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Journal articles on the topic 'Megakaryopoiesis'

Author: Grafiati

Published: 4 June 2021

Last updated: 21 February 2023

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1

Geddis, Amy E. "Megakaryopoiesis." Seminars in Hematology 47, no. 3 (July 2010): 212–19. http://dx.doi.org/10.1053/j.seminhematol.2010.03.001.

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2

Tozawa, Keiichi, Yukako Ono-Uruga, and Yumiko Matsubara. "Megakaryopoiesis." Clinical & Experimental Thrombosis and Hemostasis 1, no. 2 (November 10, 2014): 54–58. http://dx.doi.org/10.14345/ceth.14014.

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3

Jeanpierre, Sandrine, Franck Emmanuel Nicolini, Bastien Kaniewski, Charles Dumontet, Ruth Rimokh, Alain Puisieux, and Véronique Maguer-Satta. "BMP4 regulation of human megakaryocytic differentiation is involved in thrombopoietin signaling." Blood 112, no. 8 (October 15, 2008): 3154–63. http://dx.doi.org/10.1182/blood-2008-03-145326.

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Abstract Activin A, BMP2, and BMP4, 3 members of the transforming growth factor-β family, are involved in the regulation of hematopoiesis. Here, we explored the role of these molecules in human megakaryopoiesis using an in vitro serum-free assay. Our results highlight for the first time that, in the absence of thrombopoietin, BMP4 is able to induce CD34+ progenitor differentiation into megakaryocytes through all stages. Although we have previously shown that activin A and BMP2 are involved in erythropoietic commitment, these molecules have no effect on human megakaryopoietic engagement and dif

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4

Blobel, Gerd A. "Krüppeling megakaryopoiesis." Blood 110, no. 12 (December 1, 2007): 3823–24. http://dx.doi.org/10.1182/blood-2007-09-110999.

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5

KOZUMA, Yukinori. "Megakaryopoiesis and apoptosis." Japanese Journal of Thrombosis and Hemostasis 23, no. 6 (2012): 552–58. http://dx.doi.org/10.2491/jjsth.23.552.

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6

Jubinsky, Paul T. "Megakaryopoiesis and thrombocytosis." Pediatric Blood & Cancer 44, no. 1 (2004): 45–46. http://dx.doi.org/10.1002/pbc.20243.

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7

Feng, Gege, Wen Cui, Wenyu Cai, Tiejun Qin, Yue Zhang, Zefeng Xu, Liwei Fang, et al. "Impact of Megakaryocyte Morphology on Prognosis of Persons with Myelodysplastic Syndromes." Blood 126, no. 23 (December 3, 2015): 2876. http://dx.doi.org/10.1182/blood.v126.23.2876.2876.

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Abstract Purpose: To describe the morphological evolution of megakaryocytic dysplasia by developing a systematic classification and evaluate the impact of our classification of dys-megakaryopoiesis on prognosis of persons with MDS. Patients and methods: 423 consecutive patients who had received no prior therapy with MDS diagnosed from January 2000 to April 2014 were enrolled. Follow-up data were available for 371 subjects (88%). Date of last follow-up was December 15, 2014 or date of last contact. Median follow-up was 22 months (range, 1¨C180 months). Subjects with lower-risk MDS fall into Rev

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8

Liu, Zhi-Jian, and Martha Sola-Visner. "Neonatal and adult megakaryopoiesis." Current Opinion in Hematology 18, no. 5 (September 2011): 330–37. http://dx.doi.org/10.1097/moh.0b013e3283497ed5.

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9

Behrens, Kira, and Warren S. Alexander. "Cytokine control of megakaryopoiesis." Growth Factors 36, no. 3-4 (July 4, 2018): 89–103. http://dx.doi.org/10.1080/08977194.2018.1498487.

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10

Szalai, G., A. C. LaRue, and D. K. Watson. "Molecular mechanisms of megakaryopoiesis." Cellular and Molecular Life Sciences 63, no. 21 (August 11, 2006): 2460–76. http://dx.doi.org/10.1007/s00018-006-6190-8.

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11

Nicolini, Franck E., Sandrine Jeanpierre, Bastien Kaniewski, Charles Dumontet, Ruth Rimokh, Alain Puisieux, and Véronique Maguer-Satta. "The Bone Morphogenetic Protein (BMP)-4 Is Involved in the Regulation of Human Megakaryocytic Differentiation during Thrombopoietin Signaling." Blood 112, no. 11 (November 16, 2008): 1339. http://dx.doi.org/10.1182/blood.v112.11.1339.1339.

