hypoxia-inducible Factor-α (HIF-α) versus Ankyrin Repeat Substrates

Quantitative MS‐Based Proteomics: Comparing the MCF‐7 Cellular Response to Hypoxia and a 2‐Oxoglutarate Analogue

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