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Ypel4-null Mice Display Secondary Polycythemia Associated with Ovalocytosis and Lower Band 3 Protein Levels on Red Blood Cells

ABSTRACT: Ypel4-null Mice Display Secondary Polycythemia Associated with Ovalocytosis and Lower Band 3 Protein Levels on Red Blood Cells

PROVIDER: PRJNA721452 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14218183.fastq.gz	Fastqsanger.gz
	SRR14218184.fastq.gz	Fastqsanger.gz
	SRR14218185.fastq.gz	Fastqsanger.gz
	SRR14218186.fastq.gz	Fastqsanger.gz
	SRR14218187.fastq.gz	Fastqsanger.gz

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Ypel4-null Mice Display Secondary Polycythemia Associated with Ovalocytosis and Lower Band 3 Protein Levels on Red Blood Cells

Project description:The YPEL family genes are highly conserved across a diverse range of eukaryotic organisms and thus potentially involved in essential cellular processes. Ypel4, one of five YPEL family gene orthologs in mouse and human, is highly and specifically expressed in late terminal erythroid differentiation. In this study, we investigated the role of Ypel4 in murine erythropoiesis, providing for the first time an in-depth description of a Ypel4-null phenotype in vivo. We demonstrated that the Ypel4-null mice displayed a secondary polycythemia with macro- and reticulocytosis. While lack of Ypel4 did not affect steady-state erythropoiesis in the bone marrow or spleen, the anemia-recovering capacity of Ypel4-null cells was diminished. Furthermore, Ypel4-null red blood cells (RBC) were cleared from the circulation at an increased rate, demonstrating an intrinsic defect of RBCs. Scanning electron micrographs revealed an ovalocytic morphology of Ypel4-null RBCs and functional testing confirmed reduced deformability. Even though Band 3 protein levels were shown to be reduced in Ypel4-null RBC membranes, we could not find support for a physical interaction between YPEL4 and the Band 3 protein. In conclusion, our findings provide crucial insights into the role of Ypel4 in preserving normal red cell membrane functionality.

2021-08-11 | GSE171959 | GEO

Investigating the proteome of red blood cells and reticulocytes in Polycythemia Vera and Essential Thrombocythemia

Project description:The project aims at comparing the effect of the JAK2V617F mutation on protein expression in human erythroid cells in the context of Polycythemia Vera and Essential Thrombocythemia

2022-02-17 | PXD029965 | Pride

Quantitative Analysis of the erythrocyte membrane proteins in polycythemia vera patients treated with hydroxycarbamide

Project description:Polycythemia vera (PV) is a myeloproliferative disorder arising in pluripotent stem cells that causes an abnormal erythrocyte mass. More than 90% of PV patients have a mutation in JAK2 protein that is closely associated with the erythrocyte membrane. We report findings on quantitative analysis of the erythrocyte membrane proteins differentially regulated in PV patients treated with hydroxycarbamide.</br>Kottahachchi et al., EuPA Open Proteomics 7, 43-53</br>Quantitative analysis of the erythrocyte membrane proteins in polycythemia vera patients treated with hydroxycarbamide</br>DOI:10.1016/j.euprot.2015.04.001</br><a href="http://www.sciencedirect.com/science/article/pii/S2212968515000100">http://www.sciencedirect.com/science/article/pii/S2212968515000100</a>

2015-05-11 | PXD001532 | Pride

25 kDa band from HSPA1A immunoprecipitation

Project description:HSPA1A was immunoprecipitated from WT and TorsinKO HeLa cells. A band around 27 kDa was identified uniquely in TorsinKO samples and for identification, this band was extracted.

2022-08-25 | PXD036266 | Pride

Gene Expression Profiling of High Altitude Polycythemia in Han Chinese migrated to Qinghai-Tibetan Plateau

Project description:Long term-exposed to high altitude, the increased numbers of red blood cells tend to stabilize to a certain extend in most people, but someone will occur over-increasing in number of red blood cells, which cause a serious of clinical symptoms and signs, and this is high altitude polycythemia. EPO-EPOR system may be the main reasons for erythroid progenitor cell proliferation and differentiation in early exposion to plateau, but, in the late, there may be other factors involved in the regulation of erythropoiesis in bone marrow, multiple factors working together lead to excessive red blood cell proliferation. We compared gene expression profiling of leukocytes in peripheral blood from high altitude polycythemia patients with those from matched controls.

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white band disease-infected Acropora cervicornis bacteria

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Differential cytokine network profile in polycythemia vera and secondary polycythemia.

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TFPI from Erythroblasts Drives Heme Production in Central Macrophages Promoting Erythropoiesis in Polycythemia Vera

Project description:Erythropoietic homeostasis is coordinated by erythroblast development and challenged by a number of genetic diseases including polycythemia vera. Erythroblasts and central macrophages form erythroblastic islands to provide a specific environment for erythropoiesis. However, how central macrophages interplay with erythroblasts during erythropoiesis remains to be further clarified. In this study, we found that erythroid-specific TFPI knockout decreased the number of erythroblasts under both steady-state and stress conditions, and the function of TFPI in erythropoiesis was mediated by macrophages. TFPI affects the downstream heme synthesis pathway of central macrophages, as shown by RNA sequencing analysis, and the deletion of TFPI reduced the heme content of macrophages by inhibiting ferrochelatase (Fech) expression. Our results show that TFPI plays an important role in the regulation of erythropoiesis and reveal a new mechanism of interplay between erythroblasts and macrophages. TFPI will also provide a new potential treatment strategy for polycythemia vera.

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Alpha kinase 3 signaling at the M-band maintains sarcomere integrity and proteostasis in striated muscle

Project description:Muscle contraction is driven by the molecular machinery of the sarcomere. While the constituent components of the sarcomere are well characterized, it is less clear how the activity and turnover of sarcomeric proteins is regulated. In particular, phosphorylation is critical regulator of muscle function. Thus, identification of regulatory kinases is key to understanding the sarcomere function. Pathogenic variants in alpha kinase 3 (ALPK3) cause cardiomyopathy and musculoskeletal disease, but little is known about this atypical kinase. Here we show that ALPK3 localizes to the M-Band of the sarcomere and define the ALPK3-dependent phosphoproteome. ALPK3 deficiency disrupted sarcomeric organization and calcium kinetics in hPSC-derived cardiomyocytes and reduced force generation in cardiac organoids. Phosphoproteomic profiling identified ALPK3-dependant phospho-peptides that were enriched for sarcomeric components of the M-band and the ubiquitin-binding protein SQSTM1. Analysis of the ALPK3 interactome confirmed binding to M-band proteins including SQSTM1. Importantly, in hPSC-derived cardiomyocytes modeling ALPK3 deficiency and cardiomyopathic ALPK3 mutations, sarcomeric organization and M-band localization of SQSTM1 were abnormal. These data suggest ALPK3 has an integral role in maintaining sarcomere integrity and proteostasis in striated muscle. We propose this mechanism may underly disease pathogenesis in patients with ALPK3 variants.

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