Protein Phosphatase 2A Catalytic Subunit α (PP2Acα) Maintains Survival of Committed Erythroid Cells in Fetal Liver Erythropoiesis through the STAT5 Pathway
Open accessAbstract
Suppression of programmed cell death is critical for the final maturation of red blood cells and depends largely on the anti-apoptotic effects of EpoR-STAT5-Bcl-x(L) signaling. As the major eukaryotic serine/threonine phosphatase, protein phosphatase 2A (PP2A) regulates multiple cellular processes, including apoptosis. However, whether PP2A plays a role in preventing erythroid cells from undergoing apoptosis remains to be elucidated. We conditionally inactivated the catalytic subunit α of PP2A (PP2Acα), which is the predominant form of PP2Ac, during early embryonic hematopoiesis. Loss of PP2Acα in hematopoietic cells perturbed definitive erythropoiesis characterized by fetal liver atrophy, reduced Ter119(+) cell number, abnormal expression patterns of molecular markers, less colony formation, and a reduction in definitive globin expression. Levels of erythropoiesis-promoting cytokines and initial seeding with hematopoietic progenitors remained unchanged in PP2Acα(TKO) fetal livers. We noted impaired expansion of the fetal erythroid compartment, which was associated with increased apoptosis of committed erythroid cells. Mechanistically, PP2Acα depletion markedly reduced Tyr(694) phosphorylation of STAT5 and expression of Bcl-x(L). Unexpectedly, PP2Acα-deficient embryos did not manifest any early embryonic vascular defects. Collectively, these data provide direct loss-of-function evidence demonstrating the importance of PP2Acα for the survival of committed erythroid cells during fetal liver erythropoiesis.
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Primitive erythropoiesis was normal, but definitive erythropoiesis was impaired, as witnessed by increased pro-erythroblasts, decreased erythroid colony- and blast-forming units, and reduced β maj/min-globin expression.
“Specifically, primitive erythropoiesis was normal, but definitive erythropoiesis was impaired, as witnessed by an increased number of pro-erythroblasts, a decreased number of erythroid colony-and blast-forming units and reduced expression of β maj/min -globin.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [38]
At E12.5 and E14.5, total cellularity of fetal liver was dramatically reduced, with a pronounced 90% reduction in erythrocytes, while other hematopoietic lineages appeared in normal numbers.
“At E12.5 and E14.5, total cellularity of fetal liver was dramatically reduced, with a pronounced 90% reduction in erythrocytes, while other hematopoietic lineages appeared in normal numbers.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [38]
Conditional knockout of Cα in early hematopoietic and endothelial cells caused embryos to look pale and die at E12.5 due to defects in hematopoiesis, despite incomplete knockout and 35% remaining PP2A activity in fetal livers.
“Another function of PP2A during embryonic development was revealed in a conditional KO model of Cα in early hematopoietic and endothelial cells [38].Homozygously targeted embryos looked pale and died at E12.5 due to defects in hematopoiesis, despite an incomplete KO and 35% remaining PP2A activity in fetal livers.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [38]
Increased apoptosis of committed erythroid cells was observed, correlating with decreased STAT5 phosphorylation (Tyr694) and decreased Bcl-XL expression in basal and EPO-stimulated cells.
