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Journal articles on the topic 'Eph-receptor A4'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

Aasheim, Hans-Christian, Else Munthe, Steinar Funderud, Erlend B. Smeland, Klaus Beiske, and Ton Logtenberg. "A splice variant of human ephrin-A4 encodes a soluble molecule that is secreted by activated human B lymphocytes." Blood 95, no. 1 (January 1, 2000): 221–30. http://dx.doi.org/10.1182/blood.v95.1.221.001k01_221_230.

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Ephrin-A4 is a ligand for the erythropoietin-producing hepatocellular (Eph) receptor family of tyrosine kinases. We have identified a secreted form of ephrin-A4, denoted ephrin-A4 (s), which is encoded by an alternatively spliced mRNA and is produced by in vivo activated B cells in tonsils. Blood B cells secrete ephrin-A4 (s) upon stimulation via the B-cell antigen receptor. A subpopulation of tonsil cells in the crypts with a dendritic cell phenotype was shown to express EphA2, an Eph receptor tyrosine kinase that was found to be capable of binding an ephrin-A4 immunoglobulin chimeric protein. We conclude that ephrin-A4 (s) may play a role in the interaction between activated B lymphocytes and dendritic cells in human tonsils. (Blood. 2000;95:221-230)

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2

Aasheim, Hans-Christian, Else Munthe, Steinar Funderud, Erlend B. Smeland, Klaus Beiske, and Ton Logtenberg. "A splice variant of human ephrin-A4 encodes a soluble molecule that is secreted by activated human B lymphocytes." Blood 95, no. 1 (January 1, 2000): 221–30. http://dx.doi.org/10.1182/blood.v95.1.221.

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Abstract Ephrin-A4 is a ligand for the erythropoietin-producing hepatocellular (Eph) receptor family of tyrosine kinases. We have identified a secreted form of ephrin-A4, denoted ephrin-A4 (s), which is encoded by an alternatively spliced mRNA and is produced by in vivo activated B cells in tonsils. Blood B cells secrete ephrin-A4 (s) upon stimulation via the B-cell antigen receptor. A subpopulation of tonsil cells in the crypts with a dendritic cell phenotype was shown to express EphA2, an Eph receptor tyrosine kinase that was found to be capable of binding an ephrin-A4 immunoglobulin chimeric protein. We conclude that ephrin-A4 (s) may play a role in the interaction between activated B lymphocytes and dendritic cells in human tonsils. (Blood. 2000;95:221-230)

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3

Xiaoli, Liu, Xuan Zhou, Yuan Zuo, Lulu Xu, Jinfang Zhang, Na Xu, Bintao Huang, Xiaozhen Xiao, Yuanlu Huang, and Qingfeng Du. "Eph-A4 Plays a Important Role in Metastasis and Invasive Activity of Myeloid Leukemia Cells." Blood 120, no. 21 (November 16, 2012): 4819. http://dx.doi.org/10.1182/blood.v120.21.4819.4819.

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Abstract Abstract 4819 The Eph receptors are found in a wide range of cancers and correlate with metastasis. However, their precise role in cancer has only started to be addressed. In this study, we investigated the role of Eph-A4 receptor in metastasis and invasive activity of myeloid leukemia cells. We fisr tested the expression of Eph-A4 in eight primary myeloid leukemias imclulding four with extramedullary metastasis and four without it, and leukemia cell line K562 by Real-time PCR and western blotting, then found that Eph- A4 was wildly expressed in myeloid Leukemia cells, especially in myeloid leukemia cells with high invasive activity. To further clarified the question, the stable over-expressing Eph-A4 cell line (K562-EphA4) based the wild K562 cell and pGC lentivirus vector were established to declare the metastasis and invasive activity in myeloid leukemia cells in vitro by trans-well migration assay. The results indicated that the mRNA level and protein expression of Eph-A4 were significantly increased in myeloid leukemias with extramedullary metastasis and K562 cells compared to those without it (P<0.05).After we successfully established the stable over-expressing Eph-A4 cell line, we verified its mRNA level and protein expression were both significantly increased ((P<0.05).Furthermore, RhoA and Rac1/cdc42, which are important adhesion molecules and related to metastasis and invasive activity were both highly expressed in K562-EphA4 cells compared to wild K562 cells (P<0.05). Moreover, the trans-well migration assay showed that cells that migrated to lower chambers and matrigel hydrogel were both increased in K562-EphA4 cells compared to wild K562 cells (5.22±2.11*104/ml vs 13.56±2.70*104 /ml P<0.000;18.07±3.15/cm2 vs 28.53±2.50/cm2P<0.000 respectively). Our findings suggest that Eph- A4 is likely to play an important role in the regulation the of myeloid Leukemia through the control of RhoA and Rac1/cdc42 associated signaling, migration and invasive activity, and therefore may represent a novel target for cancer treatment. Disclosures: No relevant conflicts of interest to declare.

