Targeting Bid to prevent programmed cell death in neurons.
AuthorsCulmsee C, Plesnila N
JournalBiochem Soc Trans
PubMed ID17073814
'Sustained progression of neuronal cell death causes brain tissue loss and subsequent functional deficits following stroke or central nervous system trauma and in neurodegenerative diseases. Despite obvious differences in the pathology of these neurological disorders, the underlying delayed neuronal demise is carried out by a common biochemical cell death programme. ... More
Regulation and pathological role of bid in ischemic acute kidney injury.
AuthorsWei Q, Dong Z
JournalRen Fail
PubMed ID18067037
Bid, a BH3-only member of the Bcl-2 family proteins, is most abundantly expressed in the kidneys. Recent research has shown Bid activation in renal tubular cells in vitro following ATP-depletion and hypoxic injury, and also in vivo during renal ischemia-reperfusion in rats and mice. Importantly, Bid-deficient mice are resistant to ... More
BID as a double agent in cell life and death.
AuthorsGross A
JournalCell Cycle
PubMed ID16582605
DNA damage leads to the activation of ATM and ATR, which in turn either cause cell cycle arrest and DNA repair or apoptosis. We have demonstrated that DNA damage leads to ATM-mediated BID phosphorylation, and that this phosphorylation regulates a novel, pro-survival function of BID important for S phase arrest. ... More
Signal transduction mediated by Bid, a pro-death Bcl-2 family proteins, connects the death receptor and mitochondria apoptosis pathways.
AuthorsYin XM
JournalCell Res
PubMed ID11032168
Two major apoptosis pathways have been defined in mammalian cells, the Fas/TNF-R1 death receptor pathway and the mitochondria pathway. The Bcl-2 family proteins consist of both anti-apoptosis and pro-apoptosis members that regulate apoptosis, mainly by controlling the release of cytochrome c and other mitochondrial apoptotic events. However, death signals mediated ... More
Bid, a BH3-only multi-functional molecule, is at the cross road of life and death.
AuthorsYin XM
JournalGene
PubMed ID16446060
Bid, BH3-interacting domain death agonist, was initially cloned based in its ability to interact with both Bcl-2 and Bax. Bid contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. Bid is susceptible to proteolytic cleavage by caspases, calpains, ... More