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Ying-shing Chan - One of the best experts on this subject based on the ideXlab platform.
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Tyrosine Kinase receptor immunoreactivity in trigeminal mesencephalic and motor neurons following transection of masseteric nerve of the rat.
Neuroscience, 2006Co-Authors: Fu-xing Zhang, Jin-lian Li, D.k.y. Shum, Ying-shing ChanAbstract:Neurotrophins are known to promote survival after neural injury. To determine the relative importance of Tyrosine Kinase Receptors on the survival of axotomized trigeminal nuclear neurons, we examined the temporal expression profile of Tyrosine Kinase A, Tyrosine Kinase B and Tyrosine Kinase C Receptors in the mesencephalic trigeminal nucleus and the motor trigeminal nucleus following transection of the masseteric nerve in rats. Axotomized neurons in these nuclei were retrogradely identified with FluoroGold. We found increase in Tyrosine Kinase A-immunoreactive mesencephalic trigeminal nucleus neurons in the second week after axotomy but no change in the number of Tyrosine Kinase A-immunoreactive motor trigeminal nucleus neurons. There was no change in the number of Tyrosine Kinase B-immunoreactive mesencephalic trigeminal nucleus neurons but the significant increase of Tyrosine Kinase B-immunoreactive motor trigeminal nucleus neurons throughout the period of observation (3 weeks) peaked at ∼1 week after axotomy. There was no alteration in the number of Tyrosine Kinase C-immunoreactive mesencephalic trigeminal nucleus neurons but significant increase in Tyrosine Kinase C-immunoreactive motor trigeminal nucleus neurons observable by 4 days post-axotomy was followed by decline to levels lower than the control in 2 weeks. Temporal changes in the expression of individual Tyrosine Kinase Receptors in mesencephalic trigeminal nucleus and motor trigeminal nucleus neurons following transection of the masseteric nerve suggest differential contribution of Tyrosine Kinase-specific neurotrophins to the survival of these neurons after axotomy.
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Tyrosine Kinase receptor immunoreactivity in trigeminal mesencephalic and motor neurons following transection of masseteric nerve of the rat.
Neuroscience, 2006Co-Authors: Fu-xing Zhang, D.k.y. Shum, Ch Lai, Ying-shing ChanAbstract:Neurotrophins are known to promote survival after neural injury. To determine the relative importance of Tyrosine Kinase Receptors on the survival of axotomized trigeminal nuclear neurons, we examined the temporal expression profile of Tyrosine Kinase A, Tyrosine Kinase B and Tyrosine Kinase C Receptors in the mesencephalic trigeminal nucleus and the motor trigeminal nucleus following transection of the masseteric nerve in rats. Axotomized neurons in these nuclei were retrogradely identified with FluoroGold. We found increase in Tyrosine Kinase A-immunoreactive mesencephalic trigeminal nucleus neurons in the second week after axotomy but no change in the number of Tyrosine Kinase A-immunoreactive motor trigeminal nucleus neurons. There was no change in the number of Tyrosine Kinase B-immunoreactive mesencephalic trigeminal nucleus neurons but the significant increase of Tyrosine Kinase B-immunoreactive motor trigeminal nucleus neurons throughout the period of observation (3 weeks) peaked at approximately 1 week after axotomy. There was no alteration in the number of Tyrosine Kinase C-immunoreactive mesencephalic trigeminal nucleus neurons but significant increase in Tyrosine Kinase C-immunoreactive motor trigeminal nucleus neurons observable by 4 days post-axotomy was followed by decline to levels lower than the control in 2 weeks. Temporal changes in the expression of individual Tyrosine Kinase Receptors in mesencephalic trigeminal nucleus and motor trigeminal nucleus neurons following transection of the masseteric nerve suggest differential contribution of Tyrosine Kinase-specific neurotrophins to the survival of these neurons after axotomy.
Adriana Ferreira - One of the best experts on this subject based on the ideXlab platform.
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Differential subcellular localization of Ror Tyrosine Kinase Receptors in cultured astrocytes.
