Erythroblastic islands: niches for erythropoiesis

Chasis, Joel Anne; Mohandas, Narla

doi:10.1182/blood-2008-03-077883

Cited by 506Hematopoietic Stem Cell TransplantationErythropoietin and Anemia TreatmentHemoglobinopathies and Related Disorders

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Erythroblastic islands: niches for erythropoiesis

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Chasis, Joel Anne, Mohandas, Narla·2008·Blood

DOI 10.1182/blood-2008-03-077883PMC PMC2481536

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Abstract

Erythroblastic islands, the specialized niches in which erythroid precursors proliferate, differentiate, and enucleate, were first described 50 years ago by analysis of transmission electron micrographs of bone marrow. These hematopoietic subcompartments are composed of erythroblasts surrounding a central macrophage. A hiatus of several decades followed, during which the importance of erythroblastic islands remained unrecognized as erythroid progenitors were shown to possess an autonomous differentiation program with a capacity to complete terminal differentiation in vitro in the presence of erythropoietin but without macrophages. However, as the extent of proliferation, differentiation, and enucleation efficiency documented in vivo could not be recapitulated in vitro, a resurgence of interest in erythroid niches has emerged. We now have an increased molecular understanding of processes operating within erythroid niches, including cell-cell and cell-extracellular matrix adhesion, positive and negative regulatory feedback, and central macrophage function. These features of erythroblast islands represent important contributors to normal erythroid development, as well as altered erythropoiesis found in such diverse diseases as anemia of inflammation and chronic disease, myelodysplasia, thalassemia, and malarial anemia. Coupling of historical, current, and future insights will be essential to understand the tightly regulated production of red cells both in steady state and stress erythropoiesis.

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Erythroblastic islands are specialized niches supporting the proliferation and differentiation of erythroblasts, characterized by a central macrophage extending cytoplasmic protrusions to a ring of adjacent erythroblasts, and the interaction of cells within the island is crucial for early and late stages of erythroid maturation.
“Erythroblastic islands are very specialized niches supporting the proliferation and differentiation of erythroblasts.14 Erythroid islands are characterized by a central macrophage that extends cytoplasmic protrusions to a ring of adjacent erythroblasts.The interaction of cells within the island is crucial for early and late stages of erythroid maturation.”
From Inflammatory bone marrow microenvironment (2019) · cites this paper as [14]

