Caspases involved in ER stress-mediated cell death.

Authors:

J Chem Neuroanat 2004 Sep;28(1-2):101-5

Divisions of Development and Differentiation, National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi-machi, Kodaira, Tokyo 187-8502, Japan.

Caspases are cysteine proteases involved in apoptotic pathways. Excess endoplasmic reticulum (ER) stress, induced by the accumulation of unfolded or malfolded proteins, activates various apoptotic pathways. Crosstalk between the mitochondria and ER plays an essential role in ER stress-mediated cell death. The cytochrome c-dependent apoptotic pathway is activated by ER stress. On the other hand, caspase-12, which is located at the ER, is also activated by excess ER stress and results in cell death in the absence of the cytochrome c-dependent pathway. The predominant apoptotic pathway may differ among cell type and differentiation stage.

Download full-text PDF

Source
https://linkinghub.elsevier.com/retrieve/pii/S08910618040007
Publisher Site
http://dx.doi.org/10.1016/j.jchemneu.2004.05.008DOI Listing
September 2004
2 Reads

Publication Analysis

Top Keywords

cell death
12
cytochrome c-dependent
8
stress-mediated cell
8
apoptotic pathways
8
apoptotic pathway
8
c-dependent apoptotic
4
pathway activated
4
hand caspase-12
4
stress hand
4
activated stress
4
essential role
4
activates apoptotic
4
proteins activates
4
pathways crosstalk
4
mitochondria plays
4
role stress-mediated
4
plays essential
4
death cytochrome
4
located activated
4
pathway differ
4

Similar Publications