Role of the vestibular nuclei in endothelin-1-induced barrel rotation in rats

Kozako, Tomohiro; Kawachi, Asuka; Cheng, Shi-Bin; Kuchiiwa, Satoshi; Motoya, Toshiro; Nakagawa, Shiro; Yamada, Katsushi

doi:10.1016/s0014-2999(02)02498-6

Cited by 9 publications

(11 citation statements)

References 47 publications

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“…One‐month‐old male Wistar rats were used for immunohistochemical analysis. Free‐floating immunohistochemical staining of frozen sections of the brain was performed as described previously (Kozako et al. 2002).…”

Section: Methodsmentioning

confidence: 99%

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Contactin‐associated protein (Caspr) 2 interacts with carboxypeptidase E in the CNS

Oiso¹,

Takeda²,

Futagawa³

et al. 2009

Journal of Neurochemistry

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To identify proteins interacting with the intracellular domain of the neural cell adhesion molecule contactin‐associated protein 2 (Caspr2), yeast two‐hybrid screening was performed. We identified carboxypeptidase E (CPE) as a Caspr2‐interacting candidate protein. Glutathione S‐transferase pull‐down and immunoprecipitation analyses indicated that Caspr2 was associated with CPE in vitro and in vivo. Both Caspr2 and CPE were expressed predominantly in the CNS. Immunohistochemical analyses revealed that both Caspr2‐ and CPE‐like immunoreactivities were found to co‐localize in the apical dendrites and cell bodies of rat cortical neurons. In subcellular localization analysis, Caspr2‐ and CPE‐like immunoreactivities were co‐migrated in the fractions of Golgi/ER. Additionally, in COS‐7 cells co‐transfected with CPE and Caspr2 cDNAs, Caspr2‐ and CPE‐immunoreactivities were co‐localized in both Golgi and membrane, whereas it was only observed in Golgi of either COS‐7 cell transfected with CPE or Caspr2 cDNA alone. It is known that the membrane‐bound form of CPE functions as a sorting receptor of prohormones in the trans‐Golgi network. Taken together, our data suggest that CPE may be a key molecule to regulate Caspr2 trafficking to the cell membrane.

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Section: Methodsmentioning

confidence: 99%

“…One-month-old male Wistar rats were used for immunohistochemical analysis. Free-floating immunohistochemical staining of frozen sections of the brain was performed as described previously (Kozako et al 2002). Briefly, for immunohistochemical staining of CPE or Caspr2, a peroxidase-antiperoxidase detection system was used.…”

Section: Immunohistochemistrymentioning

confidence: 99%

Contactin‐associated protein (Caspr) 2 interacts with carboxypeptidase E in the CNS

Oiso¹,

Takeda²,

Futagawa³

et al. 2009

Journal of Neurochemistry

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“…The immunohistochemical detection of ATF3 was performed with the PAP method. ( 20 ) The animals were perfused transcardially with 4% paraformaldehyde in 0.1 M phosphate buffer (pH 7.4) containing 0.2% picric acid under deep anesthesia (pentobarbital sodium, 40 mg/kg, i.p.). DRGs isolated from lumbar 4 and 5 levels were sectioned at 40 µm thickness with a freezing microtome, and serial longitudinal sections were treated with 0.3% hydrogen peroxide in 0.02 M PBS for 15 min at room temperature.…”

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confidence: 99%

Up‐regulation of matrix metalloproteinase‐3 in the dorsal root ganglion of rats with paclitaxel‐induced neuropathy

Nishida¹,

Kuchiiwa

Oiso³

et al. 2008

Cancer Science

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Paclitaxel-induced painful peripheral neuropathy is a major doselimiting factor. Recently, it has been reported that macrophages accumulated in the dorsal root ganglion of paclitaxel-treated rats, and their activation is suggested to contribute to generation and development of the neuropathy. However, the mechanism for macrophage activation is still unknown. In this study, to explore candidate genes involved in the mechanism for macrophage activation in the dorsal root ganglion of paclitaxel-treated rats, we developed model rats for paclitaxel-induced neuropathic pain and performed a microarray assay to analyze the changes of gene expressions in the dorsal root ganglion. Among the genes with changed expression levels, we focused on matrix metalloproteinase-3 (MMP-3, stromelysin-1) and CD163, a macrophage marker. By reverse transcription-polymerase chain reaction, the expression levels of MMP-3 and CD163 were markedly up-regulated in paclitaxel-treated dorsal root ganglion. As a result of immunohistochemical study, large ganglion neurons, but neither Schwann cells nor macrophages, predominantly expressed MMP-3. This MMP-3 up-regulation occurred prior to macrophage accumulation in the dorsal root ganglion. In addition, recombinant MMP-3 led to the activation of RAW264 macrophages in vitro. Taken together, the up-regulation of MMP-3 and following macrophage activation caused in the dorsal root ganglion might be a significant event to trigger a series of reactions developing paclitaxel-induced peripheral neuropathic pain. (Cancer Sci 2008; 99: 1618-1625) P aclitaxel is an antineoplastic agent used clinically to treat nonsmall-cell lung cancer and ovarian cancer.(1,2) Paclitaxel suppresses microtubule dynamics, causing mitotic arrest in dividing cells.(3) On the other hand, painful peripheral neuropathy is a major dose-limiting factor in clinical cancer chemotherapy with paclitaxel. (4,5) Although the administration of glutamine and acetyl-L-carnitine has been reported to relieve paclitaxel-induced neuropathic pain as symptomatic treatment, (6,7) its effectiveness shows large interindividual variation. To develop a specific treatment, the molecular mechanisms underlying paclitaxelinduced neuropathy should be explored.It has been assumed that paclitaxel-induced neuropathy is generally due to effects on axonal microtubules.(8) Paclitaxelinduced neuropathy is characterized by an ascending distal paresthesia and dysesthesia in a 'glove and stocking' distribution. (5,8) Blocking of axonal transport due to paclitaxel-induced disruption of microtubule dynamics, which seems to be a reasonable mechanism, has been observed in vitro.(9) Nerve biopsies from patients with taxane-induced neuropathy have shown evidence of a loss of large diameter afferents.(10) In contrast, it has been reported that administration of low dose of paclitaxel caused neuropathic pain without any change of axonal morphology. (11) Additively, in vitro, axonal transport was not impaired in DRG neurons exposed to paclitaxel at chemotherapeutic doses. (12) ...