“In addition, increased apoptosis of committed erythroid cells was observed, correlating with decreased STAT5 phosphorylation (Tyr694) and decreased Bcl-X L expression in basal and EPO-stimulated cells [38].”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [38]
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Cites
Apoptosis in the Pathogenesis and Treatment of Disease
Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524 · see citing works
Generalized lacZ expression with the ROSA26 Cre reporter strain
Soriano, P. (1999) · Nature Genetics · doi:10.1038/5007 · Cited by 5,237 · see citing works
bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
Boise, L., González‐García, M., Postema, C. E., Ding, L., Lindsten, T., Turka, L. A., Mao, X., Núñez, G., & Thompson, C. B. (1993) · Cell · doi:10.1016/0092-8674(93)90508-n · Cited by 3,089 · see citing works
Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586 · see citing works
Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,890 · see citing works
Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/bj3530417 · Cited by 1,392 · see citing works
Massive Cell Death of Immature Hematopoietic Cells and Neurons in Bcl-x-Deficient Mice
Motoyama, N., Wang, F., Roth, K. A., Sawa, H., Nakayama, K., Nakayama, K., Negishi, I., Senju, S., Zhang, Q., Fujii, S., et al. (1995) · Science · doi:10.1126/science.7878471 · Cited by 1,164 · see citing works
Wu, H., Liu, X., Jaenisch, R., & Lodish, H. F. (1995) · Cell · doi:10.1016/0092-8674(95)90234-1 · Cited by 1,007 · see citing works
Jak2 Deficiency Defines an EssentialDevelopmental Checkpoint in DefinitiveHematopoiesis
Neubauer, H. J., Cumano, A., Müller, M. M., Wu, H., Huffstadt, U., & Pfeffer, K. (1998) · Cell · doi:10.1016/s0092-8674(00)81168-x · Cited by 923 · see citing works
Efficacy of Lenalidomide in Myelodysplastic Syndromes
List, A., Kurtin, S., Roe, D. J., Buresh, A., Mahadevan, D., Fuchs, D., Rimsza, L., Heaton, R., Knight, R., & Zeldis, J. B. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa041668 · Cited by 880 · see citing works
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 841 · see citing works
Erythropoietin: Physiology and Pharmacology Update
Fisher, J. W. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800101 · Cited by 700 · see citing works
Fetal Anemia and Apoptosis of Red Cell Progenitors in Stat5a−/−5b−/− Mice
Socolovsky, M., Fallon, A. E. J., Wang, S., Brugnara, C., & Lodish, H. F. (1999) · Cell · doi:10.1016/s0092-8674(00)81013-2 · Cited by 695 · see citing works
Ineffective erythropoiesis in Stat5a−/−5b−/− mice due to decreased survival of early erythroblasts
Socolovsky, M., Nam, H.-S., Fleming, M. D., Haase, V. H., Brugnara, C., & Lodish, H. F. (2001) · Blood · doi:10.1182/blood.v98.12.3261 · Cited by 674 · see citing works
Ikuta, K., & Weissman, I. L. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.4.1502 · Cited by 637 · see citing works
Ikuta, K., Kina, T., MacNeil, I., Uchida, N., Peault, B., Chien, Y.-H., & Weissman, I. L. (1990) · Cell · doi:10.1016/0092-8674(90)90262-d · Cited by 583 · see citing works
Springer, T. A., Galfré, G., Secher, D. S., & Milstein, C. (1978) · European Journal of Immunology · doi:10.1002/eji.1830080802 · Cited by 576 · see citing works
Angiogenesis selectively requires the p110α isoform of PI3K to control endothelial cell migration
Graupera, M., Guillermet‐Guibert, J., Foukas, L. C., Phng, L., Cain, R. J., Salpekar, A., Pearce, W. P., Meek, S. E., Millán, J., Cutillas, P. R., et al. (2008) · Nature · doi:10.1038/nature06892 · Cited by 521 · see citing works
Cui, Y., Riedlinger, G., Miyoshi, K., Tang, W., Li, C., Deng, C., Robinson, G. W., & Hennighausen, L. G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8037-8047.2004 · Cited by 497 · see citing works
Self-citationConditional Vascular Cell Adhesion Molecule 1 Deletion in Mice
Koni, P. A., Joshi, S. K., Temann, U.-A., Olson, D. L., Burkly, L. C., & Flavell, R. A. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.6.741 · Cited by 482 · see citing works
Nocka, K. H., Majumder, S., Chabot, B., Ray, P., Cervone, M., Bernstein, A., & Besmer, P. (1989) · Genes & Development · doi:10.1101/gad.3.6.816 · Cited by 473 · see citing works
González‐García, M., Ballestero, R. P., Ding, L., Duan, L., Boise, L., Thompson, C. B., & Núñez, G. (1994) · Development · doi:10.1242/dev.120.10.3033 · Cited by 430 · see citing works