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4

Bowden, Thomas A., A. Radu Aricescu, Joanne E. Nettleship, Christian Siebold, Nahid Rahman-Huq, Raymond J. Owens, David I. Stuart, and E. Yvonne Jones. "Structural Plasticity of Eph Receptor A4 Facilitates Cross-Class Ephrin Signaling." Structure 17, no. 10 (October 2009): 1386–97. http://dx.doi.org/10.1016/j.str.2009.07.018.

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5

Bowden, Thomas A., A. Radu Aricescu, Joanne E. Nettleship, Christian Siebold, Nahid Rahman-Huq, Raymond J. Owens, David I. Stuart, and E. Yvonne Jones. "Structural Plasticity of Eph-Receptor A4 Facilitates Cross-Class Ephrin Signaling." Structure 17, no. 12 (December 2009): 1679. http://dx.doi.org/10.1016/j.str.2009.11.004.

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6

MUNTHE, Else, and Hans-Christian AASHEIM. "Characterization of the human ephrin-A4 promoter." Biochemical Journal 366, no. 2 (September 1, 2002): 447–58. http://dx.doi.org/10.1042/bj20011693.

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Expression of the ephrin-A4 ligand, a family member of ligands binding the Eph receptor tyrosine kinases, is induced after an antigen–receptor stimulation of lymphocytes. To understand the transcription regulation of the ephrin-A4 gene, its promoter was identified and regulating elements were characterized. The ephrin-A4 promoter contains cis elements directing the cell-specific expression. By deletion studies, three specific regions, which were contributing to the transcription activity in lymphoid cells, were localized. In one of these regions, an inverted CCAAT box was identified and shown to bind the transcription activator nuclear factor-Y (NF-Y). The importance of NF-Y binding for the ephrin-A4 promoter activity is shown by a total abrogation of promoter activity after destruction of its binding site. NF-Y binding and activity are also crucially dependent on the integrity of the surrounding sequence. In addition, electrophoretic mobility-shift assay and serial-mutation analysis of the two remaining regulating regions revealed cis regulatory elements contributing to the transcription activity of the ephrin-A4 promoter.

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7

Kuang, Shao-Qing, Hao Bai, Zhi-Hong Fang, Gonzalo Lopez, Hui Yang, Weigang Tong, Zack Z. Wang, and Guillermo Garcia-Manero. "Aberrant DNA methylation and epigenetic inactivation of Eph receptor tyrosine kinases and ephrin ligands in acute lymphoblastic leukemia." Blood 115, no. 12 (March 25, 2010): 2412–19. http://dx.doi.org/10.1182/blood-2009-05-222208.

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Eph receptors and their ephrin ligands are involved in normal hematopoietic development and tumorigenesis. Using methylated CpG island amplification/DNA promoter microarray, we identified several EPH receptor and EPHRIN genes as potential hypermethylation targets in acute lymphoblastic leukemia (ALL). We subsequently studied the DNA methylation status of the Eph/ephrin family by bisulfite pyrosequencing. Hypermethylation of EPHA2, -A4, -A5, -A6, -A7, -A10, EPHB1, -B2, -B3, -B4, EFNA1, -A3, -A5, and EFNB1 and -B2 genes was detected in leukemia cell lines and primary ALL bone marrow samples. Expression analysis of EPHB4, EFNB2, and EFNA5 genes demonstrated that DNA methylation was associated with gene silencing. We cloned the promoter region of EPHB4 and demonstrated that promoter hypermethylation can result in EPHB4 transcriptional silencing. Restoration of EPHB4 expression by lentiviral transduction resulted in reduced proliferation and apoptotic cell death in Raji cells in which EPHB4 is methylated and silenced. Finally, we demonstrated that phosphorylated Akt is down-regulated in Raji cells transduced with EPHB4. These results suggest that epigenetic silencing by hypermethylation of EPH/EPHRIN family genes contributes to ALL pathogenesis and that EPHB4 can function as a tumor suppressor in ALL.

