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Study maps protein network enabling red blood cells to adapt to low oxygen

Phys.org1 min read154 words
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Scientists have charted a previously hidden network of proteins that enables red blood cells to adjust rapidly to fluctuating oxygen levels. Using advanced proteomic mapping and high‑resolution mass spectrometry, researchers at the University of Cambridge identified more than 150 interacting proteins that reorganize in response to hypoxic and hyperoxic conditions, revealing a dynamic scaffold that modulates cell shape, membrane stability, and metabolic pathways essential for oxygen delivery.

The study, published in *Nature Communications*, demonstrates that the protein network operates through coordinated phosphorylation events and reversible binding of chaperones, allowing erythrocytes to maintain flexibility and prevent premature clearance from circulation. By comparing healthy donors with samples from patients suffering from sickle‑cell disease and hereditary spherocytosis, the team showed that disruptions in this network correlate with reduced cell deformability and increased hemolysis. The findings provide a molecular framework for future therapeutic strategies aimed at enhancing red blood cell resilience in disorders where oxygen transport is compromised.

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