Stat5a/b are essential for normal lymphoid development and differentiation
Yao, Z., Cui, Y., Watford, W. T., Bream, J. H., Yamaoka, K., Hissong, B. D., Li, D., Durum, S. K., Jiang, Q., Bhandoola, A., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507350103 · Cited by 391 · see citing works
Gregory, T. C., Yu, C., Ma, A. I., Orkin, S. H., Blobel, G. A., & Weiss, M. J. (1999) · Blood · doi:10.1182/blood.v94.1.87.413k41_87_96 · Cited by 366 · see citing works
Turning cells red: signal transduction mediated by erythropoietin
Richmond, T. D., Chohan, M., & Barber, D. L. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.01.007 · Cited by 349 · see citing works
CIS3/SOCS-3 Suppresses Erythropoietin (EPO) Signaling by Binding the EPO Receptor and JAK2
Sasaki, A. T., Yasukawa, H., Shouda, T., Kitamura, T., Đikić, I., & Yoshimura, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003456200 · Cited by 341 · see citing works
Ceramide Induces Bcl2 Dephosphorylation via a Mechanism Involving Mitochondrial PP2A
Ruvolo, P. P., Deng, X., Ito, T., Carr, B. K., & May, W. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20296 · Cited by 338 · see citing works
Protein phosphatase 2A: a panoply of enzymes
Virshup, D. M. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)00074-5 · Cited by 330 · see citing works
Critical Role of the TIE2 Endothelial Cell Receptor in the Development of Definitive Hematopoiesis
Takakura, N., Huang, X.-L., Naruse, T., Hamaguchi, I., Dumont, D., Yancopoulos, G. D., & Suda, T. (1998) · Immunity · doi:10.1016/s1074-7613(00)80665-2 · Cited by 302 · see citing works
PP2A: Unveiling a Reluctant Tumor Suppressor
Mumby, M. (2007) · Cell · doi:10.1016/j.cell.2007.06.034 · Cited by 295 · see citing works
Interaction of the erythropoietin and stem-cell-factor receptors
Wu, H., Klingmüller, U., Besmer, P., & Lodish, H. F. (1995) · Nature · doi:10.1038/377242a0 · Cited by 295 · see citing works
Role of stem cell migration in initiation of mouse foetal liver haemopoiesis
Johnson, G. R., & Moore, M. A. S. (1975) · Nature · doi:10.1038/258726a0 · Cited by 273 · see citing works
Bax Protein Expression Is Increased in Alzheimerʼs Brain
Su, J. H., Deng, G., & Cotman, C. W. (1997) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199701000-00009 · Cited by 239 · see citing works
Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit Cα
Götz, J., Probst, A., Ehler, E., Hemmings, B., & Kues, W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12370 · Cited by 220 · see citing works
Yoshimura, A., Ichihara, M., Kinjyo, I., Moriyama, M., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Hara, T., & Miyajima, A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00443.x · Cited by 213 · see citing works
Pim and Akt oncogenes are independent regulators of hematopoietic cell growth and survival
Hammerman, P. S., Fox, C. J., Birnbaum, M. J., & Thompson, C. B. (2005) · Blood · doi:10.1182/blood-2004-09-3706 · Cited by 206 · see citing works
Wagner, K., Claudio, E., Rucker, E. B., Riedlinger, G., Broussard, C., Schwartzberg, P. L., Siebenlist, U. K., & Hennighausen, L. G. (2000) · Development · doi:10.1242/dev.127.22.4949 · Cited by 205 · see citing works
The Roles of Bcl-XL and Apopain in the Control of Erythropoiesis by Erythropoietin
Gregoli, P. A., & Bondurant, M. C. (1997) · Blood · doi:10.1182/blood.v90.2.630 · Cited by 165 · see citing works
Whitelaw, E., Tsai, S., Hogben, P., & Orkin, S. H. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.12.6596-6606.1990 · Cited by 163 · see citing works
Kelley, L., Koury, M., Bondurant, M. C., Koury, S. T., Sawyer, S. T., & Wickrema, A. (1993) · Blood · doi:10.1182/blood.v82.8.2340.2340 · Cited by 154 · see citing works
Regulation of Protein Phosphatase 2A Activity by Caspase-3 during Apoptosis
Santoro, M. F., Annand, R. R., Robertson, M. M., Peng, Y.-W., Brady, M., Mankovich, J. A., Hackett, M. C., Ghayur, T., Walter, G., Wong, W. W., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13119 · Cited by 152 · see citing works
Deng, X., Ito, T., Carr, B. K., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.34157 · Cited by 142 · see citing works
Motoyama, N., Kimura, T., Takahashi, T., Watanabe, T., & Nakano, T. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.11.1691 · Cited by 134 · see citing works
Cloning and molecular characterization of mouse bcl-x in B and T lymphocytes.
