MAP Kinase Expression
Published by Anonymous on 2007/9/28 (2142 reads)
1: Ann N Y Acad Sci. 2002 Jun;965:55-67.
Gene expression related to synaptogenesis, neuritogenesis, and MAP kinase in behavioral sensitization to psychostimulants.
Ujike H, Takaki M, Kodama M, Kuroda S.
Department of Neuropsychiatry, Okayama University Medical School and Graduate School of Medicine and Dentistry, Okayama, Japan. hujike@cc.okayama-u.ac.jp
The most important characteristic of behavioral sensitization to psychostimulants, such as amphetamine and cocaine, is the very long-lasting hypersensitivity to the drug after cessation of exposure. Rearrangement and structural modification of neural networks in CNS must be involved in behavioral sensitization. Previous microscopic studies have shown that the length of dendrites and density of dendritic spines increased in the nucleus accumbens and frontal cortex after repeated exposure to amphetamine and cocaine, but the molecular mechanisms responsible are not well understood. We investigated a set of genes related to synaptogenesis, neuritogenesis, and mitogen-activated protein (MAP) kinase after exposure to methamphetamine. Synaptophysin mRNA, but not VAMP2 (synaptobrevin 2) mRNA, which are considered as synaptogenesis markers, increased in the accumbens, striatum, hippocampus, and several cortices, including the medial frontal cortex, after a single dose of 4 mg/kg methamphetamine. Stathmin mRNA, but not neuritin or narp mRNA, which are markers for neuritic sprouting, increased in the striatum, hippocampus, and cortices after a single dose of methamphetamine. The mRNA of arc, an activity-regulated protein associated with cytoskeleton, but not of alpha-tubulin, as markers for neuritic elongation, showed robust increases in the striatum, hippocampus, and cortices after a single dose of methamphetamine. The mRNAs of MAP kinase phosphatase-1 (MKP-1), MKP-3, and rheb, a ras homologue abundant in brain, were investigated to assess the MAP kinase cascades. MKP-1 and MKP-3 mRNAs, but not rheb mRNA, increased in the striatum, thalamus, and cortices, and in the striatum, hippocampus, and cortices, respectively, after a single methamphetamine. Synaptophysin and stathmin mRNAs did not increase again after chronic methamphetamine administration, whereas the increases in arc, MKP-1, and MKP-3 mRNAs persisted in the brain regions after chronic methamphetamine administration. These findings indicate that the earlier induction process in behavioral sensitization may require various plastic modifications, such as synaptogenesis, neuritic sprouting, neuritic elongation, and activation of MAP kinase cascades, throughout almost the entire brain. In contrast, later maintenance process of sensitization may require only limited plastic modification in restricted regions.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 12105085 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Cell Adhes Commun. 1998;6(2-3):217-24.
Integrin signaling: cytoskeletal complexes, MAP kinase activation, and regulation of gene expression.
Danen EH, Lafrenie RM, Miyamoto S, Yamada KM.
Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892, USA. edanen@yoda.nidr.nih.gov
Members of the integrin family of adhesion receptors mediate interactions of cells with the extracellular matrix. Besides their role in tissue morphogenesis by anchorage of cells to basement membranes and migration along extracellular matrix proteins, integrins are thought to play a key role in mediating the control of gene expression by the extracellular matrix. Studies over the past 10 years have shown that integrin-mediated cell adhesion can trigger signal transduction cascades involving translocation of proteins and protein tyrosine phosphorylation events. In this review, we discuss approaches used in our lab to study early events in integrin signalling as well as further downstream changes.
Publication Types:
Review
PMID: 9823472 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Endocr J. 1998 Apr;45 Suppl:S27-31.
Growth hormone-induced tyrosine phosphorylation of EGF receptor as an essential element leading to MAP kinase activation and gene expression.
Yamauchi T, Ueki K, Tobe K, Tamemoto H, Sekine N, Wada M, Honjo M, Takahashi M, Takahashi T, Hirai H, Tsushima T, Akanuma Y, Fujita T, Komuro I, Yazaki Y, Kadowaki T.
Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.