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8

Ding, Linlin, Yaodong Shen, Jing Ni, Yiqing Ou, Yangyu Ou, and Hong Liu. "EphA4 promotes cell proliferation and cell adhesion–mediated drug resistance via the AKT pathway in multiple myeloma." Tumor Biology 39, no. 3 (March 2017): 101042831769429. http://dx.doi.org/10.1177/1010428317694298.

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Eph receptor A4 (EphA4), a member of the erythropoietin-producing hepatocellular (Eph) family, has been reported to upregulate in several tumors. However, the role of EphA4 in multiple myeloma has not been clarified yet. In this study, we found that EphA4 promoted proliferation of multiple myeloma cells via the regulation of cell cycle. Besides, EphA4 was closely related to cell adhesion of multiple myeloma cells and promoted cell adhesion–mediated drug resistance by enhancing the phosphorylation levels of Akt (p-AKT) expression in multiple myeloma. More interestingly, we discovered that EphA4 can interact with cyclin-dependent kinase 5 (CDK5) and regulate its expression in multiple myeloma. CDK5 has been reported to be overexpressed in multiple myeloma which mediated bortezomib resistance and also participated in AKT pathway. And we have also proved the fact. So, we supposed that EphA4 interacted with CDK5 and promoted its expression which in turn enhanced p-AKT expression and promoted cell adhesion–mediated drug resistance in multiple myeloma. Therefore, this study clarifies the molecular mechanism of cell adhesion–mediated drug resistance and may be useful in identifying potential target for treatment of multiple myeloma.

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9

Patel, Ketan, Helen Makarenkova, and Han-Sung Jung. "The role of long range, local and direct signalling molecules during chick feather bud development involving the BMPs, Follistatin and the Eph receptor tyrosine kinase Eph-A4." Mechanisms of Development 86, no. 1-2 (August 1999): 51–62. http://dx.doi.org/10.1016/s0925-4773(99)00107-0.

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10

Takano, Hironobu, Toru Nakamura, Takahiro Tsuchikawa, Toshihiro Kushibiki, Kouji Hontani, Kazuho Inoko, Mizuna Takahashi, et al. "Inhibition of Eph receptor A4 by 2,5-dimethylpyrrolyl benzoic acid suppresses human pancreatic cancer growing orthotopically in nude mice." Oncotarget 6, no. 38 (October 19, 2015): 41063–76. http://dx.doi.org/10.18632/oncotarget.5729.

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11

Theocharis, Stamatios, Jerzy Klijanienko, Constantinos Giaginis, Paraskevi Alexandrou, Efstratios Patsouris, and Xavier Sastre-Garau. "Ephrin Receptor (Eph) -A1, -A2, -A4 and -A7 Expression in Mobile Tongue Squamous Cell Carcinoma: Associations with Clinicopathological Parameters and Patients Survival." Pathology & Oncology Research 20, no. 2 (September 11, 2013): 277–84. http://dx.doi.org/10.1007/s12253-013-9692-3.

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12

Yan, Yan, Yue-Chen Luo, Hai-Ying Wan, Jun Wang, Pei-Pei Zhang, Min Liu, Xin Li, Shengping Li, and Hua Tang. "MicroRNA-10a is involved in the metastatic process by regulating Eph tyrosine kinase receptor A4-Mediated epithelial-mesenchymal transition and adhesion in hepatoma cells*." Hepatology 57, no. 2 (January 8, 2013): 667–77. http://dx.doi.org/10.1002/hep.26071.

