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1.
Curr Pharm Des ; 20(36): 5738-43, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-24502574

RESUMO

A spinal cord injury leads to disturbances of sensory and motor signals due to the damage to white matter and myelinated fiber tracts. Moreover, the damage to gray matter causes segmental loss of interneurons of dorsal horn and motoneurons and restricts the therapeutic options. Neuroprotective strategies have the potential to improve the neurological outcome of patients. To achieve this, concerns to anesthetics or analgesics as neuroprotective interventions have been accumulating to explore neuroprotection during perioperative period. This review includes consideration of: 1) basic concepts of the pathophysiological mechanisms following spinal cord injury and 2) anesthetics and analgesics displaying neuroprotective potential. In particular, we review the application of isoflurane as an inhalational neuroprotectant and discuss evidence for the neuroprotection provided by barbiturates. In addition, 3) recent advances in stem cell biology, neural injury and repair, and progress toward the development of neuroprotective and regenerative interventions are the basis for increased optimism.


Assuntos
Analgésicos/farmacologia , Anestésicos/farmacologia , Traumatismos da Medula Espinal/complicações , Anestésicos Inalatórios/farmacologia , Animais , Humanos , Isoflurano/farmacologia , Fármacos Neuroprotetores/farmacologia , Regeneração/fisiologia , Traumatismos da Medula Espinal/fisiopatologia , Isquemia do Cordão Espinal/complicações , Isquemia do Cordão Espinal/fisiopatologia
3.
Mol Cell Biol ; 21(24): 8626-37, 2001 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-11713295

RESUMO

AMSH, a molecule that associates with STAM1, is involved in the in vitro cell growth signaling mediated by interleukin 2 and granulocyte-macrophage colony-stimulating factor. To investigate the in vivo functional role of AMSH, we have generated AMSH-deficient mice by gene targeting. The AMSH-deficient mice were morphologically indistinguishable from their littermates at birth, and histopathological examinations revealed normal morphogenesis in all tissues tested. However, all the AMSH-deficient mice exhibited postnatal growth retardation and died between postnatal day 19 (P19) and P23. Examination of brain sections at P6 demonstrated significant loss of neurons and apoptotic cells in the CA1 subfield of the hippocampus. Brain atrophy developed by P16 and was accompanied by complete loss of the CA1 neurons in the hippocampus and marked atrophy of the cerebral cortex. Furthermore, AMSH-deficient hippocampal neuronal cells were unable to survive in vitro, even in the presence of several stimulatory cytokines, while AMSH-deficient cerebellar neurons, thymocytes, and embryonic fibroblasts survived normally. Taken together, these observations indicate that AMSH is an essential molecule for the survival of neuronal cells in early postnatal mice.


Assuntos
Proteínas Adaptadoras de Transdução de Sinal , Proteínas de Transporte/química , Córtex Cerebral/citologia , Córtex Cerebral/metabolismo , Endopeptidases , Hipocampo/citologia , Hipocampo/metabolismo , Neurônios/metabolismo , Animais , Apoptose , Northern Blotting , Encéfalo/metabolismo , Proteínas de Transporte/biossíntese , Divisão Celular , Sobrevivência Celular , Células Cultivadas , Complexos Endossomais de Distribuição Requeridos para Transporte , Citometria de Fluxo , Marcação de Genes , Hibridização In Situ , Marcação In Situ das Extremidades Cortadas , Metaloproteases , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Transgênicos , Modelos Genéticos , Fenótipo , Fosfoproteínas/metabolismo , Estrutura Terciária de Proteína , Receptores de Antígenos de Linfócitos T/metabolismo , Transdução de Sinais , Fatores de Tempo , Ubiquitina Tiolesterase , Domínios de Homologia de src
4.
Brain Res Mol Brain Res ; 94(1-2): 119-30, 2001 Oct 19.
Artigo em Inglês | MEDLINE | ID: mdl-11597772

