Dataset Information

DIA-PASEF Proteomic Analysis of Metabolic Responses to Amino Acid Supplementation in H441 Cells

ABSTRACT: This dataset contains untargeted proteomic measurements from H441 epithelial cells cultured under physiologic metabolic conditions. Cells were conditioned in human plasma–like medium (HPLM) and treated with or without an amino acid supplement. Proteomic profiling was performed to quantify global protein abundance changes associated with amino acid supplementation under these metabolic conditions. Pathway-level analyses were conducted to characterize cellular processes altered by supplementation. This dataset provides a resource for examining proteome-level responses to metabolic modulation in epithelial cells.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Ryan McClure

LAB HEAD: Ryan McClure

PROVIDER: PXD072867 | Pride | 2026-03-11

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	G5R1_proteomics_F1_R1_T1_DIA001-EvoSepWZ40SPD_000996_WEWA001_timsTOFultra_S2-E2_1_2805.d.zip	Other
	G5R1_proteomics_F1_R2_T1_DIA001-EvoSepWZ40SPD_000963_WEWA001_timsTOFultra_S2-F2_1_2772.d.zip	Other
	G5R1_proteomics_F1_R3_T1_DIA001-EvoSepWZ40SPD_001020_WEWA001_timsTOFultra_S2-G2_1_2829.d.zip	Other
	G5R2_proteomics_F1_R1_T1_DIA001-EvoSepWZ40SPD_000984_WEWA001_timsTOFultra_S2-E6_1_2793.d.zip	Other
	G5R2_proteomics_F1_R2_T1_DIA001-EvoSepWZ40SPD_001019_WEWA001_timsTOFultra_S2-F6_1_2828.d.zip	Other

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Project description:The metabolic adaptation of eukaryotic cells to hypoxia involves increasing dependence upon glycolytic ATP production, an event with consequences for both cell bioenergetics and cell fate. This response is regulated at the transcriptional level by HIF-1-dependent transcriptional upregulation of all ten glycolytic enzymes. However, this response alone does not account for the levels of ATP produced in hypoxia. Here, we investigated additional mechanisms of regulating glycolysis in hypoxia. We found that both intestinal epithelial cells treated with inhibitors of transcription and translation and human platelets (which lack nuclei) maintained the capacity for hypoxia-induced glycolysis, suggesting the involvement of a non-transcriptional component to the hypoxia-induced metabolic switch to a highly glycolytic phenotype. Mass spectrometric analysis of the interactome of immunoprecipitated rate-limiting glycolytic enzymes identified hypoxia-sensitive complexes comprising multiple glycolytic enzymes and glucose transporters in intestinal epithelial cells. Surprisingly, the formation of glycolytic complexes, though not dependent upon transcription, occurs via a HIF-1?-dependent mechanism, suggesting that HIF-1? may play a moonlighting role in the formation / maintenance of glycolytic complexes. Furthermore, we provide evidence for the presence of HIF-1? in cytosolic fractions of hypoxic cells which physically associated with the glucose transporter GLUT1 and the glycolytic enzyme PFKP in a hypoxia-sensitive manner. In conclusion, we hypothesize that HIF-1? plays a role in initiation and/or maintenance of glycolytic complexes in intestinal epithelial cells under hypoxic conditions in a manner which optimizes catalytic efficiency of the pathway by facilitating substrate channeling of glycolytic intermediates between sequential pathway enzymes. In hypoxia, cells undergo a metabolic switch to increased glycolysis. This has important implications for cell behavior, phenotype, and fate in both healthy and cancerous cells. Here we describe a mechanism by which HIF-1, in addition to increasing glycolytic enzyme expression, promotes glycolysis via the formation of a metabolic complex.

Dataset Information

DIA-PASEF Proteomic Analysis of Metabolic Responses to Amino Acid Supplementation in H441 Cells

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