Effects of an Rb mutation in the mouse
Jacks, T., Fazeli, A., Schmitt, E. M., Bronson, R. T., Goodell, M. A., & Weinberg, R. A. (1992) · Nature · doi:10.1038/359295a0 · Cited by 1,755
F4/80, a monoclonal antibody directed specifically against the mouse macrophage
Austyn, J. M., & Gordon, S. (1981) · European Journal of Immunology · doi:10.1002/eji.1830111013 · Cited by 1,580
Identification of a factor that links apoptotic cells to phagocytes
Hanayama, R., Tanaka, M., Miwa, K., Shinohara, A., Iwamatsu, A., & Nagata, S. (2002) · Nature · doi:10.1038/417182a · Cited by 1,401
Erythroid differentiation in chimaeric mice blocked by a targeted mutation in the gene for transcription factor GATA-1
Pevny, L., Simon, M. C., Robertson, E., Klein, W. H., Tsai, S.-F., D'Agati, V., Orkin, S. H., & Costantini, F. (1991) · Nature · doi:10.1038/349257a0 · Cited by 1,308
Mice deficient for Rb are nonviable and show defects in neurogenesis and haematopoiesis
Lee, E. Y.-H. P., Chang, C.-Y., Hu, N., Wang, Y.-C. J., Lai, C., Herrup, K., Lee, W., & Bradley, A. (1992) · Nature · doi:10.1038/359288a0 · Cited by 1,264
Requirement for a functional Rb-1 gene in murine development
Clarke, A. R., Maandag, E. R., van ROON, M. A., van der Lugt, N. M. T., van der Valk, M., Hooper, M., Berns, A. J. M., & Rielef, H. T. (1992) · Nature · doi:10.1038/359328a0 · Cited by 1,006
Erythropoietin Retards DNA Breakdown and Prevents Programmed Death in Erythroid Progenitor Cells
Koury, M. J., & Bondurant, M. C. (1990) · Science · doi:10.1126/science.2326648 · Cited by 819
Arrested development of embryonic red cell precursors in mouse embryos lacking transcription factor GATA-1.
Fujiwara, Y., Browne, C. P., Cunniff, K., Goff, S. C., & Orkin, S. H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12355 · Cited by 778
Regulation of Iron Metabolism by Hepcidin
Nemeth, E., & Ganz, T. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111303 · Cited by 756
Novel insights into erythroid development revealed through in vitro differentiation of GATA-1 embryonic stem cells.
Weiss, M. J., Keller, G., & Orkin, S. H. (1994) · Genes & Development · doi:10.1101/gad.8.10.1184 · Cited by 541
Integrin signaling to the actin cytoskeleton
DeMali, K. A., Wennerberg, K., & Burridge, K. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00109-1 · Cited by 511
Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion.
Humphries, M. J., Akiyama, S. K., Komoriya, A., Olden, K., & Yamada, K. M. (1986) · The Journal of cell biology · doi:10.1083/jcb.103.6.2637 · Cited by 438
Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1
Maria, R. D., Zeuner, A., Eramo, A., Domenichelli, C., Bonci, D., Grignani, F., Srinivasula, S. M., Alnemri, E. S., Testa, U., & Peschle, C. (1999) · Nature · doi:10.1038/46809 · Cited by 390
The mononuclear phagocyte system of the mouse defined by immunohistochemical localization of antigen F4/80. Relationship between macrophages, Langerhans cells, reticular cells, and dendritic cells in lymphoid and hematopoietic organs.
Hume, D. A., Robinson, A. P., MacPherson, G. G., & Gordon, S. (1983) · The Journal of Experimental Medicine · doi:10.1084/jem.158.5.1522 · Cited by 390
Requirement of DNase II for Definitive Erythropoiesis in the Mouse Fetal Liver
Kawane, K., Fukuyama, H., Kondoh, G., Takeda, J., Ohsawa, Y., Uchiyama, Y., & Nagata, S. (2001) · Science · doi:10.1126/science.292.5521.1546 · Cited by 387
Phosphatidylserine-dependent engulfment by macrophages of nuclei from erythroid precursor cells
Yoshida, H., Kawane, K., Koike, M., Mori, Y., Uchiyama, Y., & Nagata, S. (2005) · Nature · doi:10.1038/nature03964 · Cited by 346
Development of hematopoietic cells lacking transcription factor GATA-1
Pevny, L., Lin, C., D’Agati, V. D., Simon, M. C., Orkin, S. H., & Costantini, F. D. (1995) · Development · doi:10.1242/dev.121.1.163 · Cited by 345
Iron Metabolism in the Bone Marrow as Seen by Electron Microscopy: A Critical Review
BESSIS, M. C., & BRETON-GORIUS, J. (1962) · Blood · doi:10.1182/blood.v19.6.635.635 · Cited by 324
Transcription factor GATA-1 permits survival and maturation of erythroid precursors by preventing apoptosis.