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Abstract It has been shown in the past that Activin A, BMP-2 and BMP-4, three members of the TGF-β family, are involved in the regulation of hematopoiesis and particularly erythropoiesis, in humans. In this study, we explored the role of these molecules in human megakaryopoiesis using an in vitro serum-free assay initiated with purified normal CD34+ human bone marrow (BM) cells (from allogeneic BM donors), that allows the analysis of the impact of such molecules on all stages of megakaryocytic differentiation. We could demonstrate for the first time, that in the absence of thrombopoietin (TPO)

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12

Zhao, Hong-Yan, Qi Wen, Zhong-Shi Lyu, Shu-Qian Tang, Yuan-Yuan Zhang, Meng Lyu, Yu Wang, et al. "M2 Macrophages, but Not M1 Macrophages, Support Megakaryopoiesis Via up-Regulating PI3K-AKT Pathway." Blood 136, Supplement 1 (November 5, 2020): 1. http://dx.doi.org/10.1182/blood-2020-136562.

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Background Megakaryopoiesis and platelets production intensely depend on bone marrow(BM) microenvironment. Our previous studies found that impaired BM microenvironment and dysfunctional megakaryopoiesis are responsible for the occurrence of prolonged isolated thrombocytopenia (PT), which is defined as the engraftment of all peripheral blood cell lines other than a platelet count less than 20×109/L or a dependence on platelet transfusions for more than 60 days following allo-HSCT(BBMT 2014; BBMT 2017; Brit J Haematol 2018; Am J Hematol 2018). As an important component of the BM microenvironment

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13

YUZURIHA, Akinori, and Koji ETO. "Hematopoietic stem cells to megakaryopoiesis." Japanese Journal of Thrombosis and Hemostasis 27, no. 5 (2016): 519–25. http://dx.doi.org/10.2491/jjsth.27.519.

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14

Kostyak, John C., та Satya P. Kunapuli. "PKCθ is dispensable for megakaryopoiesis". Platelets 26, № 6 (23 червня 2014): 610–11. http://dx.doi.org/10.3109/09537104.2014.926474.

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15

Tsuji, Kohichiro, Kenji Muraoka та Tatsutoshi Nakahata. "Interferon-γ and Human Megakaryopoiesis". Leukemia & Lymphoma 31, № 1-2 (січень 1998): 107–13. http://dx.doi.org/10.3109/10428199809057590.

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16

Viklicky, Vladimir, Antonin Hradilek, and Jan Neuwirt. "ABNORMAL MEGAKARYOPOIESIS IN ACUTE LEUKAEMIA." British Journal of Haematology 68, no. 3 (March 1988): 393. http://dx.doi.org/10.1111/j.1365-2141.1988.tb04222.x.

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17

Hoyle, C., and F. G. J. Hayhoe. "ABNORMAL MEGAKARYOPOIESIS IN ACUTE LEUKAEMIA." British Journal of Haematology 68, no. 3 (March 1988): 393a—394. http://dx.doi.org/10.1111/j.1365-2141.1988.tb04223.x.

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18

Bluteau, O., T. Langlois, P. Rivera-Munoz, F. Favale, P. Rameau, G. Meurice, P. Dessen, et al. "Developmental changes in human megakaryopoiesis." Journal of Thrombosis and Haemostasis 11, no. 9 (September 2013): 1730–41. http://dx.doi.org/10.1111/jth.12326.

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19

Kaushansky, Kenneth. "Historical review: megakaryopoiesis and thrombopoiesis." Blood 111, no. 3 (February 1, 2008): 981–86. http://dx.doi.org/10.1182/blood-2007-05-088500.

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Abstract The study of thrombopoiesis has evolved greatly since an era when platelets were termed “the dust of the blood,” only about 100 years ago. During this time megakaryocytes were identified as the origin of blood platelets; marrow-derived megakaryocytic progenitor cells were functionally defined and then purified; and the primary regulator of the process, thrombopoietin, was cloned and characterized and therapeutic thrombopoietic agents developed. During this journey we continue to learn that the physiologic mechanisms that drive proplatelet formation can be recapitulated in cell-free sy

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20

Dupont, H., M. A. Dupont, J. Larrue, M. R. Boisseau, and H. Bricaud. "Megakaryopoiesis disturbances in atherosclerotic rabbits." Atherosclerosis 63, no. 1 (January 1987): 15–26. http://dx.doi.org/10.1016/0021-9150(87)90077-3.

