INIBIOLP   05426
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE LA PLATA "PROF. DR. RODOLFO R. BRENNER"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Apolipoprotein A-I Treatment on Thp1 Macrophages Result in the Accumulation of Sequestosome 1 (p62) via Nrf2 Dependent
Autor/es:
BECERRA R; TREJO SA; GONZALEZ MC; DIAZ LUDOVICO I; GARDA HA
Lugar:
Reunión virtual
Reunión:
Congreso; Vascular Discovery: From Genes to Medicine Scientific Sessions 2020; 2020
Institución organizadora:
American Heart Association (ATVB)
Resumen:
The human apolipoprotein A-I (apoA-I) is the major protein component of high-density lipoproteins (HDL). It?s known that the interaction of apoA-I with macrophages trigger several signal transduction pathways. We realized a total proteomics profile between apoA-I and control treatment on THP-1 macrophages in order to find differential protein levels.To address if some unknown pathway could be activated by apoA-I we have analyzed a total proteomics profiling by comparative LFQ proteomics of apoA-I treated macrophages in comparison with untreated control.Total protein extracts were analyzed in a quadrupole/orbitrap. Subsequently, spectra were identified by two different software. Differential proteins levels were confirmed by Western-blot.Between 10 differentially-expressed proteins (at least in 2 folds over expressed on apoA-I-treated cells; p≤0.05) we found sequestrosome-1 (p62), a multifunctional protein that could be regulated by the Nrf2-KEAP1 pathway. When the Nrf2 pathway was inhibited by all-trans retinoic acid (ATRA), p62 levels decreases 40 to 50% in co treated cells (ATRA + ApoA-I) compared with only apoA-I-treated cells.We conclude that p62 could accumulates in THP-1-macrophages since apoA-I treatment in a Nrf2 pathway dependent manner