IndraLab

Statements


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sparser
"Oxidized LDL but not angiotensin II induces cardiomyocyte hypertrophic responses through the interaction between LOX-1 and AT1 receptors."

sparser
"As shown in the xref , we observed yellow puncta, indicating co-localization of AT1 and LOX-1 moving on the cell surface-focused image, with some of them disappearing after application of 10 μg/mL oxLDL, implying that the complex of LOX-1 and AT1 had been internalized."

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
"Our current findings strongly suggest that oxLDL triggers the activation of GRKs, followed by β-arrestin-induced clathrin-dependent endocytosis of the AT1-LOX-1 complex, whereby circulating oxLDL is translocated into vascular endothelial cells."

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)."

reach
"Our current findings strongly suggest that oxLDL triggers the activation of GRKs, followed by beta-arrestin-induced clathrin dependent endocytosis of the AT1 and LOX-1 complex, whereby circulating oxLDL is translocated into vascular endothelial cells."

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
"Ox-LDL but not AngII could induce the binding of LOX-1 and AT1-R; inhibition of LOX-1 or AT1-R but not AngII could abolish the binding of these two receptors."

sparser
"Chimeric analysis showed that oxLDL-induced AT1 signaling events are mediated via interactions between the intracellular domain of LOX-1 and AT1 that activate AT1."

sparser
"However, since our findings imply that multiple molecules share the same LOX-1-AT1 system to exert their roles in atherogenesis, it is difficult to determine how these individual molecules utilize the system and, thus, contribute to disease progression."

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
"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."

sparser
"Therefore this cross-reactivity and interaction between LOX-1 and AT1 may also be contributing to other vasoreactivity, such as vascular responses to other vasoconstrictors, but this remains to be investigated."

sparser
"Eight genes except OLR1 and AGTR1 were significantly associated with patients' grade."

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."