Glia, 2004Co-Authors: Sabrina Paganoni, Kelsi L. Anderson, Adriana FerreiraAbstract:Ror1 and Ror2 belong to a family of Tyrosine Kinase Receptors that are highly conserved among species. They are expressed throughout the organism, including the central nervous system. In the present study, we analyzed the expression and subcellular localization of Ror1 and Ror2 in astrocytes by means of reverse transcription-polymerase chain reaction, Western blot analysis, and immunocytochemistry. Our results indicated that both Ror1 and Ror2 are readily detectable in cultured astrocytes. They also showed that Ror1 and Ror2 are associated with different components of the cytoskeleton. While Ror1 co-localized with F-actin along stress fibers, Ror2 partially co-localized with microtubules. In addition, our results suggest that Ror1 and Ror2 undergo different posttranslational modifications in cultured astrocytes. Ror1 is highly glycosylated in these cells. In contrast, no glycosylation was detected in Ror2. Taken together, these results suggest distinct roles for these Tyrosine Kinase Receptors in astrocytes. © 2004 Wiley-Liss, Inc.
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expression and subcellular localization of ror Tyrosine Kinase Receptors are developmentally regulated in cultured hippocampal neurons
Journal of Neuroscience Research, 2003Co-Authors: Sabrina Paganoni, Adriana FerreiraAbstract:Ror1 and Ror2 are two novel receptor Tyrosine Kinases that have been implicated in neuronal differentiation in Caenorhabditis elegans. As a first step toward elucidating their role in the mammalian brain, we analyzed their expression and localization patterns in hippocampal neurons. Our results showed that both Receptors are expressed from early stages of development and that their protein levels peak during periods of active synapse formation. Immunocytochemical analysis indicated that Ror1 and Ror2 are highly concentrated in the growth cones of immature neurons and are present throughout the somatodendritic compartment of mature hippocampal cells. Further analysis indicated that they are present not only in the cell membrane but also in Triton- and saponin-insoluble fractions, suggesting that they may be associated with both the cytoskeleton and membrane-bound organelles. Taken collectively, our results suggest that Ror1 and Ror2 might play a role during early stages of development in mammalian central neurons.
Fu-xing Zhang - One of the best experts on this subject based on the ideXlab platform.
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Tyrosine Kinase receptor immunoreactivity in trigeminal mesencephalic and motor neurons following transection of masseteric nerve of the rat.
Neuroscience, 2006Co-Authors: Fu-xing Zhang, Jin-lian Li, D.k.y. Shum, Ying-shing ChanAbstract:Neurotrophins are known to promote survival after neural injury. To determine the relative importance of Tyrosine Kinase Receptors on the survival of axotomized trigeminal nuclear neurons, we examined the temporal expression profile of Tyrosine Kinase A, Tyrosine Kinase B and Tyrosine Kinase C Receptors in the mesencephalic trigeminal nucleus and the motor trigeminal nucleus following transection of the masseteric nerve in rats. Axotomized neurons in these nuclei were retrogradely identified with FluoroGold. We found increase in Tyrosine Kinase A-immunoreactive mesencephalic trigeminal nucleus neurons in the second week after axotomy but no change in the number of Tyrosine Kinase A-immunoreactive motor trigeminal nucleus neurons. There was no change in the number of Tyrosine Kinase B-immunoreactive mesencephalic trigeminal nucleus neurons but the significant increase of Tyrosine Kinase B-immunoreactive motor trigeminal nucleus neurons throughout the period of observation (3 weeks) peaked at ∼1 week after axotomy. There was no alteration in the number of Tyrosine Kinase C-immunoreactive mesencephalic trigeminal nucleus neurons but significant increase in Tyrosine Kinase C-immunoreactive motor trigeminal nucleus neurons observable by 4 days post-axotomy was followed by decline to levels lower than the control in 2 weeks. Temporal changes in the expression of individual Tyrosine Kinase Receptors in mesencephalic trigeminal nucleus and motor trigeminal nucleus neurons following transection of the masseteric nerve suggest differential contribution of Tyrosine Kinase-specific neurotrophins to the survival of these neurons after axotomy.
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Tyrosine Kinase receptor immunoreactivity in trigeminal mesencephalic and motor neurons following transection of masseteric nerve of the rat.
