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Master's Dissertation
DOI
https://doi.org/10.11606/D.42.2014.tde-28112014-135917
Document
Author
Full name
Gepoliano dos Santos Chaves
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 2014
Supervisor
Committee
Garcia, Celia Regina da Silva (President)
Labriola, Leticia
Schechtman, Deborah
Title in Portuguese
Investigação de PfSR25, putativo receptor serpentino de Plasmodium falciparum.
Keywords in Portuguese
Plasmodium falciparum
Cálcio
Fosfatases
GPCRs
Potássio
Quinases
Abstract in Portuguese
Este trabalho teve por objetivo dissecar o papel potencial de fosforilação/desfosforilação como efeitos da ativação de PfSR25, um candidato a receptor serpentina de P. falciparum. Como a sinalização é um evento celular complexo, não excluímos a possibilidade de que outros mecanismos moleculares ocorram além dos aqui descritos. Nossas conclusões são que potássio modula PfSR25, ativando quinases/fosfatases, levando à ativação de moléculas efetoras. Encontramos MSP1, proteína já caracterizada e Pf4-4-13 e o fator básico de transcrição 3B (PfBTF3B), que ainda não foram caracterizados em P. falciparum, como efetores. Estes dados sugerem que pelo menos em parte, o mecanismo pelo qual PfSR25 exerce seu papel no desenvolvimento de P. falciparum seja através da ativação de quinases/fosfatases. Isto não é surpreendente, pois a sinalização de PfSR25 ocorre através de K+/cálcio e o segundo mensageiro é um modulador destas classes de proteínas. No entanto, deve ser investigado se cálcio tem algum efeito direto sobre o processamento/ativação dos efetores aqui identificados.
Title in English
Investigation of PfSR25, putative serpentine receptor of Plasmodium falciparum.
Keywords in English
Plasmodium falciparum
Calcium
GPCRs
Kinases
Phosphatases
Potassium
Abstract in English
This work aimed at dissecting the potential role of phosphorylation/dephosphorylation as downstream effect of PfSR25 activation. PfSR25 is a serpentine receptor candidate from P. falciparum. As signaling is a quite complex cellular event, we do not exclude the possibility that other molecular mechanisms, take place additionally to those here described. Our conclusions are that potassium modulates PfSR25 by activation of kinases/phosphatases, leading to activation of effector molecules. We found MSP1 already characterized protein and Pf4.4.13 and the basic transcription factor 3B (PfBTF3B), which have not yet been characterized in P. falciparum as effectors. These data suggest that, at least in part, the mechanism by which PfSR25 exerts its role in the P. falciparum development is through the activation of kinase/phosphatase. This is not surprising, since PfSR25 signaling occurs through K+/Calcium and the second messenger is a modulator of these classes of proteins. However, remains to be investigated rather calcium has a direct effect on processing/activation the effectors here identified.
 
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Publishing Date
2014-11-28
 
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