The Experts below are selected from a list of 352290 Experts worldwide ranked by ideXlab platform
Ying-shing Chan - One of the best experts on this subject based on the ideXlab platform.
-
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.
-
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.
Isabelle Cournu-rebeix - One of the best experts on this subject based on the ideXlab platform.
-
Tyrosine Kinase 2 variant influences T lymphocyte polarization and multiple sclerosis susceptibility
Brain, 2011Co-Authors: Nicolas Couturier, Florence Bucciarelli, Ramil N. Nurtdinov, Marc Debouverie, Christine Lebrun-frenay, Gilles Defer, Thibault Moreau, Christian Confavreux, Sandra Vukusic, Isabelle Cournu-rebeixAbstract:The Tyrosine Kinase 2 variant rs34536443 has been established as a genetic risk factor for multiple sclerosis in a variety of populations. However, the functional effect of this variant on disease pathogenesis remains unclear. This study replicated the genetic association of Tyrosine Kinase 2 with multiple sclerosis in a cohort of 1366 French patients and 1802 controls. Furthermore, we assessed the functional consequences of this polymorphism on human T lymphocytes by comparing the reactivity and cytokine profile of T lymphocytes isolated from individuals expressing the protective TYK2 GC genotype with the disease-associated TYK2 GG genotype. Our results demonstrate that the protective C allele infers decreased Tyrosine Kinase 2 activity, and this reduction of activity is associated with a shift in the cytokine profile favouring the secretion of Th2 cytokines. These findings suggest that the rs34536443 variant effect on multiple sclerosis susceptibility might be mediated by deviating T lymphocyte differentiation toward a Th2 phenotype. This impact of Tyrosine Kinase 2 on effector differentiation is likely to be of wider importance because other autoimmune diseases also have been associated with polymorphisms within Tyrosine Kinase 2. The modulation of Tyrosine Kinase 2 activity might therefore represent a new therapeutic approach for the treatment of autoimmune diseases. * Abbreviations : IFNβ : interferon beta IFNλ : interferon lambda IL : interleukin JAKs : Janus Kinase superfamily STAT : signal transducers and activators of transcription family TNF : tumour necrosis factor TYK2 : Tyrosine Kinase 2
-
Tyrosine Kinase 2 variant influences T lymphocyte polarization and multiple sclerosis susceptibility.
Brain : a journal of neurology, 2011Co-Authors: Nicolas Couturier, Florence Bucciarelli, Ramil N. Nurtdinov, Marc Debouverie, Christine Lebrun-frenay, Gilles Defer, Thibault Moreau, Christian Confavreux, Sandra Vukusic, Isabelle Cournu-rebeixAbstract:The Tyrosine Kinase 2 variant rs34536443 has been established as a genetic risk factor for multiple sclerosis in a variety of populations. However, the functional effect of this variant on disease pathogenesis remains unclear. This study replicated the genetic association of Tyrosine Kinase 2 with multiple sclerosis in a cohort of 1366 French patients and 1802 controls. Furthermore, we assessed the functional consequences of this polymorphism on human T lymphocytes by comparing the reactivity and cytokine profile of T lymphocytes isolated from individuals expressing the protective TYK2(GC) genotype with the disease-associated TYK2(GG) genotype. Our results demonstrate that the protective C allele infers decreased Tyrosine Kinase 2 activity, and this reduction of activity is associated with a shift in the cytokine profile favouring the secretion of Th2 cytokines. These findings suggest that the rs34536443 variant effect on multiple sclerosis susceptibility might be mediated by deviating T lymphocyte differentiation toward a Th2 phenotype. This impact of Tyrosine Kinase 2 on effector differentiation is likely to be of wider importance because other autoimmune diseases also have been associated with polymorphisms within Tyrosine Kinase 2. The modulation of Tyrosine Kinase 2 activity might therefore represent a new therapeutic approach for the treatment of autoimmune diseases.
Douglas C. Eaton - One of the best experts on this subject based on the ideXlab platform.
-
Tyrosine Kinase regulates epithelial sodium transport in A6 cells.
American Journal of Physiology-Cell Physiology, 1993Co-Authors: P. S. Matsumoto, Akito Ohara, Pascal Duchatelle, Douglas C. EatonAbstract:Insulin increases epithelial Na+ reabsorption, and many of its actions involve Tyrosine Kinase. We used Tyrosine Kinase inhibitors to examine the role of Tyrosine Kinase in the action of insulin. Pretreatment of Na+ transporting cells with Tyrosine Kinase inhibitors attenuates the subsequent action of insulin, suggesting that the action of insulin on epithelial Na+ transport involves Tyrosine Kinase activity. In addition to their effect on insulin-induced Na+ transport, the Tyrosine Kinase inhibitors also significantly reduce Na+ transport in Na(+)-transporting epithelial cells, suggesting that there is a significant tonic Tyrosine Kinase activity that modulates epithelial Na+ transport. Using patch-clamp methods, we found that one inhibitor, genistein, reduces the number of active Na+ channels in cell-attached patches without significantly affecting the open probability of any remaining channels. The effects of the Tyrosine Kinase inhibitors are not due to inhibition of protein Kinase A (PKA), since H89,...