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“…Como contribuição fica a possibilidade de utilizá-la no desenvolvimento de novos medicamentos para importantes doenças como esclerose e hipertensão (KOSAKO et al, 2000), podendo servir também como um modelo experimental das desordens do movimento humano (KAWACHI et al, 1998).…”

Section: ) Nas Diversas Respostas Biológicas à Ação Desta Toxina Utunclassified

“…As dúvidas sobre a pureza das preparações de giroxina foram esclarecidas quando MAGALHÃES et al (1993) (KOSAKO et al, 2000), podendo servir também como um modelo experimental das desordens do movimento humano (KAWACHI et al, 1998).…”

Section: Figura 1 Distribuição Geográfica Da Espécie Crotalus Durissunclassified

Mediação dos receptores ativados por proteases (PARs) em atividades biológicas da giroxina

Silva¹

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De fato quebrei a cabeça, mas nunca soube que substância é essa. Sinto, porém, que me faz muita falta -Otto Lara Resende É um erro capital teorizar antes de ter os dados. Insensivelmente, começa-se a distorcer os fatos para adaptá-los as teorias, em vez de fazer com que as teorias se adaptem aos fatos -Conan Doyle (1981) Nada é mais digno de nosso patrocínio que o fomento da ciência e da literatura. O conhecimento é, em todo e qualquer país, a base mais segura da felicidade pública -Politicagens ( À minha Orientadora Doutora Maria Aparecida Pires Camillo pela confiança e dedicação.Ao Doutor José Roberto Rogero por todo apoio e confiança desde a iniciação científica.Ao CNPq pelo apoio financeiro.À Doutora Nanci do Nascimento por todo apoio.À Doutora Olga Zazuco Higa pelo apoio e utilização de alguns equipamentos no laboratório.Á Doutora Lígia Ely Morganti F. Dias, pela utilização de aparelhos e materiais de seu grupo de estudo.Ao Doutor Patrick Jack Spencer por toda ajuda e incentivo.Ao Doutor Paulo Sérgio Cardoso da Silva por todo apoio, amizade e incentivo. Ao Doutor Luis Gonzaga e a Mestre Bianca Zychar, do Laboratório de Fisiopatologia doInstituto Butantan, por disponibilizarem o laboratório nos experimentos de microscopia intravital.Aos meus amigos Rubens Zanatta, Eduardo Moura, Murilo Casare, Vanessa, Larissa, Rosa, Sr. Longino, Dona G, Fernanda Calvo, Priscila Caproni, Jean Queiroz, Brito, Keli, Taís, Renata, Claudinha, Johnny, Camila Yonamine por toda amizade, ajuda e muitos momentos de descontração.Às chocólatras Janaína e Karina Corleto que sempre me extorquiram em troca de discussões filosóficas sobre a vida acadêmica, a vida cotidiana e, também, a vida alheia! Agradeço por todas as broncas e gargalhadas espalhafatosas (preciso mencionar de quem?), foi um grande prazer tê-las por perto durante muitas etapas desse trabalho.Devo um agradecimento especial à minha grande e estimada amiga Natália Malavasi por todo "sangue", digo, apoio nos momentos finais desse trabalho, não teria conseguido sem você! 20 MEDIAÇÃO DOS RECEPTORES ATIVADOS POR PROTEASES (PARs) EM ATIVIDADES BIOLÓGICAS DA GIROXINA RESUMOA giroxina é uma enzima serinoprotease do veneno da cascavel sul-americanaCrotalus durissus terrificus. É uma toxina apenas parcialmente caracterizada e com múltiplas atividades. Atua na coagulação, na diminuição da pressão arterial e induz um comportamento neurotóxico descrito como rolamento em barril. Os mecanismos envolvidos nestas atividades não são conhecidos. Considerando que a giroxina é uma enzima com alto potencial para ser um novo fármaco com aplicações em clínica médica como a trombina, tripsina, ancrod ® , batroxobin ® e calicreína, é importante determinar como a giroxina atua. As análises em eletroforese em gel de poliacrilamida e dicroísmo circular confirmaram a pureza e integridade da molécula.A administração intravenosa em camundongos comprovou a neurotoxicidade (SCH 79797 e tcY-NH 2 , respectivamente). Finalmente, foi demonstrado que a giroxina alterou temporariamente a permeabilidade da barreir...

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Role of the vestibular nuclei in endothelin-1-induced barrel rotation in rats

Cited by 9 publications

References 47 publications

Contactin‐associated protein (Caspr) 2 interacts with carboxypeptidase E in the CNS

Contactin‐associated protein (Caspr) 2 interacts with carboxypeptidase E in the CNS

Up‐regulation of matrix metalloproteinase‐3 in the dorsal root ganglion of rats with paclitaxel‐induced neuropathy

Mediação dos receptores ativados por proteases (PARs) em atividades biológicas da giroxina

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