GH binding to its receptor, which belongs to the cytokine receptor superfamily, activates Janus kinase (JAK) 2 tyrosine kinase, thereby activating a number of intracellular key proteins such as STAT (signal transducers and activators of transcription) proteins and mitogen-activated protein (MAP) kinases, which finally lead to GH's biological actions including gene expression. In contrast to receptor tyrosine kinases, the signalling pathways leading to MAP kinase activation by GH are poorly understood but appear to involve Grb2 and Shc. We now show that GH stimulated tyrosine phosphorylation of epidermal growth factor receptor (EGFR) and its association with Grb2, and concomitantly stimulated MAP kinase activity in liver, a major target tissue. Expression of EGFR and its mutants into CHO-GH receptor (GHR) cells revealed that GH-induced full activation of MAP kinase and c-fos expression required tyrosine phosphorylation sites of EGFR but not its intrinsic tyrosine kinase activity. Moreover, by also using dominant negative JAK2 and in vitro kinase assay, we demonstrated that tyrosine 1068 of EGFR was evidently one of the major phosphorylation and Grb2 binding sites stimulated by GH via JAK2. These data suggest that the role of EGFR in GH signalling is to be phosphorylated by JAK2, thereby providing docking sites for Grb2 and activating MAP kinases and gene expression. This novel cross talk pathway may provide the first example of the hormone and cytokine receptor superfamily transducing signals via associated nonreceptor tyrosine kinase by phosphorylating growth factor receptor and utilizing it as a docking protein independent of its receptor tyrosine kinase activity.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9790226 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Front Biosci. 1998 Aug 1;3:d804-16.
MAP kinase signaling cascades and gene expression in osteoblasts.
Hipskind RA, Bilbe G.
Institut de Genetique Moleculaire de Montpellier, CNRS, 1919 Route de Mende, 34293 Montpellier cedex 5, France. hipskind@igm.cnrs-mop.fr
Environmental cues direct osteoblasts to proliferate and differentiate. The mitogen-activated protein (MAP) kinase pathways provide a key link between the membrane bound receptors that receive these cues and changes in the pattern of gene expression. The three MAPK cascades in mammalian cells are: the extracellular signal-regulated kinase (ERK) cascade, the stress activated protein kinase/c-jun N-terminal kinase (SAPK/JNK) cascade and the p38MAPK/RK/HOG cascade. Each has varied roles, depending upon the cell type and context, that include transmitting stress, growth, differentiative and apoptotic signals to the nucleus. These pathways target an overlapping set of transcription factors that lead to the differential activation of rapid response genes, particularly members of the fos and jun family of proto-oncogenes. These proteins are the principal components of the transcription factor AP-1, which plays a central role in regulating genes activated early in osteoblast differentiation. We discuss in detail a) the nature and activation of these pathways b) how they induce c-fos expression and c) how these MAPK cascades can differentially regulate the activity of AP-1 and thereby osteoblast-specific gene expression.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9682034 [PubMed - indexed for MEDLINE]
Gene expression related to synaptogenesis, neuritogenesis, and MAP kinase in behavioral sensitization to psychostimulants.
Ujike H, Takaki M, Kodama M, Kuroda S.
Department of Neuropsychiatry, Okayama University Medical School and Graduate School of Medicine and Dentistry, Okayama, Japan. hujike@cc.okayama-u.ac.jp
The most important characteristic of behavioral sensitization to psychostimulants, such as amphetamine and cocaine, is the very long-lasting hypersensitivity to the drug after cessation of exposure. Rearrangement and structural modification of neural networks in CNS must be involved in behavioral sensitization. Previous microscopic studies have shown that the length of dendrites and density of dendritic spines increased in the nucleus accumbens and frontal cortex after repeated exposure to amphetamine and cocaine, but the molecular mechanisms responsible are not well understood. We investigated a set of genes related to synaptogenesis, neuritogenesis, and mitogen-activated protein (MAP) kinase after exposure to methamphetamine. Synaptophysin mRNA, but not VAMP2 (synaptobrevin 2) mRNA, which are considered as synaptogenesis markers, increased in the accumbens, striatum, hippocampus, and several cortices, including the medial frontal cortex, after a single dose of 4 mg/kg methamphetamine. Stathmin mRNA, but not neuritin or narp mRNA, which are markers for neuritic sprouting, increased in the striatum, hippocampus, and cortices after a single dose of methamphetamine. The mRNA of arc, an activity-regulated protein associated with cytoskeleton, but not of alpha-tubulin, as markers for neuritic elongation, showed robust increases in the striatum, hippocampus, and cortices after a single dose of methamphetamine. The mRNAs of MAP kinase phosphatase-1 (MKP-1), MKP-3, and rheb, a ras homologue abundant in brain, were investigated to assess the MAP kinase cascades. MKP-1 and MKP-3 mRNAs, but not rheb mRNA, increased in the striatum, thalamus, and cortices, and in the striatum, hippocampus, and cortices, respectively, after a single methamphetamine. Synaptophysin and stathmin mRNAs did not increase again after chronic methamphetamine administration, whereas the increases in arc, MKP-1, and MKP-3 mRNAs persisted in the brain regions after chronic methamphetamine administration. These findings indicate that the earlier induction process in behavioral sensitization may require various plastic modifications, such as synaptogenesis, neuritic sprouting, neuritic elongation, and activation of MAP kinase cascades, throughout almost the entire brain. In contrast, later maintenance process of sensitization may require only limited plastic modification in restricted regions.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 12105085 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Cell Adhes Commun. 1998;6(2-3):217-24.