Weiss, M. J., & Orkin, S. H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.21.9623 · Cited by 296
Yolk sac–derived primitive erythroblasts enucleate during mammalian embryogenesis
Kingsley, P. D., Malik, J. T., Fantauzzo, K. A., & Palis, J. (2004) · Blood · doi:10.1182/blood-2003-12-4162 · Cited by 253
Mouse macrophage hemagglutinin (sheep erythrocyte receptor) with specificity for sialylated glycoconjugates characterized by a monoclonal antibody.
Crocker, P. R., & Gordon, S. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.4.1333 · Cited by 249
The CS5 peptide is a second site in the IIICS region of fibronectin recognized by the integrin alpha 4 beta 1. Inhibition of alpha 4 beta 1 function by RGD peptide homologues
Mould, A. P., Komoriya, A., Yamada, K. M., & Humphries, M. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67834-8 · Cited by 245
ROLE OF GENETIC VARIATION AT THE FIBRINOGEN LOCUS IN DETERMINATION OF PLASMA FIBRINOGEN CONCENTRATIONS
Humphries, S. E., Dubowitz, M., Cook, M., Stirling, Y., & Meade, T. W. (1987) · The Lancet · doi:10.1016/s0140-6736(87)92205-7 · Cited by 233
Molecular Cloning of F4/80, a Murine Macrophage-restricted Cell Surface Glycoprotein with Homology to the G-protein-linked Transmembrane 7 Hormone Receptor Family
McKnight, A. J., Macfarlane, A., Dri, P., TURLEY, L., Willis, A. C., & Gordon, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.486 · Cited by 229
Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin.
Udani, M., Zen, Q., Cottman, M. J., Leonard, N., Jefferson, S., Daymont, C. B., Truskey, G. A., & Telen, M. J. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1204 · Cited by 214
Properties and distribution of a lectin-like hemagglutinin differentially expressed by murine stromal tissue macrophages.
Crocker, P. R., & Gordon, S. (1986) · The Journal of Experimental Medicine · doi:10.1084/jem.164.6.1862 · Cited by 208
Identification of a novel recognition sequence for the integrin alpha 4 beta 1 in the COOH‐terminal heparin‐binding domain of fibronectin.
Mould, A. P., & Humphries, M. J. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04985.x · Cited by 190
Human colony-forming units-erythroid do not require accessory cells, but do require direct interaction with insulin-like growth factor I and/or insulin for erythroid development.
Sawada, K., Krantz, S. B., Dessypris, E., Koury, S. T., & Sawyer, S. T. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114070 · Cited by 188
Transforming growth factor inhibits erythropoiesis by blocking proliferation and accelerating differentiation of erythroid progenitors
Zermati, Y., Fichelson, S., Valensi, F., Freyssinier, J. M., Rouyer‐Fessard, P., Cramer, E. M., Guichard, J., Varet, B. R., & Hermine, O. (2000) · Experimental Hematology · doi:10.1016/s0301-472x(00)00488-4 · Cited by 179
Very late activation antigen 4-vascular cell adhesion molecule 1 interaction is involved in the formation of erythroblastic islands.
Sadahira, Y., Yoshino, T., & Monobe, Y. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.181.1.411 · Cited by 171
TNF-related apoptosis-inducing ligand (TRAIL) as a negative regulator of normal human erythropoiesis.
Zamai, L., Secchiero, P., Pierpaoli, S., Bassini, A., Papa, S., Alnemri, E. S., Guidotti, L., Vitale, M., & Zauli, G. (2000) · PubMed · doi:10.1182/blood.v95.12.3716 · Cited by 165
The association of erythroblasts with macrophages promotes erythroid proliferation and maturation: a 30-kD heparin-binding protein is involved in this contact
Hanspal, M., & Hanspal, J. (1994) · Blood · doi:10.1182/blood.v84.10.3494.3494 · Cited by 164
A fibronectin matrix is required for differentiation of murine erythroleukemia cells into reticulocytes.
Patel, V. P., & Lodish, H. F. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.6.3105 · Cited by 162
[Erythroblastic island, functional unity of bone marrow].
BESSIS, M. C. (2000) · PubMed · Cited by 161
Absence of Erythroblast Macrophage Protein (Emp) Leads to Failure of Erythroblast Nuclear Extrusion