RESUMO

The glycine cleavage system (GCS) is a mitochondrial multienzyme system consisting of four individual proteins, three specific components (P-, T-, and H-proteins) and one house-keeping enzyme, dihydrolipoamide dehydrogenase. Inherited deficiency of the GCS causes nonketotic hyperglycinemia (NKH), an inborn error of glycine metabolism. NKH is characterized by massive accumulation of glycine in serum and cerebrospinal fluids and severe neuronal dysfunction in neonates. To elucidate the neuropathogenesis of NKH, we cloned cDNAs encoding three specific components of the GCS and studied the gene expression in rat central nervous system. P-, T-, and H-protein cDNAs encoded 1024, 403, and 170 amino acids, respectively. In situ hybridization analysis revealed that P-protein mRNA was expressed mainly in glial-like cells, including Bergmann glias in the cerebellum, while T- and H-protein mRNAs were detected in both glial-like cells and neurons. T- and H-protein mRNAs, but not P-protein mRNA, were expressed in the spinal cord. Primary astrocyte cultures established from cerebral cortex had higher GCS activities than hepatocytes whereas those from spinal cord expressed only H-protein mRNA and had no enzymatic activity. An important role of glycine as inhibitory neurotransmitter has been established in the brainstem and spinal cord and another role of glycine as an excitation modulator of N-methyl-D-aspartate receptor is suggested in the hippocampus, cerebral cortex, olfactory bulbus, and cerebellum. Our results suggest that the GCS plays a major role in the forebrain and cerebellum rather than in the spinal cord, and that N-methyl-D-aspartate receptor may participate in neuropathogenesis of NKH.


Assuntos
Aminoácido Oxirredutases/genética , Encéfalo/enzimologia , Proteínas de Transporte/genética , Glicina/metabolismo , Mitocôndrias/enzimologia , Fatores Etários , Aminoácido Oxirredutases/metabolismo , Sequência de Aminoácidos , Animais , Astrócitos/citologia , Astrócitos/fisiologia , Sequência de Bases , Encéfalo/citologia , Proteínas de Transporte/metabolismo , Células Cultivadas , Clonagem Molecular , DNA Complementar , Expressão Gênica/fisiologia , Proteína H do Complexo Glicina Descarboxilase , Glicina Desidrogenase (Descarboxilante) , Hiperglicinemia não Cetótica/genética , Hiperglicinemia não Cetótica/metabolismo , Hibridização In Situ , Fígado/enzimologia , Dados de Sequência Molecular , RNA Mensageiro/análise , Ratos , Ratos Wistar , Receptores de Glicina/metabolismo , Receptores de N-Metil-D-Aspartato/metabolismo
5.
J Biol Chem ; 276(24): 20813-6, 2001 Jun 15.
Artigo em Inglês | MEDLINE | ID: mdl-11319214

RESUMO

Detergent-resistant membrane microdomains in the plasma membrane, known as lipid rafts, have been implicated in various cellular processes. We report here that a low-density Triton X-100-insoluble membrane (detergent-resistant membrane; DRM) fraction is present in bovine rod photoreceptor outer segments (ROS). In dark-adapted ROS, transducin and most of cGMP-phosphodiesterase (PDE) were detergent-soluble. When ROS membranes were exposed to light, however, a large portion of transducin localized in the DRM fraction. Furthermore, on addition of guanosine 5'-3-O-(thio)triphosphate (GTPgammaS) to light-bleached ROS, transducin became detergent-soluble again. PDE was not recruited to the DRM fraction after light stimulus alone, but simultaneous stimulation by light and GTPgammaS induced a massive translocation of all PDE subunits to the DRM. A cholesterol-removing reagent, methyl-beta-cyclodextrin, selectively but partially solubilized PDE from the DRM, suggesting that cholesterol contributes, at least in part, to the association of PDE with the DRM. By contrast, transducin was not extracted by the depletion of cholesterol. These data suggest that transducin and PDE are likely to perform their functions in phototransduction by changing their localization between two distinct lipid phases, rafts and surrounding fluid membrane, on disc membranes in an activation-dependent manner.


