scholarly journals The Crucial Role of c-Src Tyrosine Kinase in Bone Metabolism

10.5772/37995 ◽  
2012 ◽  
Author(s):  
Barbara Peruzzi ◽  
Nadia Rucci ◽  
Anna Teti
Keyword(s):  
Tyrosine Kinase ◽  
Bone Metabolism ◽  
Crucial Role ◽  
Src Tyrosine Kinase

scholarly journals Crucial role of Mer tyrosine kinase in the maintenance of SIGN-R1+ marginal zone macrophages

2018 ◽  
Vol 96 (3) ◽  
pp. 298-315
Author(s):  
Chetna Soni ◽  
Stephanie L Schell ◽  
Melinda J Fasnacht ◽  
Sathi Babu Chodisetti ◽  
Ziaur SM Rahman
Keyword(s):  
Tyrosine Kinase ◽  
Crucial Role ◽  
Marginal Zone ◽  
Mer Tyrosine Kinase ◽  
Marginal Zone Macrophages

scholarly journals The Role of Hypoxia and SRC Tyrosine Kinase in Glioblastoma Invasiveness and Radioresistance

Cancers ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 2860 ◽  
Author(s):  
Filippo Torrisi ◽  
Nunzio Vicario ◽  
Federica M. Spitale ◽  
Francesco P. Cammarata ◽  
Luigi Minafra ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Poor Prognosis ◽  
High Rate ◽  
Crucial Importance ◽  
Src Tyrosine Kinase ◽  
Complete Surgical Resection ◽  
Radiation Induced ◽  
Proliferation And Invasion

Advances in functional imaging are supporting neurosurgery and radiotherapy for glioblastoma, which still remains the most aggressive brain tumor with poor prognosis. The typical infiltration pattern of glioblastoma, which impedes a complete surgical resection, is coupled with a high rate of invasiveness and radioresistance, thus further limiting efficient therapy, leading to inevitable and fatal recurrences. Hypoxia is of crucial importance in gliomagenesis and, besides reducing radiotherapy efficacy, also induces cellular and molecular mediators that foster proliferation and invasion. In this review, we aimed at analyzing the biological mechanism of glioblastoma invasiveness and radioresistance in hypoxic niches of glioblastoma. We also discussed the link between hypoxia and radiation-induced radioresistance with activation of SRC proto-oncogene non-receptor tyrosine kinase, prospecting potential strategies to overcome the current limitation in glioblastoma treatment.

scholarly journals p130Cas mediates the transforming properties of the anaplastic lymphoma kinase

Blood ◽  
2005 ◽  
Vol 106 (12) ◽  
pp. 3907-3916 ◽  
Author(s):  
Chiara Ambrogio ◽  
Claudia Voena ◽  
Andrea D. Manazza ◽  
Roberto Piva ◽  
Ludovica Riera ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Anaplastic Lymphoma Kinase ◽  
Kinase Activity ◽  
Adaptor Protein ◽  
Dominant Negative ◽  
Lymphoid Cells ◽  
Src Tyrosine Kinase ◽  
Anaplastic Lymphoma ◽  
Proteomic Approach

Translocations of the anaplastic lymphoma kinase (ALK) gene have been described in anaplastic large-cell lymphomas (ALCLs) and in stromal tumors. The most frequent translocation, t(2;5), generates the fusion protein nucleophosmin (NPM)–ALK with intrinsic tyrosine kinase activity. Along with transformation, NPM-ALK induces morphologic changes in fibroblasts and lymphoid cells, suggesting a direct role of ALK in cell shaping. In this study, we used a mass-spectrometry–based proteomic approach to search for proteins involved in cytoskeleton remodeling and identified p130Cas (p130 Crk-associated substrate) as a novel interactor of NPM-ALK. In 293 cells and in fibroblasts as well as in human ALK-positive lymphoma cell lines, NPM-ALK was able to bind p130Cas and to induce its phosphorylation. Both of the effects were dependent on ALK kinase activity and on the adaptor protein growth factor receptor–bound protein 2 (Grb2), since no binding or phosphorylation was found with the kinase-dead mutant NPM-ALKK210R or in the presence of a Grb2 dominant-negative protein. Phosphorylation of p130Cas by NPM-ALK was partially independent from Src (tyrosine kinase pp60c-src) kinase activity, as it was still detectable in Syf-/- cells. Finally, p130Cas-/- (also known as Bcar1-/-) fibroblasts expressing NPM-ALK showed impaired actin filament depolymerization and were no longer transformed compared with wild-type cells, indicating an essential role of p130Cas activation in ALK-mediated transformation.