Soni, S., Bala, S., Gwynn, B., Sahr, K. E., Peters, L. L., & Hanspal, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603226200 · Cited by 159
Molecular Identification and Functional Characterization of a Novel Protein That Mediates the Attachment of Erythroblasts to Macrophages
Hanspal, M., Smockova, Y., & Uong, Q. (1998) · Blood · doi:10.1182/blood.v92.8.2940.420k31_2940_2950 · Cited by 155
Adherence to macrophages in erythroblastic islands enhances erythroblast proliferation and increases erythrocyte production by a different mechanism than erythropoietin
Rhodes, M., Kopsombut, P., Bondurant, M. C., Price, J. O., & Koury, M. J. (2007) · Blood · doi:10.1182/blood-2007-06-098178 · Cited by 149
The mononuclear phagocyte system of the mouse defined by immunohistochemical localisation of antigen F4/80
Hume, D., & Gordon, S. (1985) · Springer eBooks · doi:10.1007/978-94-009-5020-7_2 · Cited by 147
Targeted Gene Deletion Demonstrates that Cell Adhesion Molecule ICAM-4 is Critical for \nErythroblastic Island Formation
Lee, G. S., Lo, A., Short, S. A., et al. (2006) · eScholarship (California Digital Library) · Cited by 145
The Lutheran Blood Group Glycoproteins, the Erythroid Receptors for Laminin, Are Adhesion Molecules
Nemer, W. E., Gane, P., Colin, Y., Bony, V., Rahuel, C., Galactéros, F., Cartron, J., & Kim, C. L. V. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16686 · Cited by 142
Retinoblastoma promotes definitive erythropoiesis by repressing Id2 in fetal liver macrophages
Iavarone, A., King, E. R., Dai, X.-M., Leone, G. W., Stanley, E. R., & Lasorella, A. (2004) · Nature · doi:10.1038/nature03068 · Cited by 140
Stem cell factor retards differentiation of normal human erythroid progenitor cells while stimulating proliferation
Muta, K., Krantz, S. B., Bondurant, M. C., & Dai, C. (1995) · Blood · doi:10.1182/blood.v86.2.572.bloodjournal862572 · Cited by 139
The macrophage CD163 surface glycoprotein is an erythroblast adhesion receptor
Fabriek, B. O., Polfliet, M. M. J., Vloet, R. P. M., van der Schors, R. C., Ligtenberg, A. J. M., Weaver, L. K., Geest, C., Matsuno, K., Moestrup, S. K., Dijkstra, C. D., et al. (2007) · Blood · doi:10.1182/blood-2006-08-036467 · Cited by 138
Macrophages function as a ferritin iron source for cultured human erythroid precursors
Leimberg, M. J., Prus, E., Konijn, A. M., & Fibach, E. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21499 · Cited by 137
Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind α5 chain-containing human laminin with high affinity
Parsons, S. F., Lee, G. S., Spring, F. A., Willig, T.-N., Peters, L. L., Gimm, J. A., Tanner, M. J. A., Mohandas, N., Anstee, D. J., & Chasis, J. A. (2001) · Blood · doi:10.1182/blood.v97.1.312 · Cited by 133
Self-citation
Rb intrinsically promotes erythropoiesis by coupling cell cycle exit with mitochondrial biogenesis
Sankaran, V. G., Orkin, & Walkley, C. R. (2008) · Genes & Development · doi:10.1101/gad.1627208 · Cited by 133
The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver.
Parsons, S. F., Mallinson, G., Holmes, C. H., Houlihan, J. M., Simpson, K. L., Mawby, W. J., Spurr, N. K., Warne, D., Barclay, A. N., & Anstee, D. J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5496 · Cited by 131
In vitro characterization of hematopoietic microenvironment cells from patients with myelodysplastic syndrome
Figueroa, E. F., Gutiérrez-Espíndola, G. R., Montesinos, J. J., Arana-Trejo, R. M., & Mayani, H. (2002) · Leukemia Research · doi:10.1016/s0145-2126(01)00193-x · Cited by 127
TRAIL regulates normal erythroid maturation through an ERK-dependent pathway
Secchiero, P., Melloni, E., Heikinheimo, M., Mannisto, S., Pietro, R. D., Iacone, A., & Zauli, G. (2003) · Blood · doi:10.1182/blood-2003-06-2137 · Cited by 124
Enucleation of primitive erythroid cells generates a transient population of “pyrenocytes” in the mammalian fetus
McGrath, K. E., Kingsley, P. D., Koniski, A. D., Porter, R. L., Bushnell, T. P., & Palis, J. (2007) · Blood · doi:10.1182/blood-2007-08-107581 · Cited by 122
Three-dimensional model of bone marrow
