Elizabeth Leibold
University of Utah, UT·Biochemistry
Red blood cells need iron to make hemoglobin, the protein that carries oxygen. Dividing cells also need iron to copy their DNA.
- Fields
Biochemistry
Physiology
Medicine & Clinical Research
- Topics
iron metabolism
iron-regulatory protein 2
iron-responsive element
- Grants
- 1 known grant, through Jun 2027
What they work on
- Determine whether loss of Irp2 serine 157 phosphorylation disrupts red blood cell production from within blood-forming cells, using bone marrow transplantation and flow cytometry of cell cycle, proliferation and iron.
- Identify mechanisms behind faulty red-cell maturation in Irp2A/A mice by differentiating normal and mutant bone marrow into erythroblasts in vitro and comparing their proteins with proteomics.
- Generate an erythroid-specific Irp2A/A knock-in mouse, carrying the mutation only in red-cell lineages, to study late-stage red blood cell maturation and anemia.
More about the research
Too little iron causes anemia, but free iron can be harmful, so cells must control their iron supply tightly. A key controller is iron-regulatory protein 2 (Irp2). It binds to iron-responsive elements (IREs), short control sequences on the mRNAs, or gene messages, of proteins that bring iron in, store it (ferritin) or export it. By binding, it adjusts how much of each protein is made. This project asks how a newly found, cell-cycle-linked switch on Irp2 shapes red blood cell production.
Why it matters
Anemia affects more than two billion people worldwide, and iron is essential for making hemoglobin. Understanding how cells link iron handling to cell division while making red blood cells could reveal how red cell production goes wrong. This could offer new insight into the causes of anemia and other blood disorders, and may suggest new points of intervention.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Yvette Yien
University of Pittsburgh, PA·Biochemistry
Determine how the mitochondrial unfoldase CLPX regulates PPOX and FECH, the final two enzymes of heme synthesis, in differentiating red blood cells.
James Palis
University of Rochester, NY·Biology
Test whether BMI1 and RING1B, proteins that silence genes by packaging chromatin, sustain self-renewal of human self-renewing erythroblasts by controlling gene activity epigenetically.
Nicolae David
Northwestern University, IL·Physiology
Test whether inflammation suppresses HNF4α, a gene-activating transcription factor, in bone-forming osteoblasts, creating a feed-forward loop that blunts parathyroid hormone (PTH) response, by switching Hnf4α2 on or off in mice with CKD or PTH challenges.
The school
University of Utah: 58 labs on PI Pages, $789M a year on research, 366 research doctorates a year.
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