P42: Luteolin Counteracts ER Stress in PC12 Cells through Moderating ER Chaperones and Heat Shock Proteins
Authors
Abstract:
This article doesn't have abstract
similar resources
p42: luteolin counteracts er stress in pc12 cells through moderating er chaperones and heat shock proteins
luteolin, as a natural polyphenolic compound, has neuroprotective effect and exerts its function by attenuation of apoptosis and oxidative stress factors. emerging evidences indicate that oxidative stress leads to neurodegeneration but is not the initial event and endoplasmic reticulum stress (er) is often considered to be the stimulus event which is caused by accumulating of misfolded proteins...
full textCapsaicin induces apoptosis in PC12 cells through ER stress
Capsaicin, the pungent agent in chili peppers, has been shown to act as a tumor-suppressor in cancer. In our previous study, capsaicin was shown to induce apoptosis in the rat pheochromocytoma cell line (PC12 cells). Thus, the aim of the present study was to determine the potential mechanism by which capsaicin induces apoptosis. We treated PC12 cells with 50, 100 and 500 µM capsaicin and measur...
full textHeat shock response relieves ER stress.
Accumulation of misfolded protein in the endoplasmic reticulum (ER) causes stress. The unfolded protein response (UPR), a transcriptional induction pathway, is activated to relieve ER stress. Although UPR is not essential for viability, UPR-deficient cells are more sensitive to ER stress; ire1Delta cells cannot grow when challenged with tunicamycin or by overexpression of misfolded CPY(*). In t...
full textBiP chaperones ER entry
gate that guards the translocon is opened and closed by ATP cycles that also give the same protein chaperone activity, as shown on page 389 by Alder et al. The translocon is an aqueous pore in the ER membrane through which secreted proteins pass during translation. To prevent the unwanted passage of ions, unused pores are plugged on the lumen side by the action of BiP. Within the ER, BiP is als...
full textRegulation of OSU-03012 toxicity by ER stress proteins and ER stress-inducing drugs.
The present studies examined the toxic interaction between the non-coxib celecoxib derivative OSU-03012 and phosphodiesterase 5 (PDE5) inhibitors, and also determined the roles of endoplasmic reticulum stress response regulators in cell survival. PDE5 inhibitors interacted in a greater than additive fashion with OSU-03012 to kill parental glioma and stem-like glioma cells. Knockdown of the endo...
full textMolecular chaperones and heat shock proteins in atherosclerosis.
In response to stress stimuli, mammalian cells activate an ancient signaling pathway leading to the transient expression of heat shock proteins (HSPs). HSPs are a family of proteins serving as molecular chaperones that prevent the formation of nonspecific protein aggregates and assist proteins in the acquisition of their native structures. Physiologically, HSPs play a protective role in the hom...
full textMy Resources
Journal title
volume 2 issue 4
pages 92- 92
publication date 2014-12
By following a journal you will be notified via email when a new issue of this journal is published.
No Keywords
Hosted on Doprax cloud platform doprax.com
copyright © 2015-2023