Linked Life Data

15033718

Source:http://linkedlifedata.com/resource/pubmed/id/15033718

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2004-3-22
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:volume
1010
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
186-94
pubmed:dateRevised
2007-7-25
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Caspase-12 and ER-stress-mediated apoptosis: the story so far.
pubmed:affiliation
Cell Stress and Apoptosis Research Group, Department of Biochemistry, National Centre for Biomedical Engineering Science, National University of Ireland, Galway, Ireland.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't