Assuntos
3',5'-GMP Cíclico Fosfodiesterases/metabolismo , Guanosina 5'-O-(3-Tiotrifosfato)/farmacologia , Microdomínios da Membrana/fisiologia , Segmento Externo da Célula Bastonete/fisiologia , Transducina/metabolismo , beta-Ciclodextrinas , 3',5'-GMP Cíclico Fosfodiesterases/isolamento & purificação , Animais , Bovinos , Colesterol/isolamento & purificação , Colesterol/metabolismo , Ciclodextrinas , Escuridão , Detergentes , Humanos , Cinética , Luz , Microdomínios da Membrana/efeitos dos fármacos , Microdomínios da Membrana/efeitos da radiação , Transporte Proteico , Transducina/efeitos dos fármacos , Transducina/efeitos da radiação
6.
Brain Res Mol Brain Res ; 88(1-2): 14-25, 2001 Mar 31.
Artigo em Inglês | MEDLINE | ID: mdl-11295228

RESUMO

Heat shock proteins (HSPs) 60 and 10 are stress-inducible mitochondrial matrix proteins that form a chaperonin complex that is important for mitochondrial protein folding and function. The effect of cerebral ischemia on mitochondrial HSPs is unclear. The topographical and chronological patterns of HSP60 and HSP10 messenger ribonucleic acid (mRNA) expression and induction were investigated in the rat focal cerebral ischemia model. Focal cerebral ischemia was produced by transient middle cerebral artery occlusion for 30 or 90 min. Expression of mRNAs was analyzed using reverse transcription-polymerase chain reaction (RT-PCR) and in situ hybridization. RT-PCR analysis showed that both HSP60 and HSP10 mRNA levels increased significantly in the ischemic cortex from 4 to 24 h of reperfusion after 30 min of occlusion. In situ hybridization analysis demonstrated significant induction of both mRNAs in the whole ischemic cortex after 30 min of occlusion and in the dorsomedial border (penumbra) of the ischemic cortex and ipsilateral hippocampus after 90 min of occlusion. Expression patterns and the timing of the induction of both HSP60 and HSP10 mRNAs were identical throughout the experiments. Simultaneous induction of the mRNAs for the mitochondrial chaperonins, HSP60 and HSP10, in various regions in focal cerebral ischemia demonstrates that mitochondrial stress conditions persist concomitantly with cytosolic stress conditions in focal cerebral ischemia.


Assuntos
Chaperonina 10/genética , Chaperonina 60/genética , Ataque Isquêmico Transitório/fisiopatologia , Animais , Northern Blotting , Córtex Cerebral/irrigação sanguínea , Córtex Cerebral/fisiopatologia , Regulação da Expressão Gênica/fisiologia , Hipocampo/irrigação sanguínea , Hipocampo/fisiopatologia , Hibridização In Situ , Infarto da Artéria Cerebral Média/fisiopatologia , Masculino , RNA Mensageiro/análise , Ratos , Ratos Sprague-Dawley , Reação em Cadeia da Polimerase Via Transcriptase Reversa
7.
Brain Res Mol Brain Res ; 88(1-2): 124-34, 2001 Mar 31.
Artigo em Inglês | MEDLINE | ID: mdl-11295238

