INVESTIGADORES
PERDOMO Virginia Gabriela
congresos y reuniones científicas
Título:
Trypanosoma cruzi HIGH MOBILITY GROUP B PROTEIN: WHAT WE KNOW ABOUT ITS NUCLEAR AND EXTRACELLULAR FUNCTIONS
Autor/es:
CRIBB P; TAVERNELLI L; PERDOMO V; MANARIN R; SERRA EC
Lugar:
Rosario
Reunión:
Congreso; L Reunión de la Sociedad Argentina de Investigación Bioquímica y Biología Molecular.; 2014
Resumen:
High Mobility Group Box (HMGB) proteins are evolutionary-conserved components of chromatin. They act as
architectural factors taking part of important nuclear processes like transcriptional regulation, DNA repair and
replication. Beyond these intranuclear functions, some HMGBs can be secreted by certain cells and play important
roles as inflammatory mediators. The HMGB protein from Trypanosoma cruzi (TcHMGB) has two HMG box
domains and a 110 N-terminal domain unique of kinetoplastid HMGBs. It is a nuclear protein expressed in all life
cycle stages and shows architectural properties. The specific N-terminal domain seems to have an additional DNA
binding site and a putative nuclear localization signal. We found that TcHMGB can also be secreted, and protein
acetylation seems to enhance this process. To test if TcHMGB can act as an immune regulator, we stimulated RAW
264.7 macrophages with recombinant TcHMGB for different time periods. Culture supernatants were collected and
nitric oxide production was analyzed measuring nitrite release by Griess reaction. Also, total RNA was purified from
treated macrophages and mRNAs for different cytokines were quantified by qRT-PCR. Recombinant TcHMGB
showed to be able of inducing macrophage activation in vitro, suggesting a role in inflammation. These preliminary
results indicate that TcHMGB may have both nuclear and extracellular functions.