Fang, W., Rivard, J. J., Mueller, D. L., et al. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.153.10.4388 · Cited by 132 · see citing works
Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes.
Ariño, J., Woon, C.-W., Brautigan, D. L., Miller, T. B., & Johnson, G. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4252 · Cited by 130 · see citing works
Zang, H., Sato, K., Nakajima, H., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.12.3156 · Cited by 114 · see citing works
Schlaeger, T. M., Mikkola, H. K. A., Gekas, C., Helgadóttir, H., & Orkin, S. H. (2005) · Blood · doi:10.1182/blood-2004-11-4467 · Cited by 105 · see citing works
Tissue‐specific expression of mRNAs encoding α‐ and β‐catalytic subunits of protein phosphatase 2A
Khew-Goodall, Y., & Hemmings, B. A. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80493-9 · Cited by 102 · see citing works
Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes
Khew‐Goodall, Y., Mayer, R. E., Maurer, F., Stone, S. R., & Hemmings, B. A. (1991) · Biochemistry · doi:10.1021/bi00215a014 · Cited by 101 · see citing works
Alvarado-Kristensson, M., & Andersson, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409718200 · Cited by 101 · see citing works
Serine/threonine protein phosphatases and regulation of K-Cl cotransport in human erythrocytes
Bize, I., Güvenç, B., Robb, A., et al. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.277.5.c926 · Cited by 82 · see citing works
Hamaguchi, I., Huang, X.-L., Takakura, N., et al. (1999) · Blood · doi:10.1182/blood.v93.5.1549 · Cited by 81 · see citing works
Hematopoietic stem cells express Tie-2 receptor in the murine fetal liver
Hsu, H.-C., Ema, H., Osawa, M., Nakamura, Y., Suda, T., & Nakauchi, H. (2000) · Blood · doi:10.1182/blood.v96.12.3757.h8003757_3757_3762 · Cited by 67 · see citing works
Differential Roles of SOCS Family Members in EpoR Signal Transduction
Jegalian, A. G., & Wu, H. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002760274863 · Cited by 66 · see citing works
Wu, F. Y., & Wilson, J. X. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn246 · Cited by 66 · see citing works
Chida, D., Miura, O., Yoshimura, A., & Miyajima, A. (1999) · Blood · doi:10.1182/blood.v93.5.1567 · Cited by 59 · see citing works
Pim-1 kinase protects hematopoietic FDC cells from genotoxin-induced death
Pircher, T. J., Zhao, S., Geiger, J. N., Joneja, B., & Wojchowski, D. M. (2000) · Oncogene · doi:10.1038/sj.onc.1203684 · Cited by 56 · see citing works
Kutcher, M., Klagsbrun, M., & Mamluk, R. (2004) · The FASEB Journal · doi:10.1096/fj.04-2320fje · Cited by 43 · see citing works
Lacombe, C. (1996) · New England Journal of Medicine · doi:10.1056/nejm199603073341012 · Cited by 34 · see citing works
Protein phosphatase 2A contributes to the cardiac dysfunction induced by endotoxemia
Marshall, M. J., Anilkumar, N. P., Layland, J., et al. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp037 · Cited by 30 · see citing works
Boogaerts, M., Mittelman, M., & Vaupel, P. W. (2005) · Oncology · doi:10.1159/000088285 · Cited by 20 · see citing works
