Binding of anti-GRP78 autoantibodies to cell surface GRP78 increases tissue factor procoagulant activity via the release of calcium from endoplasmic reticulum stores
AA Al-Hashimi, J Caldwell, M Gonzalez-Gronow… - Journal of Biological …, 2010 - ASBMB
The increased risk of venous thromboembolism in cancer patients has been attributed to
enhanced tissue factor (TF) procoagulant activity (PCA) on the surface of cancer cells …
enhanced tissue factor (TF) procoagulant activity (PCA) on the surface of cancer cells …
Regulation of tissue factor–mediated initiation of the coagulation cascade by cell surface grp78
G Bhattacharjee, J Ahamed, B Pedersen… - … , and vascular biology, 2005 - Am Heart Assoc
Objective—To test the hypothesis that Grp78 negatively regulates cell surface tissue factor
(TF) procoagulant activity and whether this is mediated by physical interaction. Methods and …
(TF) procoagulant activity and whether this is mediated by physical interaction. Methods and …
Overexpression of the 78-kDa glucose-regulated protein/immunoglobulin-binding protein (GRP78/BiP) inhibits tissue factor procoagulant activity
LM Watson, AKC Chan, LR Berry, J Li, SK Sood… - Journal of Biological …, 2003 - ASBMB
Previous studies have demonstrated that overexpression of GRP78/BiP, an endoplasmic
reticulum (ER)-resident molecular chaperone, in mammalian cells inhibits the secretion of …
reticulum (ER)-resident molecular chaperone, in mammalian cells inhibits the secretion of …
Autoantibodies against the cell surface–associated chaperone GRP78 stimulate tumor growth via tissue factor
AA Al-Hashimi, P Lebeau, F Majeed, E Polena… - Journal of Biological …, 2017 - ASBMB
Tumor cells display on their surface several molecular chaperones that normally reside in
the endoplasmic reticulum. Because this display is unique to cancer cells, these chaperones …
the endoplasmic reticulum. Because this display is unique to cancer cells, these chaperones …
Scratching the surface—An overview of the roles of cell surface GRP78 in cancer
J Chen, EG Lynn, TR Yousof, H Sharma… - Biomedicines, 2022 - mdpi.com
The 78 kDa glucose-regulated protein (GRP78) is considered an endoplasmic reticulum
(ER)-resident molecular chaperone that plays a crucial role in protein folding homeostasis …
(ER)-resident molecular chaperone that plays a crucial role in protein folding homeostasis …
Ligation of cell surface GRP78 with antibody directed against the COOH-terminal domain of GRP78 suppresses Ras/MAPK and PI 3-kinase/AKT signaling while …
UK Misra, SV Pizzo - Cancer biology & therapy, 2010 - Taylor & Francis
We have previously shown that treatment of prostate cancer and melanoma cells expressing
GRP782 on their cell surface with antibody directed against the COOH-terminal domain of …
GRP782 on their cell surface with antibody directed against the COOH-terminal domain of …
GRP78: a multifunctional receptor on the cell surface
M Gonzalez–Gronow, MA Selim, J Papalas… - Antioxidants & redox …, 2009 - liebertpub.com
The 78 kDa glucose-regulated protein (GRP78) is an endoplasmic reticulum chaperone,
whose function is generally thought to be restricted to controlling the structural maturation of …
whose function is generally thought to be restricted to controlling the structural maturation of …
Glucose‐regulated protein (GRP78) is an important cell surface receptor for viral invasion, cancers, and neurological disorders
The 78 kDa glucose‐regulated protein (GRP78) is an endoplasmic reticulum (ER)‐resident
molecular chaperone. GRP78 is a member of the 70 kDa heat shock family of proteins …
molecular chaperone. GRP78 is a member of the 70 kDa heat shock family of proteins …
Ligation of cancer cell surface GRP78 with antibodies directed against its COOH-terminal domain up-regulates p53 activity and promotes apoptosis
UK Misra, Y Mowery, S Kaczowka, SV Pizzo - Molecular cancer therapeutics, 2009 - AACR
Binding of activated α2-macroglobulin to GRP78 on the surface of human prostate cancer
cells promotes proliferation by activating signaling cascades. Autoantibodies directed …
cells promotes proliferation by activating signaling cascades. Autoantibodies directed …
Ligation of prostate cancer cell surface GRP78 activates a proproliferative and antiapoptotic feedback loop: a role for secreted prostate-specific antigen
UK Misra, S Payne, SV Pizzo - Journal of Biological Chemistry, 2011 - ASBMB
GRP78, a well characterized chaperone in the endoplasmic reticulum, is critical to the
unfolded protein response. More recently, it has been identified on the cell surface, where it …
unfolded protein response. More recently, it has been identified on the cell surface, where it …