Src tyrosine kinase is the trigger but not the mediator of ischemic preconditioning

2001 ◽  
Vol 281 (3) ◽  
pp. H1066-H1074 ◽  
Author(s):  
Reiji Hattori ◽  
Hajime Otani ◽  
Takamichi Uchiyama ◽  
Hiroji Imamura ◽  
Jianhua Cui ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Ischemic Preconditioning ◽  
Tyrosine Kinases ◽  
Src Kinase ◽  
Src Tyrosine Kinase ◽  
Kinase Activation ◽  
Rat Hearts ◽  
Perfused Rat Hearts ◽  
Src Activation

The signal cascade that triggers and mediates ischemic preconditioning (IPC) remains unclear. The present study investigated the role of the Src family of tyrosine kinases in IPC. Isolated and buffer-perfused rat hearts underwent IPC with three cycles of 5-min ischemia and 5-min reperfusion, followed by 30-min ischemia and 120-min reperfusion. The Src tyrosine kinase family-selective inhibitor PP1 was administered between 45 and 30 min before ischemia (early PP1 treatment) or for 15 min before IPC [early PP1-preconditioning (PC) treatment]. PP1 was also administered for 5 min before the sustained ischemia (late PP1 treatment) or after IPC (late PP1-PC treatment). Src kinase was activated after 30 min of ischemia in both the membrane and cytosolic fractions. Src kinase was also activated by IPC but was attenuated after the sustained ischemia. Early and late PP1 treatment inhibited Src activation after the sustained ischemia and reduced infarct size. Early PP1-PC inhibited Src activation after IPC but not after the sustained ischemia and blocked cardioprotection afforded by IPC. Late PP1-PC treatment abrogated IPC-induced activation of Src and protein kinase C (PKC)-ε in the membrane but not in the cytosolic fraction. This treatment modality abrogated Src activation after the sustained ischemia and failed to block cardioprotection afforded by IPC. These results suggest that Src kinase activation mediates ischemic injury but triggers IPC in the position either upstream of or parallel to membrane-associated PKC-ε.

Role of the PKCα-c-Src tyrosine kinase pathway in the mediation of p120-catenin degradation in ventilator-induced lung injury

Respirology ◽  
2016 ◽  
Vol 21 (8) ◽  
pp. 1404-1410 ◽  
Author(s):  
Tao Zhao ◽  
Hongwei Zhao ◽  
Gang Li ◽  
Shengfa Zheng ◽  
Mengjie Liu ◽  
...  
Keyword(s):  
Lung Injury ◽  
Tyrosine Kinase ◽  
Src Tyrosine Kinase ◽  
P120 Catenin ◽  
Ventilator Induced Lung Injury ◽  
Kinase Pathway

scholarly journals Role of c-Src Tyrosine Kinase in G Protein-coupled Receptorand Gβγ Subunit-mediated Activation of Mitogen-activated Protein Kinases

1996 ◽  
Vol 271 (32) ◽  
pp. 19443-19450 ◽  
Author(s):  
Louis M. Luttrell ◽  
Brian E. Hawes ◽  
Tim van Biesen ◽  
Deirdre K. Luttrell ◽  
Timothy J. Lansing ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Protein Kinases ◽  
G Protein ◽  
Src Tyrosine Kinase ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
G Protein Coupled

scholarly journals The role of water molecules in the binding of class I and II peptides to the SH3 domain of the Fyn tyrosine kinase

2016 ◽  
Vol 72 (9) ◽  
pp. 707-712 ◽  
Author(s):  
Ana Camara-Artigas ◽  
Emilia Ortiz-Salmeron ◽  
Montserrrat Andujar-Sánchez ◽  
Julio Bacarizo ◽  
Jose Manuel Martin-Garcia
Keyword(s):  
Tyrosine Kinase ◽  
Conformational Changes ◽  
Sh3 Domain ◽  
Class I ◽  
Water Molecules ◽  
Src Tyrosine Kinase ◽  
Sh3 Domains ◽  
Binding Interface ◽  
Fyn Tyrosine Kinase

Interactions of proline-rich motifs with SH3 domains are present in signal transduction and other important cell processes. Analysis of structural and thermodynamic data suggest a relevant role of water molecules in these protein–protein interactions. To determine whether or not the SH3 domain of the Fyn tyrosine kinase shows the same behaviour, the crystal structures of its complexes with two high-affinity synthetic peptides, VSL12 and APP12, which are class I and II peptides, respectively, have been solved. In the class I complexes two water molecules were found at the binding interface that were not present in the class II complexes. The structures suggest a role of these water molecules in facilitating conformational changes in the SH3 domain to allow the binding of the class I or II peptides. In the third binding pocket these changes modify the cation–π and salt-bridge interactions that determine the affinity of the binding. Comparison of the water molecules involved in the binding of the peptides with previous reported hydration spots suggests a different pattern for the SH3 domains of the Src tyrosine kinase family.

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