Mohandas, N., & Prenant, M. (1978) · Blood · doi:10.1182/blood.v51.4.633.633 · Cited by 121
Self-citation
Characterization of Bone Marrow Laminins and Identification of 5-Containing Laminins as Adhesive Proteins for Multipotent Hematopoietic FDCP-Mix Cells
Gu, Y., Sorokin, L. M., Durbeej, M., Hjalt, T. Å. H., Jönsson, J., & Ekblom, M. (1999) · Blood · doi:10.1182/blood.v93.8.2533 · Cited by 119
Loss of attachment to fibronectin with terminal human erythroid differentiation
Gaugler, M., Breton-Gorius, J., Vainchenker, W., Guichard, J., Leroy, C., Tchernia, G., & Coulombel, L. (1990) · Blood · doi:10.1182/blood.v75.4.865.865 · Cited by 114
An intrinsic but cell-nonautonomous defect in GATA-1-overexpressing mouse erythroid cells
Whyatt, D., Lindeboom, F., Karis, A., Ferreira, R., Milot, É., Hendriks, R. W., Bruijn, M. F. T. R. D., Langeveld, A., Gribnau, J. H., Grosveld, F. G., et al. (2000) · Nature · doi:10.1038/35020086 · Cited by 112
Coexpression of two fibronectin receptors, VLA-4 and VLA-5, by immature human erythroblastic precursor cells.
Rosemblatt, M. S., Gaugler, M., Leroy, C., & Coulombel, L. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115002 · Cited by 108
Growth factor induced activation of Rho and Rac GTPases and actin cytoskeletal reorganization in human lens epithelial cells.
Maddala, R., Reddy, V. N., Epstein, D. L., & Rao, V. (2003) · PubMed · Cited by 107
Role of Gas6 in erythropoiesis and anemia in mice
Angelillo‐Scherrer, A., Burnier, L., Lambrechts, D., Fish, R. J., Tjwa, M., Plaisance, S., Sugamele, R., DeMol, M., Martínez-Soria, E., Maxwell, P. H., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci30375 · Cited by 105
Mechanism of protein sorting during erythroblast enucleation: role of cytoskeletal connectivity
Lee, J. C., Gimm, J. A., Lo, A., Koury, M. J., Krauss, S. W., Mohandas, N., & Chasis, J. A. (2003) · Blood · doi:10.1182/blood-2003-03-0928 · Cited by 101
Self-citation
Ultrastructural localization of a macrophage-restricted sialic acid binding hemagglutinin, SER, in macrophage-hematopoietic cell clusters
Crocker, P. R., Werb, Z., Gordon, S., & Bainton, D. (1990) · Blood · doi:10.1182/blood.v76.6.1131.1131 · Cited by 101
Erythroblasts are a source of angiogenic factors
Tordjman, R., Delaire, S., Plouët, J., Ting, S. B., Gaulard, P., Fichelson, S., Roméo, P., & Lemarchandel, V. (2001) · Blood · doi:10.1182/blood.v97.7.1968 · Cited by 99
Critical Factors in Basal Cell Adhesion Molecule/Lutheran-mediated Adhesion to Laminin
Zen, Q., Cottman, M. J., Truskey, G. A., Fraser, R., & Telen, M. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.728 · Cited by 96
α4β1 integrin and erythropoietin mediate temporally distinct steps in erythropoiesis: integrins in red cell development
Eshghi, S., Vogelezang, M. G., Hynes, R. O., Griffith, L. G., & Lodish, H. F. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702080 · Cited by 92
Current concepts in erythropoiesis
Dunn, C. D. R. (1983) · Medical Entomology and Zoology · Cited by 91
Ultrastructural Aspects of Erythropoietic Differentiation in Long-term Bone Marrow Culture
Allen, T. D., & Dexter, T. M. (1982) · Differentiation · doi:10.1111/j.1432-0436.1982.tb01201.x · Cited by 88
A unique gene encodes spliceoforms of the B-cell adhesion molecule cell surface glycoprotein of epithelial cancer and of the Lutheran blood group glycoprotein
Rahuel, C., Kim, C. L. V., Mattéi, M., CARTRON, J., & Colin, Y. (1996) · Blood · doi:10.1182/blood.v88.5.1865.1865 · Cited by 85
Receptor binding cancer antigen expressed on SiSo cells, a novel regulator of apoptosis of erythroid progenitor cells
Matsushima, T., Nakashima, M., Oshima, K., Abe, Y., Nishimura, J., Nawata, H., Watanabe, T., & Muta, K. (2001) · Blood · doi:10.1182/blood.v98.2.313.h8000313_313_321 · Cited by 84
Activity in fetal bovine serum that stimulates erythroid colony formation in fetal mouse livers is insulinlike growth factor I.
Kurtz, A., Härtl, W., JELKMANN, W. E. B., Zapf, J., & Bauer, C. (1985) · Journal of Clinical Investigation · doi:10.1172/jci112149 · Cited by 84
Role of the macrophage in erythropoiesis