Integrin signaling: cytoskeletal complexes, MAP kinase activation, and regulation of gene expression.
Danen EH, Lafrenie RM, Miyamoto S, Yamada KM.
Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892, USA. edanen@yoda.nidr.nih.gov
Members of the integrin family of adhesion receptors mediate interactions of cells with the extracellular matrix. Besides their role in tissue morphogenesis by anchorage of cells to basement membranes and migration along extracellular matrix proteins, integrins are thought to play a key role in mediating the control of gene expression by the extracellular matrix. Studies over the past 10 years have shown that integrin-mediated cell adhesion can trigger signal transduction cascades involving translocation of proteins and protein tyrosine phosphorylation events. In this review, we discuss approaches used in our lab to study early events in integrin signalling as well as further downstream changes.
Publication Types:
Review
PMID: 9823472 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Endocr J. 1998 Apr;45 Suppl:S27-31.
Growth hormone-induced tyrosine phosphorylation of EGF receptor as an essential element leading to MAP kinase activation and gene expression.
Yamauchi T, Ueki K, Tobe K, Tamemoto H, Sekine N, Wada M, Honjo M, Takahashi M, Takahashi T, Hirai H, Tsushima T, Akanuma Y, Fujita T, Komuro I, Yazaki Y, Kadowaki T.
Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.
GH binding to its receptor, which belongs to the cytokine receptor superfamily, activates Janus kinase (JAK) 2 tyrosine kinase, thereby activating a number of intracellular key proteins such as STAT (signal transducers and activators of transcription) proteins and mitogen-activated protein (MAP) kinases, which finally lead to GH's biological actions including gene expression. In contrast to receptor tyrosine kinases, the signalling pathways leading to MAP kinase activation by GH are poorly understood but appear to involve Grb2 and Shc. We now show that GH stimulated tyrosine phosphorylation of epidermal growth factor receptor (EGFR) and its association with Grb2, and concomitantly stimulated MAP kinase activity in liver, a major target tissue. Expression of EGFR and its mutants into CHO-GH receptor (GHR) cells revealed that GH-induced full activation of MAP kinase and c-fos expression required tyrosine phosphorylation sites of EGFR but not its intrinsic tyrosine kinase activity. Moreover, by also using dominant negative JAK2 and in vitro kinase assay, we demonstrated that tyrosine 1068 of EGFR was evidently one of the major phosphorylation and Grb2 binding sites stimulated by GH via JAK2. These data suggest that the role of EGFR in GH signalling is to be phosphorylated by JAK2, thereby providing docking sites for Grb2 and activating MAP kinases and gene expression. This novel cross talk pathway may provide the first example of the hormone and cytokine receptor superfamily transducing signals via associated nonreceptor tyrosine kinase by phosphorylating growth factor receptor and utilizing it as a docking protein independent of its receptor tyrosine kinase activity.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9790226 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Front Biosci. 1998 Aug 1;3:d804-16.
MAP kinase signaling cascades and gene expression in osteoblasts.
Hipskind RA, Bilbe G.
Institut de Genetique Moleculaire de Montpellier, CNRS, 1919 Route de Mende, 34293 Montpellier cedex 5, France. hipskind@igm.cnrs-mop.fr
Environmental cues direct osteoblasts to proliferate and differentiate. The mitogen-activated protein (MAP) kinase pathways provide a key link between the membrane bound receptors that receive these cues and changes in the pattern of gene expression. The three MAPK cascades in mammalian cells are: the extracellular signal-regulated kinase (ERK) cascade, the stress activated protein kinase/c-jun N-terminal kinase (SAPK/JNK) cascade and the p38MAPK/RK/HOG cascade. Each has varied roles, depending upon the cell type and context, that include transmitting stress, growth, differentiative and apoptotic signals to the nucleus. These pathways target an overlapping set of transcription factors that lead to the differential activation of rapid response genes, particularly members of the fos and jun family of proto-oncogenes. These proteins are the principal components of the transcription factor AP-1, which plays a central role in regulating genes activated early in osteoblast differentiation. We discuss in detail a) the nature and activation of these pathways b) how they induce c-fos expression and c) how these MAPK cascades can differentially regulate the activity of AP-1 and thereby osteoblast-specific gene expression.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9682034 [PubMed - indexed for MEDLINE]
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