Neuroscience, 2006Co-Authors: Fu-xing Zhang, D.k.y. Shum, Ch Lai, Ying-shing ChanAbstract:Neurotrophins are known to promote survival after neural injury. To determine the relative importance of Tyrosine Kinase Receptors on the survival of axotomized trigeminal nuclear neurons, we examined the temporal expression profile of Tyrosine Kinase A, Tyrosine Kinase B and Tyrosine Kinase C Receptors in the mesencephalic trigeminal nucleus and the motor trigeminal nucleus following transection of the masseteric nerve in rats. Axotomized neurons in these nuclei were retrogradely identified with FluoroGold. We found increase in Tyrosine Kinase A-immunoreactive mesencephalic trigeminal nucleus neurons in the second week after axotomy but no change in the number of Tyrosine Kinase A-immunoreactive motor trigeminal nucleus neurons. There was no change in the number of Tyrosine Kinase B-immunoreactive mesencephalic trigeminal nucleus neurons but the significant increase of Tyrosine Kinase B-immunoreactive motor trigeminal nucleus neurons throughout the period of observation (3 weeks) peaked at approximately 1 week after axotomy. There was no alteration in the number of Tyrosine Kinase C-immunoreactive mesencephalic trigeminal nucleus neurons but significant increase in Tyrosine Kinase C-immunoreactive motor trigeminal nucleus neurons observable by 4 days post-axotomy was followed by decline to levels lower than the control in 2 weeks. Temporal changes in the expression of individual Tyrosine Kinase Receptors in mesencephalic trigeminal nucleus and motor trigeminal nucleus neurons following transection of the masseteric nerve suggest differential contribution of Tyrosine Kinase-specific neurotrophins to the survival of these neurons after axotomy.
Fabrice Lalloué - One of the best experts on this subject based on the ideXlab platform.
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Sortilin limits EGFR signaling by promoting its internalization in lung cancer
Nature Communications, 2017Co-Authors: Hussein Al Akhrass, Thomas Naves, François Vincent, Boris Melloni, Marie-odile Jauberteau-marchan, Amandine Magnaudeix, Karine Durand, François Bertin, Fabrice LallouéAbstract:Tyrosine Kinase Receptors such as the epidermal growth factor receptor (EGFR) transduce information from the microenvironment into the cell and activate homeostatic signaling pathways. Internalization and degradation of EGFR after ligand binding limits the intensity of proliferative signaling, thereby helping to maintain cell integrity. In cancer cells, deregulation of EGFR trafficking has a variety of effects on tumor progression. Here we report that sortilin is a key regulator of EGFR internalization. Loss of sortilin in tumor cells promoted cell proliferation by sustaining EGFR signaling at the cell surface, ultimately accelerating tumor growth. In lung cancer patients, sortilin expression decreased with increased pathologic grade, and expression of sortilin was strongly correlated with survival, especially in patients with high EGFR expression. Sortilin is therefore a regulator of EGFR intracellular trafficking that promotes receptor internalization and limits signaling, which in turn impacts tumor growth.
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Sortilin mediates the release and transfer of exosomes in concert with two Tyrosine Kinase Receptors.
Journal of cell science, 2014Co-Authors: Cornelia M Wilson, Thomas Naves, François Vincent, Boris Melloni, François Bonnaud, Fabrice Lalloué, Marie-odile JauberteauAbstract:The transfer of exosomes containing both genetic and protein materials is necessary for the control of the cancer cell microenvironment to promote tumor angiogenesis. The nature and function of proteins found in the exosomal cargo, and the mechanism of their action in membrane transport and related signaling events are not clearly understood. In this study, we demonstrate, in human lung cancer A549 cells, that the exosome release mechanism is closely linked to the multifaceted receptor sortilin (also called neurotensin receptor 3). Sortilin is already known to be important for cancer cell function. Here, we report for the first time its role in the assembly of a Tyrosine Kinase complex and subsequent exosome release. This new complex (termed the TES complex) is found in exosomes and results in the linkage of the two Tyrosine Kinase Receptors TrkB (also known as NTRK2) and EGFR with sortilin. Using in vitro models, we demonstrate that this sortilin-containing complex exhibits a control on endothelial cells and angiogenesis activation through exosome transfer.
