Proteomics

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A renal function for 2,3-bisphosphoglycerate mutase (BPGM)

ABSTRACT: The enzyme 2,3 bisphosphoglycerate mutase (BPGM) catalyzes the production of 2,3-bisphosphoglycerate (2,3-BPG). The main role of 2,3-BPG is to shift the equilibrium of hemoglobin toward the deoxy-state, accounting for the notion that 2,3-BPG production would appear to be solely useful in cells which contain hemoglobin. 2,3-BPG level determines the baseline O2-Hb affinity at rest, which shows a broad diversity among human population. The kidney is the site of oxygen sensing and erythropoietin synthesis through the action of the hypoxia-inducible factor (HIF) transcription factors, especially HIF-2. We observed a marked BPGM expression in distal parts of renal tubules that is elevated during kidney injury, thus, indicating cellular functions of BPGM not related to oxygen binding to hemoglobin. We, thus, explored the function of renal BPGM, particularly as related to down-stream metabolic effects.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Kidney

SUBMITTER: Anja Freiwald  

LAB HEAD: Michael Fähling

PROVIDER: PXD040789 | Pride | 2025-05-06

REPOSITORIES: Pride

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20220714_QEP_KTT_001_50-0082_Faehling_P00_QC-001_dia.raw.Zip Raw
20220714_QEP_KTT_002_50-0082_Faehling_sample01_dia.raw.Zip Raw
20220714_QEP_KTT_003_50-0082_Faehling_sample05_dia.raw.Zip Raw
20220714_QEP_KTT_004_50-0082_Faehling_sample03_dia.raw.Zip Raw
20220714_QEP_KTT_005_50-0082_Faehling_sample06_dia.raw.Zip Raw
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Publications

<h4>Aim</h4>2,3-bisphosphoglycerate mutase (BPGM) is traditionally recognized for its role in modulating oxygen affinity to hemoglobin in erythrocytes. Recent transcriptomic analyses, however, have indicated a significant upregulation of BPGM in acutely injured murine and human kidneys, suggesting a potential renal function for this enzyme. Here we aim to explore the physiological role of BPGM in the kidney.<h4>Methods</h4>A tubular-specific, doxycycline-inducible Bpgm-knockout mouse model was g  ...[more]

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