Journal article
Endoplasmic Reticulum Chaperone Protein GRP78 Protects Cells from Apoptosis Induced by Topoisomerase Inhibitors ROLE OF ATP BINDING SITE IN SUPPRESSION OF CASPASE-7 ACTIVATION*
Abstract
A large number of correlative studies have established that the activation of the unfolded protein response (UPR) alters the cell's sensitivity to chemotherapeutic agents. Although the induction of the glucose-regulated proteins (GRPs) is commonly used as an indicator for the UPR, the direct role of the GRPs in conferring resistance to DNA damaging agents has not been proven. We report here that without the use of endoplasmic reticulum (ER) …
Authors
Reddy RK; Mao C; Baumeister P; Austin RC; Kaufman RJ; Lee AS
Journal
Journal of Biological Chemistry, Vol. 278, No. 23, pp. 20915–20924
Publisher
Elsevier
Publication Date
6 2003
DOI
10.1074/jbc.m212328200
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Adenosine TriphosphateAnimalsAntineoplastic AgentsAntineoplastic Agents, PhytogenicApoptosisBinding SitesCamptothecinCarrier ProteinsCaspase 7CaspasesCell MembraneCricetinaeDoxorubicinEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPEnzyme PrecursorsEtoposideG1 PhaseGene ExpressionHeat-Shock ProteinsHumansLeukemiaMolecular ChaperonesProtein Structure, TertiarySubcellular FractionsTopoisomerase I InhibitorsTopoisomerase II InhibitorsTransfectionTumor Cells, CulturedUrinary Bladder Neoplasms