Sadahira, Y., & Mori, M. (1999) · Pathology International · doi:10.1046/j.1440-1827.1999.00954.x · Cited by 77
A role of EphB4 receptor and its ligand, ephrin-B2, in erythropoiesis
Suenobu, S., Takakura, N., Inada, T., Yamada, Y., Yuasa, H., Zhang, X., Sakano, S., Oike, Y., & Suda, T. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00330-3 · Cited by 70
The level of the tissue‐specific factor GATA‐1 affects the cell‐cycle machinery
Whyatt, D., Karis, A., Harkes, I. C., Verkerk, A., Gillemans, N., Elefanty, A. G., Vairo, G., Ploemacher, R., Grosveld, F. G., & Philipsen, S. (1997) · Genes and Function · doi:10.1046/j.1365-4624.1997.00003.x · Cited by 69
Isolation and immunocytochemical characterization of human bone marrow stromal macrophages in hemopoietic clusters.
Lee, S. H., Crocker, P. R., Westaby, S., Key, N. S., Mason, D. Y., Gordon, S., & Weatherall, D. J. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.168.3.1193 · Cited by 65
Use of Domain-Deletion Mutants to Locate Lutheran Blood Group Antigens to Each of the Five Immunoglobulin Superfamily Domains of the Lutheran Glycoprotein: Elucidation of the Molecular Basis of the Lua/Lub and the Aua/Aub Polymorphisms
Parsons, S. F., Mallinson, G., Daniels, G. L., Green, C. A., Smythe, J. S., & Anstee, D. J. (1997) · Blood · doi:10.1182/blood.v89.11.4219 · Cited by 63
Negative Autoregulation by FAS Mediates Robust Fetal Erythropoiesis
Socolovsky, M., Murrell, M. P., Liu, Y. M., Pop, R., Porpiglia, E., & Levchenko, A. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050252 · Cited by 59
Erythropoiesis: comparison of in vivo and in vitro amplification.
BESSIS, M. C., Mize, C. E., & Prenant, M. (1978) · PubMed · Cited by 58
Hepcidin and Cytokines in Anaemia
Means, R. T. (2004) · Hematology · doi:10.1080/10245330400018540 · Cited by 57
Cell-intrinsic requirement for pRb in erythropoiesis
Clark, A. J., Doyle, K. M., & Humbert, P. O. (2004) · Blood · doi:10.1182/blood-2004-02-0618 · Cited by 55
Migration of Erythroblastic Islands toward the Sinusoid as Erythroid Maturation Proceeds in Rat Bone Marrow
YOKOYAMA, T., Takao, E. T. O. H., Kitagawa, H., Tsukahara, S., & Kannan, Y. (2003) · Journal of Veterinary Medical Science · doi:10.1292/jvms.65.449 · Cited by 54
Novel secreted isoform of adhesion molecule ICAM-4: potential regulator of membrane-associated ICAM-4 interactions
Lee, G. S., Spring, F. A., Parsons, S. F., Mankelow, T. J., Peters, L. L., Koury, M. J., Mohandas, N., Anstee, D. J., & Chasis, J. A. (2003) · Blood · doi:10.1182/blood-2002-08-2529 · Cited by 50
Self-citation
Disruption of palladin leads to defects in definitive erythropoiesis by interfering with erythroblastic island formation in mouse fetal liver
Liu, X., Li, X., Wang, Y., Shu, R., Wang, L., Lu, S., Kong, H., Jin, Y., Zhang, L., Fei, J., et al. (2007) · Blood · doi:10.1182/blood-2007-01-068528 · Cited by 47
Importance of cell-cell interactions in regulation of erythropoiesis
Hanspal, M. (1997) · Current Opinion in Hematology · doi:10.1097/00062752-199704020-00011 · Cited by 47
The Laminin 511/521–binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3
Mankelow, T. J., Burton, N., Stefansdottir, F. O., Spring, F. A., Parsons, S. F., Pedersen, J. S., Oliveira, C. L. P., Lammie, D., Wess, T. J., Mohandas, N., et al. (2007) · Blood · doi:10.1182/blood-2007-06-094748 · Cited by 47
Self-citation
Expression of a divalent cation-dependent erythroblast adhesion receptor by stromal macrophages from murine bone marrow
Morris, L., Crocker, P. R., Fraser, I. P., Hill, M. E., & Gordon, S. (1991) · Journal of Cell Science · doi:10.1242/jcs.99.1.141 · Cited by 46
Selective Expression of the Receptor Tyrosine Kinase, HTK, on Human Erythroid Progenitor Cells
Inada, T., Iwama, A., Sakano, S., Ohno, M., Sawada, K., & Suda, T. (1997) · Blood · doi:10.1182/blood.v89.8.2757 · Cited by 41
On the expulsion of the erythroid nucleus and its phagocytosis
Skutelsky, E., & Danon, D. (1972) · The Anatomical Record · doi:10.1002/ar.1091730111 · Cited by 36
Impaired splenic erythropoiesis in phlebotomized mice injected with CL2MDP-liposome: an experimental model for studying the role of stromal macrophages in erythropoiesis