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13

Cilloni, Daniela, Francesca Arruga, Sonia Carturan, Francesca Messa, Monica Pradotto, Ilaria Defilippi, Marisa Pautasso, et al. "EphA3 Kinase Is Constitutively Activated in Chronic Myeloid Leukaemia during Progression to Accelerated and Blast Crisis and It Could Represent a New Molecular Target." Blood 112, no. 11 (November 16, 2008): 1092. http://dx.doi.org/10.1182/blood.v112.11.1092.1092.

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Abstract Eph receptors tyrosine kinases are involved in many key developmental processes. Ephs are overexpressed or mutated in solid tumours suggesting their possible role in oncogenesis. The majority of the genes and processes involved in CML progression are still unknown. The aim of this study was to investigate the role of EphA3 in CML progression and to explore the possibility to selectively target EphA3 with a monoclonal antibody. The expression of EphA3 and ligands were analyzed by RQ-PCR in 92 samples from 76 CML patients and in 38 healthy controls. 56 patients were in chronic phase (CP) enrolled in TOPS (Cortes, EHA, 2008) studies, 10 in accelerated phase (AP) and 10 in blast crisis (BC). In 5 patients and 10 healthy subjects EphA3 was studied also in enriched CD34+ population. Protein expression and localization were examined using Western Blot and immunofluorescence using specific antibodies. EphA3 expression in CD34+ cells were analyzed by FACS. The effects of EphA3 overexpression were studied by transfecting EphA3 plasmid in 293T e COS cells. In addition, sequencing of EphA3 TK domain was performed in 45 EphA3+ patients. BM, PB and CD34+ cells from CP CML patients expressed very low levels of EphA3, similar to normal controls with a median of 2−Δ ΔCt of 0,0018. By contrast, during the advanced phases of disease (AP and BC) we found high transcript levels (mean of 2−Δ ΔCt 43 and 67 respectively). Moreover, purified CD34+ CML cells presented significantly higher levels as compared to the unfractioned sample (p=0,001). RT-PCR showed no increase of the expression of the ligands Ephrin A2,A3,A4,A5 and B2, all of them able to bind to the receptor EphA3. WB and immunofluorescence confirmed the presence of phosphorylated protein in EphA3 in AP and BC CML cells. Western Blot and immunofluorescence confirmed the presence and the high level of phophorylation of EphA3 protein in AP and BC, but not in CP cells. EphA3 transfection into normal cells results in loss of adhesion, cell rounding and increased proliferation. Incubation of CML cells or transfected cells with a specific antibody able to block the EphA3 receptor induced a significant reduction of proliferation (31±4% of reduction in primary cells and 45±9% in transfected cells), it reduced colony growth (median value of 34,2 vs 76,5) and mainly, it changes the adhesion properties. The antibody did not induced any significant change of proliferation or colony growth in CP cells and normal controls. Finally, no kinase domain mutations were found in EphA3 overexpressing cells. In conclusion, our experimental data have shown that EphA3 was abnormally expressed in cells derived from advanced stage CML. The ectopic expression of EphA3, as demonstrated in our experimental system is responsible for increased proliferation and loss of cell adhesion. The inhibition of EphA3 induced by a specific antibody results in proliferation and colony growth inhibition. Although preliminary, our findings suggest that EphA3 may represent a potential candidate for a molecular therapy in advanced phase of chronic myeloid leukaemia. This investigation was conducted by CML Correlative Studies Network (CCSN), TOPS, which is sponsored by Novartis Oncology

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14

"EPH receptor A4 (EPHA4)." Science-Business eXchange 5, no. 37 (September 2012): 984. http://dx.doi.org/10.1038/scibx.2012.984.

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15

"EPH receptor A4 (EPHA4); β-amyloid (Aβ)." Science-Business eXchange 7, no. 29 (July 2014): 869. http://dx.doi.org/10.1038/scibx.2014.869.

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16

Giaginis, Constantinos, Nikolaos Tsoukalas, Evangelos Bournakis, Paraskevi Alexandrou, Nikolaos Kavantzas, Efstratios Patsouris, and Stamatios Theocharis. "Ephrin (Eph) receptor A1, A4, A5 and A7 expression in human non-small cell lung carcinoma: associations with clinicopathological parameters, tumor proliferative capacity and patients’ survival." BMC Clinical Pathology 14, no. 1 (February 4, 2014). http://dx.doi.org/10.1186/1472-6890-14-8.

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