RESUMO

ADP-ribosylation factors (ARFs) play crucial roles in the intracellular vesicular transport and in regulation of phospholipid-modifying enzyme activities and cytoskeletons. Using in situ hybridization histochemistry, the gene expression for six isoforms of ARF was examined during normal development of rats and in the hypoglossal nucleus following its axotomy. In the embryonic brain, the expression for ARF-1, -4, -5, -6 mRNAs was distinct in the ventricular germinal zone while that for ARF-3, -4, -5 in the mantle zone. In early postnatal brain, the expression for six ARFs was seen widely in various loci of the gray matter with different intensity, and the expression of ARF-4, -5, -6 mRNAs was evident in the cerebellar external granule cell layer. In the adult brain, the gene expression for all ARF isoforms decreased more or less in most gray matters and the distinct expression was maintained mainly in the hippocampal and dentate neuronal layers and cerebellar cortex. The expression levels of ARF-2 and -4 mRNAs in affected hypoglossal nucleus increased after 24 h up to 7 days following axotomy of the hypoglossal nerve, while no such changes were seen in the expression levels for the other ARFs. The present findings suggest that ARFs are differentially involved in some processes essential to nerve regeneration as well as neuronal differentiation and maturation.


Assuntos
Fator 1 de Ribosilação do ADP/genética , Fatores de Ribosilação do ADP/genética , Regulação da Expressão Gênica no Desenvolvimento , Nervo Hipoglosso/fisiologia , Proteínas de Saccharomyces cerevisiae , Fator 6 de Ribosilação do ADP , Fatores Etários , Animais , Axotomia , Northern Blotting , Feminino , Nervo Hipoglosso/crescimento & desenvolvimento , Hibridização In Situ , Gravidez , RNA Mensageiro/análise , Ratos , Ratos Wistar
8.
Histochem J ; 33(8): 453-7, 2001 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-11931385

RESUMO

Almost all alveolar macrophages in the mouse lung were strongly immunoreactive for epidermal-type fatty acid binding protein. At the electron microscope level, the immunoreactive material was localized diffusely in the cytoplasm but not within the nucleus. A certain number of alveolar type II epithelial cells were also immunoreactive for the protein with variable immunointensity, while a substantial number of the type II cells were immunonegative. No immunoreactive interstitial fibroblasts were encountered. Based on the present findings, possible roles of epidermal-type fatty acid binding protein in the host-defence mechanism played by alveolar macrophages are suggested.


Assuntos
Proteínas de Transporte/metabolismo , Macrófagos Alveolares/metabolismo , Proteínas de Neoplasias , Proteínas do Tecido Nervoso , Alvéolos Pulmonares/metabolismo , Animais , Northern Blotting , Proteínas de Transporte/genética , Epiderme/química , Proteína 7 de Ligação a Ácidos Graxos , Proteínas de Ligação a Ácido Graxo , Feminino , Pulmão/química , Macrófagos Alveolares/ultraestrutura , Masculino , Camundongos , Camundongos Endogâmicos BALB C , Microscopia Imunoeletrônica , Alvéolos Pulmonares/ultraestrutura , RNA Mensageiro/metabolismo
9.
Brain Res Mol Brain Res ; 84(1-2): 127-34, 2000 Dec 08.
Artigo em Inglês | MEDLINE | ID: mdl-11113539

RESUMO

Several investigations have postulated evidence of the involvement of apoptosis in delayed neuronal death following brief periods of global cerebral ischemia. Apoptosis may be closely linked to mitochondrial dysfunction. Heat shock protein (HSP) 60 and HSP10 are mitochondrial matrix proteins induced by stress and form the chaperonin complex that is implicated in protein folding and assembly within the mitochondria. This study investigated the induction of these mitochondrial stress protein genes in the hippocampal CA1 region and less vulnerable regions following transient forebrain ischemia. In situ hybridization analysis revealed that the induction pattern of HSP60 mRNA was identical to that of HSP10 mRNA throughout the entire ischemic course. No changes occurred in the expression of both mRNAs after 2 min ischemia. Strong induction of both mRNAs occurred in the CA1 region after 10 min ischemia and persisted until 1 d after reperfusion. In contrast, induction of both mRNAs in the less vulnerable regions was terminated by 1 d after reperfusion. These results demonstrate that mitochondrial stress conditions persist concomitantly with cytosolic stress conditions in regions vulnerable to transient forebrain ischemia.