Sadahira, Y., Yasuda, T., Yoshino, T., Manabe, T., Takeishi, T., Kobayashi, Y., Ebe, Y., & Naito, M. (2000) · Journal of Leukocyte Biology · doi:10.1189/jlb.68.4.464 · Cited by 36
A novel bone marrow frozen section assay for studying hematopoietic interactions in situ: the role of stromal bone marrow macrophages in erythroblast binding
Barbé, E., Huitinga, I., Döpp, E. A., Bauer, J., & Dijkstra, C. D. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.12.2937 · Cited by 36
Forssman glycosphingolipid as an immunohistochemical marker for mouse stromal macrophages in hematopoietic foci
Sadahira, Y., Mori, M., Awai, M., Watarai, S., & Yasuda, T. (1988) · Blood · doi:10.1182/blood.v72.1.42.42 · Cited by 35
Fas/Fas ligand and hematopoietic progenitor cells
Niho, Y., & Asano, Y. (1998) · Current Opinion in Hematology · doi:10.1097/00062752-199805000-00002 · Cited by 29
Erythropoietin gene expression in vitro and in vivo detected by in situ hybridization.
Rich, I. N., Vogt, C., & Pentz, S. (1988) · PubMed · Cited by 25
Cellular interactions in erythroblastic islands in long-term bone marrow cultures, as studied by time-lapse video.
Allen, T., & Testa, N. G. (1991) · PubMed · Cited by 24
Hypoxic stress underlies defects in erythroblast islands in the Rb-null mouse
Spike, B. T., Dibling, B. C., & Macleod, K. F. (2007) · Blood · doi:10.1182/blood-2007-01-069104 · Cited by 23
Homotypic signalling regulates Gata1 activity in the erythroblastic island
Gutiérrez, L., Lindeboom, F., Langeveld, A., Grosveld, F. G., Philipsen, S., & Whyatt, D. (2004) · Development · doi:10.1242/dev.01198 · Cited by 23
Regulation of Forssman antigen expression during maturation of mouse stromal macrophages in haematopoietic foci.
Sadahira, Y., Yasuda, T., & Kimoto, T. (1991) · PubMed · Cited by 20
ROLE OF THE RETICULAR CELLS DURING MATURATION PROCESS OF THE ERYTHROBLAST REPORT III. THE FATE OF PHAGOCYTIZED NUCLEUS.
Seki, M., & Shirasawa, H. (1965) · Acta Pathologica Japonica · doi:10.1111/j.1440-1827.1965.tb01930.x · Cited by 20
Three-dimensional model of bone marrow
Mohandas, N., & Prenant, M. (1978) · Blood · doi:10.1182/blood.v51.4.633.bloodjournal514633 · Cited by 20
Self-citation
ROLE OF THE RETICULAR CELLS DURING MATURATION PROCESS OF THE ERYTHROBLAST
Seki, M., Yoneyama, T., & Shirasawa, H. (1965) · Acta Pathologica Japonica · doi:10.1111/j.1440-1827.1965.tb02894.x · Cited by 18
No Apoptotic Cell Death of Erythroid Cells of Erythroblastic Islands in Bone Marrow of Healthy Rats.
YOKOYAMA, T., Kitagawa, H., Takeuchi, T., Tsukahara, S., & Kannan, Y. (2002) · Journal of Veterinary Medical Science · doi:10.1292/jvms.64.913 · Cited by 18
Targeted gene deletion demonstrates that the cell adhesion molecule ICAM-4 is critical for erythroblastic island formation
Lee, G., Lo, A., Short, S. A., Mankelow, T. J., Spring, F., Parsons, S. F., Yazdanbakhsh, K., Mohandas, N., Anstee, D. J., & Chasis, J. A. (2006) · Blood · doi:10.1182/blood-2006-03-006759 · Cited by 15
Self-citation
Changing pattern of the subcellular distribution of erythroblast macrophage protein (Emp) during macrophage differentiation
Soni, S., Bala, S., Kumar, A., & Hanspal, M. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2006.09.005 · Cited by 14
Reduction of cell cycle progression in human erythroid progenitor cells treated with tumour necrosis factor alpha occurs with reduced CDK6 and is partially reversed by CDK6 transduction
Dai, C., Chung, I., Jiang, S., Price, J. O., & Krantz, S. B. (2003) · British Journal of Haematology · doi:10.1046/j.1365-2141.2003.04367.x · Cited by 14
[Isolation of erythroblastic islands. Study by optical and scanning electron microscopy (author's transl)].
Charpentier, Y. L., & Prenant, M. (1975) · PubMed · Cited by 12
Surface expression of forssman glycosphingolipid antigen on murine bone marrow-derived macrophages is subject to both temporal and population-specific regulation and is modulated by IL-4 and IL-6
Monner, D. A., & Mühlradt, P. F. (1993) · Immunobiology · doi:10.1016/s0171-2985(11)80489-4 · Cited by 9

