scholarly journals Evidence for a role of NF- B in the survival of hematopoietic cells mediated by interleukin 3 and the oncogenic TEL/platelet-derived growth factor receptor   fusion protein

1998 ◽  
Vol 95 (14) ◽  
pp. 8081-8086 ◽  
Author(s):  
F. Besancon ◽  
A. Atfi ◽  
C. Gespach ◽  
Y. E. Cayre ◽  
M.-F. Bourgeade
Keyword(s):  
Growth Factor ◽  
Fusion Protein ◽  
Hematopoietic Cells ◽  
Growth Factor Receptor ◽  
Platelet Derived Growth Factor ◽  
Interleukin 3

The Role of Platelet-Derived Growth Factor Receptor in Eotaxin Signaling of Eosinophils

2006 ◽  
Vol 140 (1) ◽  
pp. 28-34 ◽  
Author(s):  
Tetsuya Adachi ◽  
Satoko Hanaka ◽  
Tomoko Yano ◽  
Koichi Yamamura ◽  
Hisanao Yoshihara ◽  
...  
Keyword(s):  
Growth Factor ◽  
Growth Factor Receptor ◽  
Platelet Derived Growth Factor

scholarly journals Postnatal Tendon Growth and Remodeling Requires Platelet-Derived Growth Factor Receptor Signaling

2017 ◽  
Author(s):  
Kristoffer B Sugg ◽  
James F Markworth ◽  
Nathaniel P Disser ◽  
Andrew M Rizzi ◽  
Jeffrey R Talarek ◽  
...  
Keyword(s):  
Growth Factor ◽  
Biological Activities ◽  
Growth Factor Receptor ◽  
Normal Growth ◽  
Platelet Derived Growth Factor ◽  
Growth And Remodeling ◽  
Fibroblast Migration ◽  
Membrane Type ◽  
And Migration

ABSTRACTPlatelet-derived growth factor receptor (PDGFR) signaling plays an important role in the fundamental biological activities of many cells that compose musculoskeletal tissues. However, little is known about the role of PDGFR signaling during tendon growth and remodeling in adult animals. Using the hindlimb synergist ablation model of tendon growth, our objectives were to determine the role of PDGFR signaling in the adaptation of tendons subjected to a mechanical growth stimulus, as well as to investigate the biological mechanisms behind this response. We demonstrate that both PDGFRs, PDGFRα and PDGFRβ, are expressed in tendon fibroblasts, and that the inhibition of PDGFR signaling suppresses the normal growth of tendon tissue in response to mechanical growth cues due to defects in fibroblast proliferation and migration. We also identify that membrane type-1 matrix metalloproteinase (MT1-MMP) as an essential proteinase for the migration of tendon fibroblasts through their extracellular matrix. Furthermore, we report that MT1-MMP translation is regulated by PI3K/Akt signaling, while ERK1/2 controls post-translational trafficking of MT1-MMP to the plasma membrane of tendon fibroblasts. Taken together, these findings demonstrate that PDGFR signaling is necessary for postnatal tendon growth and remodeling, and that MT1-MMP is a critical mediator of tendon fibroblast migration and a potential target for the treatment of tendon injuries and diseases.

The Jak2 V617F Oncogene Associated with Polycythemia Vera Requires a Functional FERM Domain for Transformation and for Expression of the Myc and Pim Proto-Oncogenes.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 3611-3611
Author(s):  
Martin Sattler ◽  
Brian J. Crowley ◽  
Jeffrey R. Gonneville ◽  
Jeremy Ho ◽  
Heidi H. Hudon ◽  
...  
Keyword(s):  
Growth Factor ◽  
Polycythemia Vera ◽  
Point Mutation ◽  
Hematopoietic Cells ◽  
Growth Factor Receptor ◽  
Jak2 V617f ◽  
Ferm Domain ◽  
Constitutive Activation ◽  
Epo Receptor

Abstract The V617F activating point mutation in Jak2 has been shown to be associated with a proportion of patients with myeloproliferative disorders, including polycythemia vera, essential thrombocythemia, and idiopathic myelofibrosis. In normal hematopoietic cells, Jak2 signals only when associated with a growth factor receptor (such as the Epo receptor), but the role of receptors in transformation by Jak2V617F has been controversial. Constructs expressing wild type or Jak2V617F, with and without a point mutation in the FERM domain (Y114A) required for receptor binding, were introduced into BaF3 cells already expressing a human Epo receptor. These cells were then evaluated for growth factor independence, response to growth factors, and activation of several critical Jak2 signaling pathways. We found that, whereas BaF3-EpoR cells are readily transformed by Jak2V617F to Epo-independence, the addition of the FERM domain mutation blocked transformation to factor independence. Also, the FERM domain was required for induction of reactive oxygen species by Jak2V617F. Further, while cells expressing Jak2V617F had constitutive activation of STAT5, cells expressing Jak2 V617F/Y114A did not, suggesting that signaling is defective at a very proximal level. In addition, Jak2V617F induced expression of the Myc and Pim proto-oncogenes, which are known to cooperate in the transformation of hematopoietic cells. The expression of both proteins was dependent on a functional FERM domain. Finally, we evaluated the role of active STAT5 in transformation of BaF3 cells by introducing a STAT5 mutant that is constitutively activated, and found that activation of STAT5, by itself, was sufficient to induce Jak2V617F-dependent downstream targets believed to be critical for transformation, including Myc and Pim. Overall, our results suggest that constitutive activation of Jak2 requires an intact FERM domain for a transforming phenotype, and is necessary for activation of the major target of Jak2, STAT5. These results also suggest that small molecules that target Jak2, the FERM domain, or STAT5 would have activity in diseases associated with V617F mutations.

Role of platelet derived growth factor receptor (PDGFR) over-expression and angiogenesis in ependymoma

2012 ◽  
Vol 111 (2) ◽  
pp. 169-176 ◽  
Author(s):  
Lucas Moreno ◽  
Sergey Popov ◽  
Alexa Jury ◽  
Saffa Al Sarraj ◽  
Chris Jones ◽  
...  
Keyword(s):  
Growth Factor ◽  
Growth Factor Receptor ◽  
Platelet Derived Growth Factor ◽  
Over Expression

scholarly journals Redox regulation of platelet-derived-growth-factor-receptor: Role of NADPH-oxidase and c-Src tyrosine kinase

2005 ◽  
Vol 1745 (2) ◽  
pp. 166-175 ◽  
Author(s):  
Serena Catarzi ◽  
Chiara Biagioni ◽  
Elisa Giannoni ◽  
Fabio Favilli ◽  
Tommaso Marcucci ◽  
...  
Keyword(s):  
Growth Factor ◽  
Nadph Oxidase ◽  
Tyrosine Kinase ◽  
Redox Regulation ◽  
Growth Factor Receptor ◽  
Platelet Derived Growth Factor ◽  
Src Tyrosine Kinase
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