SH2-Inositol Phosphatase 1 Negatively Influences Early Megakaryocyte Progenitors
Perez, L. E., Desponts, C., Parquet, N., & Kerr, W. G. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003565 · Cited by 16 · see citing works
STAT5 acts as a repressor to regulate early embryonic erythropoiesis
Schmerer, M. W., Torregroza, I., Pascal, A., Umbhauer, M., & Evans, T. (2006) · Blood · doi:10.1182/blood-2006-05-022137 · Cited by 13 · see citing works
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- Chen et al AJP May 2011, Vol. 178, No. 5
- Neubauer H, Cumano A, Muller M, Wu H, Huffstadt U, Pfeffer K: Jak2 deficiency defines an essential developmental checkpoint in defini- tive hematopoiesis. Cell 1998, 93:397-409
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Gu, P., Qi, X., Zhou, Y., Wang, Y., & Gao, X. (2012) · genesis · doi:10.1002/dvg.20815 · Cited by 51 · see citing works
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Tang, A., Shi, P., Song, A., Zou, D., Zhou, Y., Gu, P., Huang, Z., Wang, Q., Lin, Z., & Gao, X. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1175256 · Cited by 29 · see citing works
Self-citationLu, N., Liu, Y., Tang, A., Chen, L., Miao, D., & Yuan, X. (2015) · BioMed Research International · doi:10.1155/2015/794862 · Cited by 21 · see citing works
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Huang, C., Liu, T., Wang, Q., Hou, W., Zhou, C., Song, Z., Shi, Y. S., Gao, X., Chen, G., Yin, Z., et al. (2020) · Cerebral Cortex · doi:10.1093/cercor/bhaa042 · Cited by 14 · see citing works
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- Authors
- Chen, W., Gu, P., Jiang, X., Ruan, H.-B., Li, C., & Gao, X.
- Affiliations
- Model Animal Research Center (CN)
- Corresponding author
- Gao, Xiang
- Venue
- The American Journal of Pathology
- Publisher
- Elsevier BV
- Published
- 2011-05
- Volume
- 178
- Issue
- 5
- Pages
- 2333-2343
- ISSN
- 0002-9440 (ISSN-L)
- PMC
- PMC3081176
- OpenAlex
- W1996756747
- Cited by
- 30
- References
- 63
- Citations by year
- 2025: 2 · 2024: 5 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 1 · 2016: 5 · 2015: 4
- FWCI
- 0.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- American Journal Of Pathology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Science and Technology of the People's Republic of China (2005CB522501, 2006BAI23B00, 2006CB943500)
- National Science Foundation (30825024)
- Topics
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Health Sciences › Medicine › Hematology › Hematopoietic Stem Cell Transplantation
- Keywords
- protein phosphatase 2A, erythropoiesis, fetal liver, apoptosis, STAT5 phosphorylation, Bcl-xL, erythropoietin receptor signaling, definitive erythropoiesis, conditional knockout, hematopoiesis
- MeSH terms
- Protein Phosphatase 2C, Animals, Cell Separation, Embryo, Mammalian, Erythropoiesis, Flow Cytometry, Immunohistochemistry, Liver, Phosphoprotein Phosphatases, Blotting, Western, Signal Transduction, Reverse Transcriptase Polymerase Chain Reaction, Erythroid Cells, STAT5 Transcription Factor, Mice
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