Flagged first, then by citations

Research works printed but not linked: 2

Bessis, 1958, L'ilot erythroblastique. Unite functionelle de la moelle osseuse., Rev Hematol, 13, 8
Porter, 1983, Erythroid burst promoting activity (BPA)., 81

Sorted by citations

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Self-citation
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Sou, K., Goins, B., Oyajobi, B. O., Travi, B. L., & Phillips, W. T. (2011) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.2011.553218 · Cited by 53
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Romano, L., Seu, K. G., Papoin, J., Muench, D. E., Konstantinidis, D. G., Olsson, A., Schlum, K., Chetal, K., Chasis, J. A., Mohandas, N., et al. (2022) · Blood · doi:10.1182/blood.2022015724 · Cited by 50
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Chasis, J. A. (2006) · Current Opinion in Hematology · doi:10.1097/01.moh.0000219657.57915.30 · Cited by 75
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Yeo, J. H., Cosgriff, M. P., & Fraser, S. T. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7428-3_8 · Cited by 8

Authors: Chasis, J. A., & Mohandas, N.
Affiliations: Lawrence Berkeley National Laboratory (US)
New York Blood Center (US)
ORCID: Mohandas, Narla
Venue: Blood
Publisher: American Society of Hematology
Published: 2008-08-01
Volume: 112
Issue: 3
Pages: 470-478
ISSN: 0006-4971 (ISSN-L)
1528-0020
DOI: 10.1182/blood-2008-03-077883
PMC: PMC2481536
OpenAlex: W2048719634
Cited by: 506
References: 101
Citations by year: 2026: 12 · 2025: 18 · 2024: 19 · 2023: 31 · 2022: 29 · 2021: 27 · 2020: 34 · 2019: 32 · 2018: 26 · 2017: 29 · 2016: 20 · 2015: 31 · 2014: 33 · 2013: 43 · 2012: 28
FWCI: 3.95
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Blood (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Yale University
National Institutes of Health
National Heart, Lung, and Blood Institute (T32HL007956, HL7956)
National Institute of Diabetes and Digestive and Kidney Diseases (P01DK032094, DK56267, R01DK056267, DK32094)
Topics: Health Sciences › Medicine › Hematology › Hematopoietic Stem Cell Transplantation
Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
Keywords: erythroblastic islands, erythropoiesis, erythroid progenitor cells, erythroblast enucleation, erythroid differentiation, erythropoietin, cell-matrix adhesion, feedback regulation, anemia of chronic disease, myelodysplastic syndrome, thalassemia, malarial anemia, stress erythropoiesis
MeSH terms: Bone Marrow, Cell Adhesion, Erythroblasts, Erythropoiesis, Extracellular Matrix, Humans, Macrophages, Feedback, Physiological

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Erythroblastic islands: niches for erythropoiesis

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