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Doctoral Thesis
DOI
https://doi.org/10.11606/T.87.2004.tde-03082005-091712
Document
Author
Full name
Maria Esther Ricci da Silva
E-mail
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 2004
Supervisor
Committee
Tavassi, Ana Marisa Chudzinski (President)
Baptista, Gandhi Radis
Spencer, Patrick Jack
Tambourgi, Denise Vilarinho
Terra, Walter Ribeiro
Title in Portuguese
Análise proteômica do complexo salivar da sanguessuga Haementeria depressa
Keywords in Portuguese
coagulação sanguinea
eletroforese bidimensional
espectrometria de massa
hemostasia
proteoma
saliva
sanguessuga
Abstract in Portuguese
O complexo salivar da sanguessuga H. depressa é composto pelas glândulas salivares e probóscide. Análises bidimensionais (2D) mostraram que a maioria das proteínas apresentam pI entre 3.5 à 9.5 e MM entre 10 à 105 kDa. O mapa 2D do complexo salivar apresentou 352 spots totais, sendo 249 exclusivos da saliva (corado por nitrato de prata) e 219 spots totais (corado por Coomassie Blue). As proteínas foram identificadas após sequenciamento tandem MS (proteoma) pela complementariedade às sequências traduzidas do cDNA (transcriptoma). As proteínas mais abundantes foram: antiagregante plaquetário; miohemeritrina e anidrase carbônica. Estas proteínas devem exercer um papel na digestão ou anticoagulação do sangue durante a alimentação. A zimografia também identificou uma protease gelatinolítica (45 kDa). Porém, lefaxin (inibidor de FXa) e hementerina (fibrinogenolítico e inibidor de agregação plaquetária) não foram identificados por estas técnicas biotecnológicas, o que mostra a necessidade de técnicas adicionais para a completa elucidação da constituição desta amostra.
Title in English
Proteomic analysis of the salivary complex from the leech Haementeria depressa
Keywords in English
blood coagulation
hemostase
leech
mass spectrometry
proteome
saliva
two-dimensional electrophoresis
Abstract in English
The salivary complex from H. depressa leech is composed of salivary gland and proboscis. Two-dimensional (2D) analysis showed that majority of proteins have pI from 3.5 to 9.5 and MW from 10 to 105 kDa. The 2D gel of salivary complex showed 352 total spots, 249 of them were from saliva (silver stained) and 219 total spots (Coomassie Blue stained). Proteins were identified after tandem MS sequencing (proteome) and complementar analysis of translated sequences from cDNA (transcriptome). The most abundant proteins were: antiplatelet protein; myohemerytrin; carbonic anhydrase. These proteins may have a role in digestion or antihemostatic system during blood feeding. The zymographic assay identified a gelatinolytic protein (45 kDa). But, lefaxin (inhibitor of Fxa) and hementerin (fibrinogenolytic and antiplatelet function) were not identified by these biotechonolgical techniques, showing that additional techniques are necessary for complete knowledge about the composition of this sample.
 
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Publishing Date
2007-03-01
 
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