
IndraLab
Statements
sparser
"Furthermore, through bimolecular fluorescence complementation analysis, we confirmed that ox-LDL rather than AngII stimulation induced the direct binding of LOX-1 and AT 1 -R. We conclude that direct binding of LOX-1 and AT1-R and the activation of downstream Gq protein are important mechanisms of ox-LDL-induced cardiomyocyte hypertrophy."
sparser
"Similar red fluorescence intensity was observed in in situ PLA in non-permeabilized conditions in CHO-LOX-1-AT1, CHO-LOX-1-AT1mβ, and CHO-LOX-1-AT1mg, suggesting that these AT1 mutants interact with LOX-1, similar to the interaction with intact AT1 on the cellular surface ( xref D)."
sparser
"We previously found that the proximity between LOX-1 and AT1 on the cellular membrane was absent between LOX-1 and the Ang II type receptor (AT2), which is the isoform of AT1, in an in situ proximity ligation assay (PLA), indicating that LOX-1 specifically binds to AT1 ( xref )."
sparser
"To investigate whether the activation of AT1 by oxLDL induced internalization of the LOX-1-AT1 complex, we utilized a live cell imaging technique using a real-time spinning disk confocal super-resolution microscope in CHO-K1 cells transiently transfected with LOX-1 labeled with mScarlet and AT1 labeled with eGFP."
sparser
"Furthermore, through bimolecular fluorescence complementation analysis, we confirmed that ox-LDL rather than AngII stimulation induced the direct binding of LOX-1 and AT 1 -R. We conclude that direct binding of LOX-1 and AT1-R and the activation of downstream Gq protein are important mechanisms of ox-LDL-induced cardiomyocyte hypertrophy."
reach
"To investigate whether the activation of AT1 by oxLDL induced internalization of the LOX-1 and AT1 complex, we utilized a live cell imaging technique using a real-time spinning disk confocal super-resolution microscope in CHO-K1 cells transiently transfected with LOX-1 labeled with mScarlet and AT1 labeled witheGFP."