Assuntos
Isquemia Encefálica/genética , Regulação da Expressão Gênica , Proteínas de Choque Térmico/genética , Mitocôndrias/genética , Prosencéfalo/metabolismo , Prosencéfalo/patologia , Animais , Apoptose , Northern Blotting , Isquemia Encefálica/patologia , Chaperonina 10/genética , Chaperonina 60/genética , Hipocampo/metabolismo , Hipocampo/patologia , Hibridização In Situ , Masculino , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Ratos , Ratos Wistar
10.
Brain Res Mol Brain Res ; 75(1): 172-7, 2000 Jan 10.
Artigo em Inglês | MEDLINE | ID: mdl-10648902

RESUMO

The localization of mRNA for SHIP2, SH2 domain containing inositol 5-phosphatase SHIP isozyme, was examined by in situ hybridization histochemistry in the brain of developing and mature rats. SHIP2 mRNA was first detected in the ventricular germinal zone at embryonic stages. As the postnatal development proceeded, the expression signal was evident in cell of the white matters, presumptive oligodendrocytes, and no significant expression was seen in neurons throughout the development.


Assuntos
Envelhecimento/metabolismo , Encéfalo/enzimologia , Desenvolvimento Embrionário e Fetal , Regulação da Expressão Gênica no Desenvolvimento , Monoéster Fosfórico Hidrolases/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Encéfalo/embriologia , Encéfalo/crescimento & desenvolvimento , Idade Gestacional , Dados de Sequência Molecular , Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases , RNA Mensageiro/genética , Ratos , Transcrição Gênica , Domínios de Homologia de src
11.
J Mol Neurosci ; 15(2): 121-35, 2000 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-11220785

RESUMO

Using in situ hybridization histochemistry, the localization of mRNAs for 10 isoforms of protein kinase C (PKC) in the rat brain was studied at embryonic and postnatal stages. In the embryonic brain, the gene expression was positive only for PKCepsilon, mu, lambda, and zeta with the former three more evident: The expression for PKCmu and lambda in the ventricular germinal zone and that for PKCepsilon, zeta, and lambda in the mantle zone. In the postnatal brain, the expression for PKCdelta, eta, and theta was detected differentially in a few circumscribed loci such as the thalamus, the habenula, the septum, and the cerebellar granule cells, whereas that for the other isoforms was seen widely in various loci of the gray matter with different intensity. The expression in the cerebellar external granule cell layer was positive only for PKCbeta (betaI and betaII), mu, and lambda with that for PKCbeta confined to its inner zone. There is a general tendency for all PKC isoforms that the expression levels reach at peaks in early postnatal brain and decreases more or less in adult specimens. This is the first report on the spatio-temporal heterogeneity in the gene expression for the whole members of PKC family in the brain throughout development, especially at embryonic days.


Assuntos
Envelhecimento/metabolismo , Encéfalo/enzimologia , Proteína Quinase C/genética , RNA Mensageiro/análise , Animais , Animais Recém-Nascidos , Sequência de Bases , Northern Blotting , Encéfalo/crescimento & desenvolvimento , Clonagem Molecular , Isoenzimas/genética , Dados de Sequência Molecular , Sondas de Oligonucleotídeos , Especificidade de Órgãos , Ratos , Ratos Wistar
12.
Tohoku J Exp Med ; 187(3): 249-55, 1999 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-10458481

RESUMO

Gene expression for 3-phosphoinositide-dependent protein kinase-1 (PDK-1) in developing and adult rat brains was examined by in situ hybridization histochemistry. In embryonic days, the mRNA was evident throughout the entire neuraxis. The expression remained evident throughout the entire gray matters until postnatal day 7, and thereafter it decreased overall in the mantle and ventricular zones except for the cerebellar Purkinje and granule cell layers, the olfactory and hippocampal neuronal layers. The pattern of this gene expression is similar to those of for protein kinase B and class I phosphoinositide 3-kinases.


