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Caspase‐12 and ER‐Stress‐Mediated Apoptosis
Author(s) -
SZEGEZDI EVA,
FITZGERALD UNA,
SAMALI AFSHIN
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1299.032
Subject(s) - unfolded protein response , endoplasmic reticulum , microbiology and biotechnology , apoptosis , cytosol , programmed cell death , mitochondrion , homeostasis , signal transduction , chemistry , protein folding , biology , biochemistry , enzyme
A bstract : The labyrinth of the endoplasmic reticulum (ER) interweaves the cytosol and connects to the nucleus, mitochondria, and the plasma membrane. In the lumen of the ER, the essential function of lipid synthesis, Ca 2+ storage, folding, and maturation of proteins take place. Therefore, the tight regulation and maintenance of ER homeostasis is vital. Disturbance of the Ca 2+ homeostasis during hypoxia, or imbalance between the demand and capacity of the protein‐folding apparatus, initiates an adaptive response of the cell, termed the unfolded protein response (UPR, ER stress response). As a result, ER‐localized chaperones are induced, protein synthesis is slowed down, and a protein degrading system is initiated. However, if the ER stress cannot be alleviated, it culminates in apoptosis. This paper reviews the newly outlined signaling pathways of the unfolded protein response and describes the central role of caspase‐12 in the initiation of cell death. The complex role of the ER and its signaling pathways provides a novel angle on apoptosis research and may offer a key to apoptosis‐associated diseases.