-
Tyrosine Kinase regulates epithelial sodium transport in A6 cells.
The American journal of physiology, 1993Co-Authors: P. S. Matsumoto, Akito Ohara, Pascal Duchatelle, Douglas C. EatonAbstract:Insulin increases epithelial Na+ reabsorption, and many of its actions involve Tyrosine Kinase. We used Tyrosine Kinase inhibitors to examine the role of Tyrosine Kinase in the action of insulin. Pretreatment of Na+ transporting cells with Tyrosine Kinase inhibitors attenuates the subsequent action of insulin, suggesting that the action of insulin on epithelial Na+ transport involves Tyrosine Kinase activity. In addition to their effect on insulin-induced Na+ transport, the Tyrosine Kinase inhibitors also significantly reduce Na+ transport in Na(+)-transporting epithelial cells, suggesting that there is a significant tonic Tyrosine Kinase activity that modulates epithelial Na+ transport. Using patch-clamp methods, we found that one inhibitor, genistein, reduces the number of active Na+ channels in cell-attached patches without significantly affecting the open probability of any remaining channels. The effects of the Tyrosine Kinase inhibitors are not due to inhibition of protein Kinase A (PKA), since H89, a PKA inhibitor, does not affect Na+ transport of control cells (as the Tyrosine Kinase inhibitors do), and the Tyrosine Kinase inhibitor, genistein or tyrphostin 23, does not alter the stimulation of ion transport by 8-(4-chlorophenylthio)adenosine 3',5'-cyclic monophosphate, a membrane-permeable adenosine 3',5'-cyclic monophosphate analogue (as H89 does).
Jean-laurent Casanova - One of the best experts on this subject based on the ideXlab platform.
-
A Patient with Tyrosine Kinase 2 Deficiency without Hyper-IgE Syndrome
The Journal of pediatrics, 2012Co-Authors: Sara Sebnem Kilic, Mustafa Hacimustafaoglu, Stéphanie Boisson-dupuis, Alexandra Y. Kreins, Audrey V. Grant, Laurent Abel, Jean-laurent CasanovaAbstract:We describe a Turkish patient with Tyrosine Kinase 2 deficiency who suffered from disseminated Bacille Calmette-Guerin infection, neurobrucellosis, and cutaneous herpes zoster infection. Tyrosine Kinase 2 deficiency should be considered in patients susceptible to herpes viruses and intramacrophage pathogens even in the absence of atopy, high serum IgE, and staphylococcal disease.
Hajime Karasuyama - One of the best experts on this subject based on the ideXlab platform.
-
Hyperimmunoglobulin E syndrome and Tyrosine Kinase 2 deficiency.
Current opinion in allergy and clinical immunology, 2007Co-Authors: Yoshiyuki Minegishi, Hajime KarasuyamaAbstract:PURPOSE OF REVIEW The purpose of the review is to provide recent insight into the pathogenesis and pathophysiology of hyperimmunoglobulin E syndrome. RECENT FINDINGS We recently identified a homozygous four base-pair deletion in the coding region of the Tyrosine Kinase 2 gene in a hyperimmunoglobulin E syndrome patient who exhibited susceptibility to intracellular bacteria. SUMMARY Hyperimmunoglobulin E syndrome is a primary immunodeficiency characterized by recurrent staphylococcal skin abscesses and pneumonia, and elevated serum immunoglobulin E. This syndrome is subdivided into types 1 and 2. Type 1 displays abnormalities in multiple systems, including the skeletal/dental and immune systems, whereas type 2 abnormalities are confined to the immune system. We recently identified a homozygous mutation in the Tyrosine Kinase 2 gene in a type 2 patient. Analyses of cytokine responses in the patient's cells revealed that the Tyrosine Kinase 2 deficiency had resulted in severe impairment of the signal transduction for multiple cytokines, including interleukin-6, -10, -12 and -23, and interferon-alpha/beta. The cytokine signals were successfully restored by transducing the intact Tyrosine Kinase 2 gene. Thus, Tyrosine Kinase 2 plays obligatory roles in human immunity. Based on this finding, we propose that hyperimmunoglobulin E syndrome is a primary immunodeficiency caused by genetic alterations leading to the defect in multiple cytokine signals.
