Protein 4.2 is a major component of the erythrocyte membrane cytoskeleton. Here we show that immunoreactive forms of human (Mr 72,000) and pig (Mr 75,000) protein 4.2 are also associated with the plasma membrane of various nonerythroid cells and tissues, such as platelets, brain, and kidney. Protein 4.2 can be extracted from platelet membranes under the same conditions (pH 11, 1 M KI, 1 M urea) which are required to extract protein 4.2 from the erythrocyte plasma membrane. The demonstration of protein 4.2 in nucleated cells that contain also several other proteins of the erythrocyte membrane cytoskeleton indicates some general principles underlying the molecular construction of the plasma membrane in erythrocytes and nonerythroid cells.
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BMC Gastroenterol
January 2025
Department of General Surgery, The Second Affiliated Hospital of Jiaxing University, Zhejiang Province, Jiaxing, 314000, China.
Background: Pancreatic adenocarcinoma (PAAD) is a common malignancy with a very low survival rate. More and more studies have shown that SPTAN1 may be involved in the development and progression of a variety of tumors, including rectal cancer, Pancreatic adenocarcinoma, etc., and may affect their prognosis.
View Article and Find Full Text PDFJ Biol Chem
November 2024
Molecular Medicine and Gene Therapy, Lund Stem Cell Center, Lund University, Lund, Sweden; Division of Gene and Cell Therapy, Institute for Regenerative Medicine, University of Zurich, Zurich, Switzerland. Electronic address:
During human embryogenesis, distinct waves of hematopoiesis give rise to various blood cell types, originating from hemogenic endothelial (HE) cells. As HE cells reside in hypoxic conditions in the embryo, we investigated the role of hypoxia in human endothelial to hematopoietic transition and subsequent hematopoiesis. Using single-cell RNA sequencing, we describe hypoxia-related transcriptional changes in different HE-derived blood lineages, which reveal that erythroid cells are particularly susceptible to oxidative stress, due to decreased NRF2 activity in hypoxia.
View Article and Find Full Text PDFBlood Cells Mol Dis
February 2025
Medicine & Clinical Science, Faculty of Pharmaceutical Sciences, Mukogawa Women's University, Hyogo 663-8179, Japan; Clinical Research Institute for Endocrine and Metabolic Diseases, National Hospital Organization Kyoto Medical Center, Kyoto 612-8555, Japan. Electronic address:
Blood
August 2024
Department of Hematology, St Jude Children's Research Hospital, Memphis, TN.
Red blood cells express high levels of hemoglobin A tetramer (α2β2) to facilitate oxygen transport. Hemoglobin subunits and related proteins are also expressed at lower levels in other tissues across the animal kingdom. Physiological functions for most nonerythroid globins likely derive from their ability to catalyze reduction-oxidation (redox) reactions via electron transfer through heme-associated iron.
View Article and Find Full Text PDFFront Physiol
April 2024
Molecular Medicine Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, United States.
Erythropoietin (EPO) acts primarily in regulating red blood cell production mediated by high EPO receptor (EPOR) expression in erythroid progenitor cells. EPO activity in non-erythroid tissue is evident in mice with EPOR restricted to erythroid tissues (ΔEPORE) that become obese, glucose-intolerant, and insulin-resistant. In animal models, nitric oxide synthase (NOS) contributes to EPO activities including erythropoiesis, neuroprotection, and cardioprotection against ischemia-reperfusion injury.
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