Assuntos
Encéfalo/enzimologia , Proteínas Serina-Treonina Quinases/genética , Proteínas Quinases Dependentes de 3-Fosfoinositídeo , Animais , Encéfalo/embriologia , Encéfalo/crescimento & desenvolvimento , Desenvolvimento Embrionário e Fetal , Regulação da Expressão Gênica no Desenvolvimento , Regulação Enzimológica da Expressão Gênica , RNA Mensageiro/análise , RNA Mensageiro/genética , Ratos , Ratos Wistar
13.
Brain Res Mol Brain Res ; 66(1-2): 195-9, 1999 Mar 20.
Artigo em Inglês | MEDLINE | ID: mdl-10095094

RESUMO

The expression of a gene termed Dri 42, a differentiation-related gene originally identified from intestine and a gene encoding phosphatidic acid phosphatase 2b isoform, was localized in developing and matured rat brains by in situ hybridization histochemical analysis. The gene expression was dominant in the ventricular germinal zone without significant expression in the intermediate, mantle and marginal zones throughout embryonic brain and spinal cord. The dominant expression in the ventricular germinal zone was maintained at P0 and P7, but it markedly decreased at later postnatal stages, while persistently high expression was detected in Bergmann glial cells of the cerebellar Purkinje cell layer throughout the postnatal development.


Assuntos
Química Encefálica/genética , Regulação da Expressão Gênica no Desenvolvimento , Regulação Enzimológica da Expressão Gênica , Proteínas de Membrana/genética , Fosfatidato Fosfatase/genética , Animais , Astrócitos/química , Astrócitos/fisiologia , Northern Blotting , Sistema Nervoso Central/citologia , Sistema Nervoso Central/enzimologia , Hibridização In Situ , Neurônios/química , Neurônios/fisiologia , RNA Mensageiro/análise , Ratos , Ratos Wistar
14.
Tohoku J Exp Med ; 185(2): 139-46, 1998 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-9747653

RESUMO

Mammalian homologues for Drosophila trp are likely to be candidates for capacitative calcium entry channels. By in situ hybridization histochemistry, we have demonstrated that the mRNAs for four species of the mouse homologues (Mtrps-1, -3, -4, -6) were differentially expressed in the adult mouse brain. Mtrp-1 mRNA was expressed widely throughout the gray matters, while the expression for Mtrp-3 was dominant in the cerebellar Purkinje cells, the olfactory mitral cells and the striatal large-sized intrinsic neurons. Mtrp-4 mRNA was evident in the olfactory bulb, the septum, the hippocampal neuronal layers, and the cerebellar granule cell layer, while the expression for Mtrp-6 was rather confined to the dentate granule cell layer. Their differential localization suggests that the individual homologues exert their functions in region-specific and neuron-specific manners in the calcium signaling.


Assuntos
Encéfalo/metabolismo , Canais de Cálcio/biossíntese , RNA Mensageiro/biossíntese , Animais , Hibridização In Situ , Camundongos , Camundongos Endogâmicos BALB C , RNA Mensageiro/análise
15.
J Biol Chem ; 273(13): 7731-6, 1998 Mar 27.
Artigo em Inglês | MEDLINE | ID: mdl-9516481

RESUMO

We report herein the cloning and characterization of a novel class II phosphoinositide 3-kinase, termed PI3K-IIgamma, from the cDNA library of regenerating rat liver. This cDNA encodes a protein of 1505 amino acids with a calculated molecular mass of 170,972 Da. The amino acid sequence of PI3K-IIgamma is highly similar to those of class II PI 3-kinases, including murine Cpk-m/p170 and human HsC2-PI3K. It contains a C2 domain at the C terminus but no recognizable protein motifs at its N terminus. PI3K-IIgamma displays a restricted substrate specificity for PtdIns and PtdIns 4-P, but not for PtdIns 4,5-P2. By epitope tag immunocytochemistry, the immunoreactivity for PI3K-IIgamma is localized in the juxtanuclear Golgi region at high levels and also in the plasma and nuclear membranes at low levels. By Northern blot analysis and in situ hybridization histochemistry, PI3K-IIgamma mRNA expression is confined to the liver throughout the development with much higher expression in adult liver than in fetal liver. In addition, its expression increases during liver regeneration after partial hepatectomy with maximal expression after the growth period, suggesting that PI3K-IIgamma may function mainly in highly differentiated hepatic cells.


