Regular ArticleIsolation, Expression, and Characterization of Fully Functional Nontoxic BiP/GRP78 Mutantsā
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Activated Ī±<inf>2</inf>-macroglobulin regulates transcriptional activation of c-MYC target genes through cell surface GRP78 protein
2016, Journal of Biological ChemistryCitation Excerpt :GRP78 is a stress-inducible, prosurvival, endoplasmic reticulum chaperone belonging to the HSP70 family. It is composed of an ATPase domain, a peptide binding domain, and a COOH-terminal domain of unknown function (4ā6). Several different cell types, including proliferating endothelial cells and tumor cells, express GRP78 on their surface (7ā15).
Heat shock 70-kDa protein 5 (Hspa5) is essential for pronephros formation by mediating retinoic acid signaling
2015, Journal of Biological ChemistryCitation Excerpt :In Xenopus, it has been reported previously that RA can induce lhx1 expression in animal caps (23). Heat shock 70-kDa protein 5 (Hspa5), also known as binding immunoglobulin protein (Bip) or glucose-regulated protein 78 (Grp78), belongs to the heat shock protein 70 kDa family of molecular chaperones (24). It functions in endoplasmic reticulum (ER) homeostasis and is a key regulator of the unfolded protein stress response.
Binding of tissue-type plasminogen activator to the Glucose-regulated Protein 78 (GRP78) modulates plasminogen activation and promotes human
2014, Journal of Biological ChemistryCitation Excerpt :Recombinant human microplasminogen (Genecopeia) was expressed in E. coli and purified from clones as previously described (21). Recombinant murine GRP78 and the COOH-terminal domain of GRP78 containing amino acids 516ā636 (Lys516-Gly636), a kind gift from Dr. Sylvie Y. Blond, College of Pharmacy University of Illinois, Chicago, IL, were purified as previously described (22). The goat polyclonal IgG against the NH2-terminal region of human GRP78 (N-20), goat polyclonal IgG against the COOH-terminal region of human GRP78 (C-20), goat polyclonal IgG against human Pg (H-14), goat polyclonal IgG against the NH2-terminal region of human VDAC (N-18), and goat polyclonal IgG against the NH2-terminal region of human t-PA (N-14) were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).
GRP78 expression and immunohistochemical localization in the female reproductive tract of mice
2012, TheriogenologyCitation Excerpt :The 78-kDa glucose-regulated protein (GRP78), also known as the immunoglobulin-binding protein BiP, is a stress-inducible endoplasmic reticulum (ER) chaperone that belongs to the heat shock protein 70 family [1,2].
The Escherichia coli subtilase cytotoxin a subunit specifically cleaves cell-surface GRP78 protein and abolishes COOH-terminal-dependent signaling
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This work was supported by grants from the National Institutes of Health (NIHGM-58107) to S.Y.B. and from the Talaat Basha Family Foundation to E.C.E.
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Present address: Oregon Health Sciences University, Molecular Biology and Immunology, 3181 Sam Jackson Park Road, Portland, OR 97201.
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To whom correspondence should be addressed at Center for Pharmaceutical Biotechnology (M/C 870), University of Illinois at Chicago, Molecular Biology Research Building, 900 South Ashland Avenue, Chicago, IL 60607. Fax: (312) 413-9303. E-mail: [email protected].