Mirian A. F. Hayashi *

Autora invitada por SIIC

Estudo do mecanismos moleculares e genéticos que determinam a expressão neuro-específica da NUDEL-oligopeptidase

EXPRESSÃO NEURO-ESPECÍFICA DA NUDEL-OLIGOPEPTIDASE QUE APRESENTA PAPEL FUNDAMENTAL NA PATOFISIOLOGIA DE DESORDENS NEUROLÓGICAS E NEUROPSIQUIÁTRICAS

Neste trabalho as seqüências 5’ flanqueadoras do gene humano e de coelho da NUDEL-oligopeptidase foram clonados e a atividade promotora foi analisada utilizando as linhagens de glioma de rato (C6) e neuroblastoma humano (NH15). No geral, um perfil bastante similar de atividade promotora foi observado para os dois promotores analisados, incluindo as deleções estudadas. A única exceção está relacionada com a análise da seqüência mais longa do promotor de coelho, que apresentou uma atividade quase duas vezes maior quando transfectada nas células NH15, embora nenhuma diferença tenha sido observada para o promotor humano. Todos estes resultados estão inteiramente de acordo com o padrão de distribuição e expressão da NUDEL-oligopeptidase determinado através da medida da sua atividade enzimática, análises imunoquímicas e através de hibridizações.

*Mirian A. F. Hayashi
describe para SIIC los aspectos relevantes de su trabajo
CLONING AND CHARACTERIZATION OF THE HUMAN AND RABBIT NUDEL-OLIGOPEPTIDASE PROMOTERS AND THEIR NEGATIVE REGULATION
Institución principal de la investigación
*Instituto Butantan, Centro de Toxinologia Aplicada, São Paulo, Brasil, São Paulo, Brasil
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Otros artículos escogidos

Referencias bibliográficas
1. Camargo ACM, Shapanka R, Greene LJ. Preparation, assay and partial characterization of a neutral endopeptidase from rabbit brain. Biochemistry 12:1838-1844.
2. Oliveira EB, Martins AR, Camargo ACM, Isolation of brain endopeptidases: Influence of size and sequence of substrates structurally related to bradykinin. Biochemistry 16:1967-1974.
3. Camargo ACM, Reis ML, Caldo H. Susceptibility of a peptide derived from bradykinin to hydrolysis by brain endo-oligopeptidases and pancreatic proteinases. Journal Biological Chemistry 254:5304-5307.
4. Camargo ACM, Oliveira EB, Toffoletto O, Metters KM, Rossier J. Brain endo-oligopeptidase A, a putative enkephalin-converting enzyme. Journal of Neurochemistry 48:1258-1263.
5. Camargo ACM, Gomes MD, Toffoletto O, Ribeiro MJF, Ferro ES, Fernandes BL, Suzuki K, Sasaki Y, Juliano L. Structural requirements of bioactive peptides for the interaction with endopeptidase 22.19. Neuropeptides 26:281-287.
6. Camargo ACM, Gomes MD, Reichl AP, Ferro ES, Jacchieri S, Juliano L. Structural features which make oligopeptides susceptible to hydrolysis by recombinant endooligopeptidase 24.15 (EC 3.4.24.15). Biochemical Journal 324(1197):517-522.
7. Jacchieri SG, Gomes MD, Camargo ACM, Juliano L. Cross examination of the conformational spaces of a set of peptide chains: study of oligopeptidase action. Int. J. Quantum Chem. 23:1815-1827.
8. Jacchieri S, Gomes MD, Juliano L, Camargo ACM. A comparative conformational analysis of thimet oligopeptidase (EC 3.4.24.15) substrates. Journal of Peptide Research 51:452-459.
9. Carvalho KM, Camargo ACM. Purification of rabbit brain endo-oligopeptidases and preperation of anti-enzyme antibodies. Biochemistry 20:7082-7088.
10. Coelho HLL, Cicilini MA, Carvalho KM, Carvalho IF, Camargo ACM. Inhibition of rabbit tissue kininase by anti-(endo-oligopeptidase A) antibodies. Biochemical Journal, 197:85-93.
11. Hayashi MAF, Portaro FCV, Tambourgi DV, Sucupira M, Yamane T, Fernandes BL, Ferro ES, Rebouças NA, Camargo ACM. Molecular and immunochemical evidences demonstrate that endooligopeptidase A is the predominant cytosolic oligopeptidase of rabbit brain. Biochemical and Biophysical Research Communications 269:7-13.
12. Oliveira ES, Leite PEP, Spillatini MG, Camargo ACM, Hunt SP. Localization of endo-oligopeptidase (EC. 3.4.22.19) in rat nervous tissue. Journal of Neurochemistry 55:1114-1121.
13. Hayashi MAF, Pires RS, Rebouças NA, Britto LR, Camargo ACM. Expression of endo-oligopeptidase A in the rat central nervous system: a non-radioactive in situ hybridization study. Molecular Brain Research 89:86-93.
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20. Hayashi MAF, Portaro FCV, Camargo ACM. Cytosolic oligopeptidases: features and possible physiopathological roles in the immune and nervous systems. Curr. Med. Chem. – CNSA 4:269- 277.
21. Hayashi MAF, Portaro FCV, Bastos MF, Guerreiro JR, Gorrão SS, Tambourgi DV, Sant’Anna OA, Camargo LM, Brandon NJ, Camargo ACM. Inhibition of NUDEL-oligopeptidase activity by the schizophrenia risk factor Disrupted in Schizophrenia 1 (DISC1). Proc. Natl. Acad. Sci. 102:3828-3833.
22. Guerreiro JR, Winnischofer SM, Bastos MF, Portaro FCV, Sogayar MC, Camargo ACM, Hayashi MAF. Cloning and characterization of the human and rabbit NUDEL-oligopeptidase promoters and their negative regulation. Biochim Biophys Acta 25:77-84.
23. Quinn JP. Neuronal-specific gene expression – The interaction of both positive and negative transcriptional regulators. Prog. Neurobiol. 50:363- 379.

