Article
An erythroid chaperone that facilitates folding of alpha-globin subunits for hemoglobin synthesis.
The Journal of clinical investigation - 1 Jul 2007
Yu Xiang, Kong Yi, Dore Louis C, Abdulmalik Osheiza, Katein Anne M, Zhou Suiping, Choi John K, Gell David, Mackay Joel P, Gow Andrew J, Weiss Mitchell J
Abstract excerpt
Erythrocyte precursors produce abundant alpha- and beta-globin proteins, which assemble with each other to form hemoglobin A (HbA), the major blood oxygen carrier. alphaHb-stabilizing protein (AHSP) binds free alpha subunits reversibly to maintain their structure and limit their ability to generate reactive oxygen species. Accordingly, loss of AHSP aggravates the toxicity of excessive free alpha-globin caused by...
Topics
- Animals
- Apoproteins
- Blood Proteins
- Cell Differentiation
- Cell Shape
- Erythroid Cells
- Hemoglobins
- Mice
- Mice, Knockout
- Mice, Transgenic
- Molecular Chaperones
- Mutation
- Protein Folding