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21

Johnson, Andrew D. "Pairing megakaryopoiesis methylation with PEAR1." Blood 128, no. 7 (August 18, 2016): 890–92. http://dx.doi.org/10.1182/blood-2016-06-723940.

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22

Liu, Zhi-Jian, James B. Bussel, Madhavi Lakkaraja, Francisca Ferrer-Marin, Cedric Ghevaert, Henry A. Feldman, Janice G. McFarland, Chaitanya Chavda, and Martha Sola-Visner. "Suppression of in vitro megakaryopoiesis by maternal sera containing anti-HPA-1a antibodies." Blood 126, no. 10 (September 3, 2015): 1234–36. http://dx.doi.org/10.1182/blood-2014-11-611020.

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Key Points Maternal sera containing anti-HPA-1a antibodies suppress in vitro megakaryopoiesis through induction of cell death. The degree of suppression of megakaryopoiesis is variable and is one of the factors determining the severity of neonatal thrombocytopenia.

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23

Kong, Xianguo, Lin Ma, Edward Chen, Chad Shaw, and Leonard Edelstein. "Identification of the Regulatory Elements and Target Genes of Megakaryopoietic Transcription Factor MEF2C." Thrombosis and Haemostasis 119, no. 05 (February 7, 2019): 716–25. http://dx.doi.org/10.1055/s-0039-1678694.

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AbstractMegakaryopoiesis produces specialized haematopoietic stem cells in the bone marrow that give rise to megakaryocytes which ultimately produce platelets. Defects in megakaryopoiesis can result in altered platelet counts and physiology, leading to dysfunctional haemostasis and thrombosis. Additionally, dysregulated megakaryopoiesis is also associated with myeloid pathologies. Transcription factors play critical roles in cell differentiation by regulating the temporal and spatial patterns of gene expression which ultimately decide cell fate. Several transcription factors have been describe

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24

Lambert, Michele P., Yuhuan Wang, Khalil H. Bdeir, Yvonne Nguyen, M. Anna Kowalska, and Mortimer Poncz. "Platelet factor 4 regulates megakaryopoiesis through low-density lipoprotein receptor–related protein 1 (LRP1) on megakaryocytes." Blood 114, no. 11 (September 10, 2009): 2290–98. http://dx.doi.org/10.1182/blood-2009-04-216473.

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Abstract Platelet factor 4 (PF4) is a negative regulator of megakaryopoiesis, but its mechanism of action had not been addressed. Low-density lipoprotein (LDL) receptor–related protein-1 (LRP1) has been shown to mediate endothelial cell responses to PF4 and so we tested this receptor's importance in PF4's role in megakaryopoiesis. We found that LRP1 is absent from megakaryocyte-erythrocyte progenitor cells, is maximally present on large, polyploidy megakaryocytes, and near absent on platelets. Blocking LRP1 with either receptor-associated protein (RAP), an antagonist of LDL family member recep

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25

Marziali, Giovanna, Valentina Lulli, Simona Coppola, Paolo Romania, Laura Fontana, Francesca Liuzzi, Mauro Biffoni, et al. "MicroRNAs 155, -221 and -222 Control Megakaryopoiesis at Progenitor and Precursor Level through Ets-1 Multitargeting." Blood 108, no. 11 (November 16, 2006): 1187. http://dx.doi.org/10.1182/blood.v108.11.1187.1187.

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Abstract It is generally accepted that microRNAs (miRs) control basic biological functions, such as cell proliferation and differentiation. However, only few targets of the ~ 300 known mammalian miRs have been validated so far, thus hampering delineation of miR-based control circuitries. Particularly, little is known on miR function in mammalian hematopoiesis. We have investigated by microarray and Northern blot evalutation miR expression profiles in human megakarypoiesis, as evaluated in cord blood hematopoietic progenitor cell (HPC) unilineage culture through the megakaryopoietic (MK) differ

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26

FUJITA, Rie, Hozumi MOTOHASHI, and Masayuki YAMAMOTO. "Transcriptional regulation of megakaryopoiesis and thrombopoiesis." Japanese Journal of Thrombosis and Hemostasis 23, no. 6 (2012): 539–43. http://dx.doi.org/10.2491/jjsth.23.539.