Otros artículos de Mirian A. F. Hayashi

Hayashi MAF, Gomes MD, Rebouças NA, Fernandes BL, Ferro ES, Camargo ACM. Species specificity of thimet oligopeptidase (EC 3.4.24.15). Biol. Chem. Hoppe-Seyler 377:283-291.

Murayama N, Hayashi MAF, Ohi H, Ferreira LAF, Hermann VV, Saito H, Fujita Y, Higuchi S, Fernandes BL, Yamane T, Camargo ACM. Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide. Proc. Natl. Acad. Sci. 94:1189- 1193.

Portaro FCV, Hayashi MAF, Silva CL, Camargo ACM. Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and controls oligopeptidase degradation in macrophage. Eur. J. Biochem. 268:1-9.

Cotton J, Hayashi MAF, Cuniasse P, Vazeux G, Ianzer D, Camargo ACM, Dive V. Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides. Biochemistry 41:6065-6071.

Portaro FCV, Hayashi MAF, Arauz LJ, Palma MS, Assakura MT, Silva CL, Camargo ACM. The mycobacterium leprae hsp65 displays proteolytic activity. mutagenesis studies indicate that the M. leprae hsp65 proteolytic activity is catalytically related to the HslVU protease. Biochemistry 41:7400- 7406.

Hayashi MAF, Murbach AF, Ianzer D, Portaro FCV, Prezoto BC, Silveira PF, Silva CA, Pires RS, Britto LRG, Dive V, Camargo ACM. The C-type natriuretic peptide precursor of snake brain contains highly specific inhibitors of the angiotensin-converting enzyme. J. Neurochem. 85:969- 977.

Para comunicarse con Mirian A. F. Hayashi mencionar a SIIC como referencia:
mirianhayashi@butantan.gov.br

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Acerca del trabajo completo

EXPRESSÃO NEURO-ESPECÍFICA DA NUDEL-OLIGOPEPTIDASE QUE APRESENTA PAPEL FUNDAMENTAL NA PATOFISIOLOGIA DE DESORDENS NEUROLÓGICAS E NEUROPSIQUIÁTRICAS

Título original en castellano
Clonagem e caracterização do promotor humano e de coelho da NUDEL-oligopeptidase e sua regulação negativa

Autores
Mirian A. F. Hayashi¹, Juliano Rodrigo Guerreiro², Sheila M. B. Winnischofer³, Marta F. Bastos⁴, Fernanda C. V. Portaro⁵, Mari C. Sogayar⁶, Antonio C. M. Camargo⁷
1 Farmacêutica-Bioquímica, Instituto Butantan, Pesquisadora PQC-III
2 Farmacêutico, Instituto Butantan, Centro de Toxinologia Aplicada, Doutorado
3 Química, Instituto de Química, Universidade de São Paulo, Doutorado
4 Bióloga, Instituto Butantan, Centro de Toxinologia Aplicada, Doutorado
5 Química, Instituto Butantan, Centro de Toxinologia Aplicada, Pesquisadora
6 Bióloga, Instituto de Química, Universidade de São Paulo, Professora Titular
7 Médico, Instituto Butantan, Centro de Toxinologia Aplicada, Pesquisador

Acceso a la fuente original
BBA Gene Structure and Expression
http://www.elsevier.com/wps/find/journaldescription.cws_home/506065/description

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