Expression and release of glucose-regulated protein-78 (GRP78) in multiple myeloma

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Expression and release of glucose-regulated protein-78 (GRP78) in multiple myeloma

INTRODUCTION Multiple myeloma (MM) is a plasma cell neoplasm that is mostly incurable due to acquired resistance during the treatment course. Thus, we evaluated expression and release of glucose-regulated protein 78 kDa (GRP78/BiP), an endoplasmic reticulum (ER) based pro-survival chaperone involved in immunoglobulin folding and unfolded protein responses. RESULTS GRP78 protein expression in ...

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therapeutic potential of glucose regulated protein 78 in cancer

endoplasmic reticulum has a critical role in the synthesis and folding of secretory and membrane proteins. high accumulation of proteins in er activates the unfolded protein response and glucose regulated protein 78 or gpr78 plays an essential role in this pathway.  unfolded protein response is activated in cancerous cells due to their adverse condition to survive and it has been shown that grp...

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Glucose-Regulated Protein 78 (Grp78) Confers Chemoresistance to Tumor Endothelial Cells under Acidic Stress

OBJECTIVES This study was designed to investigate the activation of the unfolded protein response (UPR) in tumor associated endothelial cells (TECs) and its association with chemoresistance during acidic pH stress. MATERIALS AND METHODS Endothelial cells from human oral squamous cell carcinomas (OSCC) were excised by laser capture microdissection (LCM) followed by analysis of UPR markers (Grp...

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Overexpression of the 78-kDa glucose-regulated protein/immunoglobulin-binding protein (GRP78/BiP) inhibits tissue factor procoagulant activity.

Previous studies have demonstrated that overexpression of GRP78/BiP, an endoplasmic reticulum (ER)-resident molecular chaperone, in mammalian cells inhibits the secretion of specific coagulation factors. However, the effects of GRP78/BiP on activation of the coagulation cascade leading to thrombin generation are not known. In this study, we examined whether GRP78/BiP overexpression mediates cel...

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Characterization and mechanism of stress-induced translocation of 78-kilodalton glucose-regulated protein (GRP78) to the cell surface.

Glucose-regulated protein (GRP78)/BiP, a major chaperone in the endoplasmic reticulum, is recently discovered to be preferably expressed on the surface of stressed cancer cells, where it regulates critical oncogenic signaling pathways and is emerging as a target for anti-cancer therapy while sparing normal organs. However, because GRP78 does not contain classical transmembrane domains, its mech...

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ژورنال

عنوان ژورنال: Oncotarget

سال: 2017

ISSN: 1949-2553

DOI: 10.18632/oncotarget.17353