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27

Kostyak, John, C. "Megakaryopoiesis: Transcriptional Insights into Megakaryocyte Maturation." Frontiers in Bioscience 12, no. 1 (2007): 2050. http://dx.doi.org/10.2741/2210.

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28

Wijgaerts, Anouck, and Kathleen Freson. "Megakaryopoiesis under normal and pathological conditions." Hématologie 20, no. 6 (November 2014): 319–28. http://dx.doi.org/10.1684/hma.2014.0970.

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29

Freson, Kathleen, Chantal Thys, Christine Wittevrongel, Rita De Vos, Jos Vermylen, Marc F. Hoylaerts, and Chris Van Geet. "VPAC1 Receptor-Mediated Regulation of Megakaryopoiesis." Blood 104, no. 11 (November 16, 2004): 735. http://dx.doi.org/10.1182/blood.v104.11.735.735.

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Abstract Identification of the regulatory pathways that direct megakaryopoiesis and platelet production is essential for the development of novel strategies to treat life threatening bleeding complications in bone marrow suppressed patients. We demonstrated that megakaryocytes and platelets express the Gs-coupled VPAC1 receptor, for which both PACAP and VIP are specific agonists. We have further identified a bleeding tendency and found three copies of the PACAP gene in two related patients with severe mental retardation, responsible for elevated PACAP plasma levels and associated increased pla

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30

Raslova, H., W. Vainchenker, and I. Plo. "Eltrombopag, a potent stimulator of megakaryopoiesis." Haematologica 101, no. 12 (November 30, 2016): 1443–45. http://dx.doi.org/10.3324/haematol.2016.153668.

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31

Suraneni, P. K., and J. D. Crispino. "The Hippo-p53 pathway in megakaryopoiesis." Haematologica 101, no. 12 (November 30, 2016): 1446–48. http://dx.doi.org/10.3324/haematol.2016.156125.

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32

Bender, Markus, Silvia Giannini, Terese Jönsson, Renata Grozovsky, Hilary Christensen, Fred G. Pluthero, Walter H. Kahr, Karin M. Hoffmeister, and Hervé Falet. "Dynamin 2-Dependent Endocytosis Regulates Megakaryopoiesis." Blood 124, no. 21 (December 6, 2014): 339. http://dx.doi.org/10.1182/blood.v124.21.339.339.

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Abstract Dynamins are large and highly conserved GTPases involved in endocytosis and vesicle trafficking. Mutations K562E/del in the ubiquitous dynamin 2 (DNM2) have been associated with thrombocytopenia in humans. To determine the role of DNM2 in megakaryopoiesis we generated Dnm2fl/fl Pf4-Cre mice specifically lacking DNM2 in the megakaryocyte (MK) lineage. Dnm2fl/fl Pf4-Cre mice were viable, but had severe macrothrombocytopenia with moderately accelerated platelet clearance and prolonged bleeding due to poorly functional platelets. Dnm2-null bone marrow MKs had altered demarcation membrane

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33

Goldfarb, Adam. "A Mad(2) modification modulating megakaryopoiesis." Journal of Experimental Medicine 211, no. 12 (November 17, 2014): 2326–27. http://dx.doi.org/10.1084/jem.21112insight2.

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34

Nagasawa, Toshiro, Yuichi Hasegawa, Masaharu Kamoshita, Kouji Ohtani, Takuya Komeno, Takayoshi Itoh, Atsushi Shinagawa, Hiroshi Kojima, Haruhiko Ninomiya, and Tsukasa Abe. "Megakaryopoiesis in patients with cyclic thrombocytopenia." British Journal of Haematology 91, no. 1 (September 1995): 185–90. http://dx.doi.org/10.1111/j.1365-2141.1995.tb05267.x.

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35

Bernard, Jamie J., Kathryn E. Seweryniak, Anne D. Koniski, Sherry L. Spinelli, Neil Blumberg, Charles W. Francis, Mark B. Taubman, James Palis, and Richard P. Phipps. "Foxp3 Regulates Megakaryopoiesis and Platelet Function." Arteriosclerosis, Thrombosis, and Vascular Biology 29, no. 11 (November 2009): 1874–82. http://dx.doi.org/10.1161/atvbaha.109.193805.

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36

Wang, Q. "BUBR1 deficiency results in abnormal megakaryopoiesis." Blood 103, no. 4 (October 23, 2003): 1278–85. http://dx.doi.org/10.1182/blood-2003-06-2158.