Assuntos
Regulação Enzimológica da Expressão Gênica , Isoenzimas/genética , Regeneração Hepática , Fígado/enzimologia , Fosfatidilinositol 3-Quinases/genética , Adulto , Sequência de Aminoácidos , Animais , Células COS , Humanos , Hibridização In Situ , Isoenzimas/biossíntese , Dados de Sequência Molecular , Peso Molecular , Fosfatidilinositol 3-Quinases/biossíntese , Ratos
16.
J Mol Neurosci ; 9(1): 27-33, 1997 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-9356924

RESUMO

By in situ hybridization histochemistry, expression of mRNAs for the two species of serine/ threonine protein kinase Akt, Akt1 and Akt2, were examined in the mouse brain during normal development and in the hypoglossal nucleus following axotomy. On the embryonic days, the gene expression for Akt1 and Akt2 was detected at high levels throughout the entire neuroaxis, then decreased gradually to adult levels during postnatal development. In the adult brain, the gene expression for Akt1 and Akt2 was weak in almost all neurons with no difference of expression levels. The expression level of Akt1 mRNA in the affected hypoglossal nucleus increased dramatically after 48 h to 7 d following axotomy of the hypoglossal nerve, whereas no change was seen in the level of Akt2 mRNA. The present findings suggest that Akt may contribute some important roles not only in neurogenesis, but also in regeneration of injured neuron.


Assuntos
Nervo Hipoglosso/metabolismo , Proteínas Serina-Treonina Quinases/metabolismo , Proteínas Proto-Oncogênicas/metabolismo , RNA Mensageiro/metabolismo , Animais , Northern Blotting , Feminino , Masculino , Camundongos , Proteínas Serina-Treonina Quinases/genética , Proteínas Proto-Oncogênicas/genética , Proteínas Proto-Oncogênicas c-akt , RNA Mensageiro/genética
17.
Brain Res Mol Brain Res ; 46(1-2): 217-22, 1997 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-9191096

RESUMO

Gene expression for rat fatty acid transport protein (FATP) and fatty acid translocase (FAT) were examined by Northern and in situ hybridization analysis. In Northern blot analysis of developing brain, FATP mRNA was detected weakly throughout all developing stages without any changes in the expression level, while no gene expression for FAT mRNA was detected at any stages. By in situ hybridization histochemistry, intense expression was seen in the ventricular germinal zone on pre- and perinatal stages, whereas distinct expression was observed in the cerebellar Purkinje and granule cell during postpostnatal development. No expression was detected in the cerebellar external granule cell layer. Because of the high expression of FATP mRNA in the embryonic ventricular zone and the postnatal cerebellar cortical neurons in parallel to the gene expression for fatty acid binding protein (FABP) which we have recently reported, co-operated involvement of FATP and FABP in the active uptake of long-chain fatty acids is plausible in these cells.


Assuntos
Encéfalo/crescimento & desenvolvimento , Encéfalo/metabolismo , Proteínas de Transporte/metabolismo , Ácidos Graxos/metabolismo , Sequência de Aminoácidos , Animais , Sequência de Bases , Northern Blotting , Expressão Gênica/genética , Hibridização In Situ , Dados de Sequência Molecular , RNA Mensageiro/metabolismo , Ratos
18.
Brain Res Mol Brain Res ; 45(2): 349-52, 1997 May.
Artigo em Inglês | MEDLINE | ID: mdl-9149113

RESUMO

Gene expression for alpha- and beta-isoforms of phosphatidylinositol transfer protein (PITP) was examined using in situ hybridization histochemistry in developing and mature rat brains. During embryonic and early post-natal stages, gene expression for both PITP-alpha and -beta were detected widely throughout the entire neuraxis. In the adult brain, the expression for PITP-alpha was positive in almost all neurons throughout the entire brain while the expression for PITP-beta markedly decreased in the entire gray matter regions except for the cerebellar cortex. By comparison with the previous findings on the expression for various molecules involved in the PI turnover, the present finding suggests that PITP is involved more intimately in some differentiation-related functions of immature neurons than those of mature neurons in co-operation with PI-related molecules and that PITPs exert their functions in adult brain in concert with PLCs in subtype-preferable inter-relation.


