ArticleThe Journal of clinical investigation1999
Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice.
Article in The Journal of clinical investigation, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 80 citations in OpenAlex.
- Two Variants of theBiomedicines · 2025Article
- Clinical characteristics of hereditary spherocytosis with red blood cell membrane protein gene variants.Frontiers in pediatrics · 2025Article
- Mitapivat reprograms the RBC metabolome and improves anemia in a mouse model of hereditary spherocytosis.JCI insight · 2023Article
- Dynamic changes in murine erythropoiesis from birth to adulthood: implications for the study of murine models of anemia.Blood advances · 2021Article
- Squeezing for Life - Properties of Red Blood Cell Deformability.Frontiers in physiology · 2018Review
- The Hematopoietic Stem and Progenitor Cell Cistrome: GATA Factor-Dependent cis-Regulatory Mechanisms.Current topics in developmental biology · 2016Review
- Fluorescence assay of the interaction between hemoglobin and the cytoplasmic domain of erythrocyte membrane band 3.Blood cells, molecules & diseases · 2015Article
- Article
- Transglutaminase regulation of cell function.Physiological reviews · 2014Review
- Parathyroid hormone ablation alters erythrocyte parameters that are rescued by calcium-sensing receptor gene deletion.European journal of haematology · 2013Article
- Strain-specific variations in cation content and transport in mouse erythrocytes.Physiological genomics · 2013Article
- Concomitant inactivation of Rb and E2f8 in hematopoietic stem cells synergizes to induce severe anemia.Blood · 2012Article
- Analysis of the mobilities of band 3 populations associated with ankyrin protein and junctional complexes in intact murine erythrocytes.The Journal of biological chemistry · 2012Article
- Comparative proteomics reveals deficiency of SLC9A1 (sodium/hydrogen exchanger NHE1) in β-adducin null red cells.British journal of haematology · 2011Article
- Formation of mammalian erythrocytes: chromatin condensation and enucleation.Trends in cell biology · 2011Review
- The carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin binding.Blood · 2010Article
- Genome-wide identification of TAL1's functional targets: insights into its mechanisms of action in primary erythroid cells.Genome research · 2010Article
- Article
- Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent manner.The Journal of biological chemistry · 2010Article
- The role of hypoxia in 2-butoxyethanol-induced hemangiosarcoma.Toxicological sciences : an official journal of the Society of Toxicology · 2010Article
Corrections and comments
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Authors and funding
11 authors at 7 institutions in 1 country.
Funding
Abstract
Protein 4.2 is a major component of the red blood cell (RBC) membrane skeleton. We used targeted mutagenesis in embryonic stem (ES) cells to elucidate protein 4.2 functions in vivo. Protein 4. 2-null (4.2(-/-)) mice have mild hereditary spherocytosis (HS). Scanning electron microscopy and ektacytometry confirm loss of membrane surface in 4.2(-/-) RBCs. The membrane skeleton architecture is intact, and the spectrin and ankyrin content of 4. 2(-/-) RBCs are normal. Band 3 and band 3-mediated anion transport are decreased. Protein 4.2(-/-) RBCs show altered cation content (increased K+/decreased Na+)resulting in dehydration. The passive Na+ permeability and the activities of the Na-K-2Cl and K-Cl cotransporters, the Na/H exchanger, and the Gardos channel in 4. 2(-/-) RBCs are significantly increased. Protein 4.2(-/-) RBCs demonstrate an abnormal regulation of cation transport by cell volume. Cell shrinkage induces a greater activation of Na/H exchange and Na-K-2Cl cotransport in 4.2(-/-) RBCs compared with controls. The increased passive Na+ permeability of 4.2(-/-) RBCs is also dependent on cell shrinkage. We conclude that protein 4.2 is important in the maintenance of normal surface area in RBCs and for normal RBC cation transport.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.