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Sortilin mediates the release and transfer of exosomes in concert with two Tyrosine Kinase Receptors.
Journal of Cell Science, 2014Co-Authors: Cornelia Wilson, Thomas Naves, François Vincent, Boris Melloni, François Bonnaud, Fabrice Lalloué, Marie-odile Jauberteau-marchanAbstract:: The transfer of exosomes containing both genetic and protein materials is necessary for the control of cancer cell microenvironment to promote tumor angiogenesis. The nature and function of proteins found in the exosomal cargo, their mechanisms in membrane transport and related signaling events are not clearly understood. In this study, we demonstrate in human lung cancer A549 cells, that the exosome release mechanism is closely linked to a multifaceted receptor, neurotensin (NT) receptor-3 also called sortilin. Sortilin is already known to be important for cancer cell function. Here, we report for the first time its role in the assembly of a Tyrosine Kinase complex and subsequent exosome release. This novel complex (TES complex) found in exosomes results in the linkage of two Tyrosine Kinase Receptors, TrkB and EGFR with sortilin. Using in vitro models, we demonstrate that this complex containing sortilin exhibits a control on endothelial cells and angiogenesis activation through exosome transfer.
Paolo M. Comoglio - One of the best experts on this subject based on the ideXlab platform.
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the Tyrosine Kinase Receptors ron and sea control scattering and morphogenesis of liver progenitor cells in vitro
Molecular Biology of the Cell, 1996Co-Authors: Enzo Medico, A M Mongiovi, J Huff, M A Jelinek, Antonia Follenzi, Giovanni Gaudino, J T Parsons, Paolo M. ComoglioAbstract:The mammalian RON and the avian sea genes encode Tyrosine Kinase Receptors of poorly characterized biological functions. We recently identified macrophage-stimulating protein as the ligand for Ron; no ligand has yet been found for Sea. In this work we investigated the biological response to macrophage-stimulating protein in mouse liver progenitor cells expressing Ron. These cells were also transfected with a chimeric cDNA encoding the cytoplasmic domain of Sea, fused to the extracellular domain of Trk (nerve growth factor receptor). In the presence of nanomolar concentrations of the respective ligands, both Receptors induced cell "scattering", extracellular matrix invasion, and DNA synthesis. When liver progenitor cells were grown in a tri-dimensional type-I collagen matrix, ligand-induced stimulation of either Ron or Sea induced sprouting of branched cell cords, evolving into ductular-like tubules. The motogenic, mitogenic, and morphogenic responses were also elicited by triggering the structurally related hepatocyte growth factor receptor (Met) but not epidermal growth factor or platelet-derived growth factor Receptors. These data show that Ron, Sea, and Met belong to a receptor subfamily that elicits a distinctive biological response in epithelial cells.
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a multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor scatter factor receptor family
Cell, 1994Co-Authors: Carola Ponzetto, Alberto Bardelli, Paolo Dalla Zonca, Z Zhen, George Panayotou, Silvia Giordano, Flavio Maina, Andrea Graziani, Paolo M. ComoglioAbstract:Abstract Signaling by Tyrosine Kinase Receptors is mediated by selective interactions between individual Src homology 2 (SH2) domains of cytoplasmic effectors and specific phosphoTyrosine residues in the activated receptor. Here, we report the existence in the hepatocyte growth factor/scatter factor (HGFSF) receptor of a multifunctional docking site made of the tandemly arranged degenerate sequence YVHNV. Phosphorylation of this site mediates intermediate- to high-affinity interactions with multiple SH2-containing signal transducers, including phosphatidylinositol 3-Kinase, phospholipase Cγ, pp60 c-src , and the GRB-2-Sos complex. Mutation of the two Tyrosines results in loss of biological function, as shown by abrogation of the transforming activity in the oncogenic counterpart of the receptor. The same bidentate motif is conserved in the evolutionarily related Receptors Sea and Ron, suggesting that in all members of the HGFSF receptor family, signal transduction is channeled through a multifunctional binding site.