Assuntos
Encéfalo/metabolismo , Proteínas de Transporte/biossíntese , Proteínas de Membrana , Transcrição Gênica , Envelhecimento/metabolismo , Animais , Encéfalo/embriologia , Encéfalo/crescimento & desenvolvimento , Desenvolvimento Embrionário e Fetal , Especificidade de Órgãos , Fosfatidilinositóis/metabolismo , Proteínas de Transferência de Fosfolipídeos , RNA Mensageiro/biossíntese , Ratos
19.
Neurosci Lett ; 223(1): 25-8, 1997 Feb 14.
Artigo em Inglês | MEDLINE | ID: mdl-9058414

RESUMO

The changeability in the gene expression for five species of fatty acid binding protein (FABP) was investigated in the crushed hypoglossal nucleus by in situ hybridization histochemistry. Increased gene expression for skin-type fatty acid binding protein (S-FABP) was evident in the affected hypoglossal neurons on the 3rd day after nerve crush, and it lasted until the postoperative day 14. On the other hand, no significant gene expression for heart-, liver-, intestinal- or brain-type FABPs was detected in the hypoglossal neurons of normal control or in these neurons for 3 weeks after the nerve crush. These findings suggest that skin-type FABP may selectively contribute to some important roles in morphological and biochemical changes of neuronal cells associated with the nerve regeneration.


Assuntos
Proteínas de Transporte/genética , Expressão Gênica , Nervo Hipoglosso/fisiologia , Eminência Mediana/fisiologia , Proteína P2 de Mielina/genética , Proteínas de Neoplasias , Compressão Nervosa , Proteínas do Tecido Nervoso , Neurônios/fisiologia , Fenômenos Fisiológicos da Pele , Animais , Proteína 7 de Ligação a Ácidos Graxos , Proteínas de Ligação a Ácido Graxo , Ácidos Graxos/metabolismo , Nervo Hipoglosso/patologia , Hibridização In Situ , Masculino , Eminência Mediana/patologia , Ratos , Ratos Wistar , Valores de Referência
20.
Intern Med ; 36(10): 690-3, 1997 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-9372328

RESUMO

The neurological manifestations of twenty-one Japanese patients with Sjögren's syndrome (SjS) were evaluated. All patients were women, and sixteen of the twenty-one cases (76%) demonstrated objective abnormal neurological symptoms, the most frequently observed of which was trigeminal neuropathy (50%). Multiple mononeuropathy was seen in almost one-third of the examined cases (31%). Central nervous system (CNS) involvement was observed in three cases (14%). All of these values differed greatly from those previously reported. Therefore, this study revealed characteristic features of Japanese SjS and also implied the existence of different immunopathological mechanisms associated with SjS in Japanese patients.


Assuntos
Doenças do Sistema Nervoso/etiologia , Síndrome de Sjogren/complicações , Adulto , Idoso , Biópsia , Encéfalo/patologia , Diagnóstico Diferencial , Progressão da Doença , Feminino , Humanos , Imuno-Histoquímica , Incidência , Japão , Imageamento por Ressonância Magnética , Pessoa de Meia-Idade , Doenças do Sistema Nervoso/diagnóstico , Síndrome de Sjogren/diagnóstico , Medula Espinal/patologia , Nervo Sural/ultraestrutura , Neuralgia do Trigêmeo/diagnóstico , Neuralgia do Trigêmeo/etiologia
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