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Master's Dissertation
DOI
10.11606/D.42.2014.tde-26062014-184010
Document
Author
Full name
Elisabete Rodrigues do Monte Silva
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 2014
Supervisor
Committee
Ferro, Emer Suavinho (President)
Gama, Patricia
Paschoalin, Thaysa
Title in Portuguese
Caracterização do repertório peptídico intracelular de células expressando o proteassomo imune.
Keywords in Portuguese
Degradação de proteínas
Epectrometria de massas
Peptídeos
Proteassomo
Proteassomo imune
Rpt2
Sistema ubiquitina-proteassomo
Abstract in Portuguese
Células eucarióticas contêm vários tipos de proteassomo que regulam o processo de degradação de proteína. Proteassomos são proteases multicatalíticas que são responsáveis pela maior parte de degradação não-lisossomal de proteínas em células eucarióticas. As três subunidades catalíticas do proteassomo são β1, β2 e β5. Em condições de stress e resposta imune essas três subunidades são substituídas por β1i, β2i and β5i, respectivamente, para formar o proteassomo imune. Estas três subunidades induzíveis, parecem alterar as especificidades de peptidase do proteassoma imune em células tratadas com IFN-g. Nosso objetivo no presente trabalho foi caracterizar um modelo celular para a indução do proteassomo imune, e ainda investigar o repertório peptídeo intracelular produzido por esta forma particular do proteassoma, através da técnica de espectrometria de massas. Em resumo, os nossos dados mostraram um aumento de 3 vezes do peptídeo EL28 derivado da proteína RPT2 em células HeLa tratadas com o IFN-g. O peptídeo EL28 pode ser de relevância clínica para o tratamento de distúrbios relacionados com a apresentação de antígenos, visto que ele parece ativar a atividade quimotripsina-like quando incubado com o extrato celular de células HeLa.
Title in English
Characterization of intracellular peptide repertoire of cells expressing the immune proteasome.
Keywords in English
Immune proteasome
Mass spectrometry
Peptides
Proteasome
Protein degradation
Rpt2
Ubiquitin-proteasome system
Abstract in English
Eukaryotic cells contain several types of proteasome regulating the process of protein degradation. The proteasome are responsible for most non - lysosomal protein degradation in eukaryotic cells. The three catalytic subunits of the proteasome are β1, β2 and β5. Under conditions of stress and immune response these three subunits are replaced by β1i, β2i and β5i, respectively, to form the immune proteasome . These three inducible subunits, appear to alter the specificity of the immune proteasome peptidase in cells treated with IFN-g. Our aim in this study was to characterize a cellular model for the induction of the immune proteasome, and even investigate the intracellular peptide repertoire produced by this particular form of the proteasome, through the technique of mass spectrometry. In summary, our data showed an increase of 3 times the peptide derived from RPT2 EL28 protein in HeLa cells treated with IFN-g. The EL28 peptide may be of clinical relevance for the treatment of disorders related to antigen presentation, since it seems to activate the chymotrypsin-like activity when incubated with the cell extract of HeLa cells.
 
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Publishing Date
2014-06-27
 
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