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Updated: Jan 29, 2026

Co-immunoprecipitation Assay Using Endogenous Nuclear Proteins from Cells Cultured Under Hypoxic Conditions
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Profiling of nuclear copper-binding proteins under hypoxic condition.

Haiying Fu1, Xueqin Ding1, Wenjing Zhang1

  • 1Regenerative Medicine Research Center, Sichuan University West China Hospital, Chengdu, 610041, Sichuan, China.

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
|February 11, 2019
PubMed
Summary

Hypoxia causes copper (Cu) to accumulate in cell nuclei, regulating hypoxia-inducible factor-1 (HIF-1) via copper-binding proteins (CuBPs). This study identified dynamic changes in nuclear CuBPs under hypoxia, revealing key proteins involved in transcriptional regulation.

Keywords:
Copper binding proteinsCuHypoxiaProteomics

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Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
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Area of Science:

  • Cell Biology
  • Proteomics
  • Molecular Biology

Background:

  • Copper (Cu) accumulation in cell nuclei under hypoxia influences hypoxia-inducible factor-1 (HIF-1) activity.
  • Copper-binding proteins (CuBPs) are crucial mediators of this nuclear Cu regulation.
  • Understanding dynamic CuBP changes is essential for elucidating Cu's role in hypoxia response.

Purpose of the Study:

  • To explore the dynamic changes of nuclear CuBPs in response to hypoxia using a proteomic approach.
  • To identify specific CuBPs that are differentially expressed or regulated under hypoxic conditions.
  • To investigate the functional implications of identified CuBPs in nuclear processes.

Main Methods:

  • Human umbilical vein endothelial cells (HUVECs) were subjected to hypoxia using dimethyloxalylglycine.
  • Copper immobilized metal affinity chromatography was used to isolate nuclear CuBPs.
  • Nanoliter-liquid chromatography-quadrupole time-of-flight tandem mass spectrometry (nanoLC-Q-TOF-MS/MS) was employed for protein identification.
  • Label-free quantitative proteomics was used to analyze differential protein expression.

Main Results:

  • A total of 278 nuclear CuBPs were identified in hypoxic cells versus 218 in control cells.
  • Functional annotation revealed enrichment of proteins involved in the negative regulation of transcription from RNA polymerase II promoters.
  • Among 17 differentially expressed nuclear proteins, 4 were identified as CuBPs (ILF2, TRA2B, LMNA, HSPB1), with distinct regulation patterns.

Conclusions:

  • Hypoxia induces significant dynamic changes in the nuclear proteome of CuBPs.
  • Several identified CuBPs, including ILF2, TRA2B, LMNA, and HSPB1, are implicated in the nuclear response to hypoxia.
  • These CuBPs represent potential targets for further research into copper's regulation of HIF-1 activity.