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37

Matsumura, Itaru, and Yuzuru Kanakura. "Molecular Control of Megakaryopoiesis and Thrombopoiesis." International Journal of Hematology 75, no. 5 (June 2002): 473–83. http://dx.doi.org/10.1007/bf02982109.

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38

Kim, Minjung, Tami J. Kingsbury, and Curt I. Civin. "RAB14 Regulates Human Erythropoiesis and Megakaryopoiesis." Blood 128, no. 22 (December 2, 2016): 2661. http://dx.doi.org/10.1182/blood.v128.22.2661.2661.

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We recently reported that RAB GTPase 14 (RAB14) knockdown (KD) increased the frequency and total numbers of erythroid cells generated in vitro in response to erythropoietin (EPO) from either the TF1 human leukemia erythropoietic model cell line or from primary human CD34+ hematopoietic stem-progenitor cells (HSPCs). RAB14 overexpression (OE) had the opposite effect. Thus, RAB14 functions as an endogenous inhibitor of human erythropoiesis (Kim et al., Br. J. Haematol., 2015). In contrast to the greater cell numbers generated in the presence of EPO, RAB14 KD TF1 cells grown in standard culture m

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39

Jin, Q., Y. Ren, M. Wang, P. K. Suraneni, D. Li, J. D. Crispino, J. Fan, and Z. Huang. "Novel function of FAXDC2 in megakaryopoiesis." Blood Cancer Journal 6, no. 9 (September 2016): e478-e478. http://dx.doi.org/10.1038/bcj.2016.87.

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40

Kono, Tomoko, Harumi Mukai, Yukinori Kozuma, Hiroshi Kojima, and Haruhiko Ninomiya. "Functional Analysis of CD9 during Megakaryopoiesis." Blood 112, no. 11 (November 16, 2008): 891. http://dx.doi.org/10.1182/blood.v112.11.891.891.

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Abstract CD9 is a four transmembrane protein belonging to a tetraspanin family and regulates cell motility and adhesion. Several reports have indicated that CD9 form complexes with integrin including platelet fibrinogen receptor integrin aIIb-b III and involve in platelet function. We have previously reported that the c-myb knock down (KD) mice exhibited anemia and thrombocytopenia, and the expression level of CD9 mRNA was markdly increased in the c-myb KD mice. Reverse correlation of c-Myb expression with the CD9 gene expression was verified and agonistic antibody of CD9 stimulated megakaryoc

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41

Mosoyan, Goar, Kevin Eng, Craig Parker, Ronald Hoffman, and Camelia Iancu-Rubin. "Inhibition of telomerase impairs normal megakaryopoiesis." Experimental Hematology 42, no. 8 (August 2014): S39. http://dx.doi.org/10.1016/j.exphem.2014.07.144.

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42

Gao, Ai, Yuemin Gong, Fang Dong, Shihui Ma, Hui Cheng, Sha Hao, and Tao Cheng. "Defective megakaryopoiesis in acute myeloid leukemia." Experimental Hematology 53 (September 2017): S117. http://dx.doi.org/10.1016/j.exphem.2017.06.292.

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43

Oh, Doyeun, Seongmin Yoon, Seonyang Park, and Jeehyeon Bae. "Differential Regulations and Roles of Mcl-1 and Bcl-Xl during Megakaryopoiesis." Blood 112, no. 11 (November 16, 2008): 4727. http://dx.doi.org/10.1182/blood.v112.11.4727.4727.

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Abstract Backgrounds: Platelet plays an essential role in thrombosis and hemostasis and is produced from hematopoietic stem cells through a serious of differentiation and maturation processes called megakaryopoiesis. The major factor known to control platelet formation is thrombopoietin (TPO), but recently more proteins including apoptosis regulators have been reported to involve in megakaryopoiesis. Evolutionally conserved Bcl-2 family proteins are central regulators of apoptosis. Antiapoptotic Bcl-2 subfamily comprised of Bcl-xL, Mcl-1, Bcl-2, Bcl-w, and Bfl-1 plays a pivotal role in control

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44

Opalinska, Joanna B., Alexey Bersenev, Zhe Zhang, Alec A. Schmaier, John Choi, Yu Yao, Janine D'Souza, Wei Tong, and Mitchell J. Weiss. "MicroRNA expression in maturing murine megakaryocytes." Blood 116, no. 23 (December 2, 2010): e128-e138. http://dx.doi.org/10.1182/blood-2010-06-292920.

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Abstract MicroRNAs are small noncoding RNAs that regulate cellular development by interfering with mRNA stability and translation. We examined global microRNA expression during the differentiation of murine hematopoietic progenitors into megakaryocytes. Of 435 miRNAs analyzed, 13 were up-regulated and 81 were down-regulated. Many of these changes are consistent with miRNA profiling studies of human megakaryocytes and platelets, although new patterns also emerged. Among 7 conserved miRNAs that were up-regulated most strongly in murine megakaryocytes, 6 were also induced in the related erythroid

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45

Hitchcock, Ian S., Norma E. Fox, Nicolas Prévost, Katherine Sear, Sanford J. Shattil, and Kenneth Kaushansky. "Roles of focal adhesion kinase (FAK) in megakaryopoiesis and platelet function: studies using a megakaryocyte lineage–specific FAK knockout." Blood 111, no. 2 (January 15, 2008): 596–604. http://dx.doi.org/10.1182/blood-2007-05-089680.

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Focal adhesion kinase (FAK) plays a key role in mediating signaling downstream of integrins and growth factor receptors. In this study, we determined the roles of FAK in vivo by generating a megakaryocyte lineage–specific FAK-null mouse (Pf4-Cre/FAK-floxed). Megakaryocyte and platelet FAK expression was ablated in Pf4-Cre/FAK-floxed mice without affecting expression of the FAK homologue PYK2, although PYK2 phosphorylation was increased in FAK−/− megakaryocytes in response to fibrinogen. Megakaryopoiesis is greatly enhanced in Pf4-Cre/FAK-floxed mice, with significant increases in megakaryocyti

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46

Wang, Jialing, Xiaodan Liu, Haixia Wang, Lili Qin, Anhua Feng, Daoxin Qi, Haihua Wang, et al. "JMJD1C Regulates Megakaryopoiesis in In Vitro Models through the Actin Network." Cells 11, no. 22 (November 18, 2022): 3660. http://dx.doi.org/10.3390/cells11223660.

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The histone demethylase JMJD1C is associated with human platelet counts. The JMJD1C knockout in zebrafish and mice leads to the ablation of megakaryocyte–erythroid lineage anemia. However, the specific expression, function, and mechanism of JMJD1C in megakaryopoiesis remain unknown. Here, we used cell line models, cord blood cells, and thrombocytopenia samples, to detect the JMJD1C expression. ShRNA of JMJD1C and a specific peptide agonist of JMJD1C, SAH-JZ3, were used to explore the JMJD1C function in the cell line models. The actin ratio in megakaryopoiesis for the JMJDC modulation was also

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47

Chen, Hui, Min Zhou, Huiying Shu, Weiqing Su, Liuming Yang, Liang Li, Beng H. Chong, and Mo Yang. "Tanshinone Iia Inhibits Megakaryopoiesis in Immune Vasculitis." Blood 138, Supplement 1 (November 5, 2021): 4288. http://dx.doi.org/10.1182/blood-2021-152162.

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Abstract Introduction Tanshinone IIA, an active component of Danshen (Salvia miltiorrhiza), has been used for centuries to treat hypercoagulation-related diseases, which attributed to its anti-platelet and anti-inflammatory effects. However, the role of Tanshinone IIA in megakaryocytes, the precursor of platelet within the bone marrow, remains unclear. Therefore, the present study established a rabbit model with immune vasculitis to examine the effect of Tanshinone IIA on megakaryopoiesis and to identify the underlying mechanism(s). Methods Immune vasculitis was established in rabbits (3-4 wee

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48

Wagner, Thomas, Gerhard Bernaschek, and Klaus Geissler. "Inhibition of Megakaryopoiesis by Kell-Related Antibodies." New England Journal of Medicine 343, no. 1 (July 6, 2000): 72. http://dx.doi.org/10.1056/nejm200007063430120.

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49

Engelfriet, C. P., T. Wagner, G. Bernaschek, and K. Geissler. "Inhibition of Megakaryopoiesis by Kell-Related Antibodies." Vox Sanguinis 79, no. 4 (December 2000): 266. http://dx.doi.org/10.1046/j.1423-0410.2000.79402654.x.

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50

Tan, Ying-Xia, Hao Cui, Lu-Ming Wan, Feng Gong, Xiao Zhang, Israel Vlodavsky, and Jin-Ping Li. "Overexpression of heparanase in mice promoted megakaryopoiesis." Glycobiology 28, no. 5 (February 19, 2018): 269–75. http://dx.doi.org/10.1093/glycob/cwy011.

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