SDS PAGE of Grp78 protein.

GRP78 is a ubiquitously expressed, 78-kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5 nontranslated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia (Barnes), to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer’s patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).

1. Cho, S. et al (2007). Mol Cell Biol 27(1): 368-83.
2. Yang, Y. et al. (1998) J Biol Chem 273:25552-25555.
3. Luo, S. et al (2006) 26 (15): 5688-97.
4. Yu, Z. et al. (1999) Exp Neurol. 15: 302-314.
5. Koomagi, R. et al. (1999) Anticancer Res. 19: 4333-4336.
6. Laquerre, S. et al. (1998) J. Virology 72: 4940-4949.
7. Dong, D. et al. (2005) Cancer Res 65(13): 5785-91.

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1. Speth C. et al. (2013). Neutrophils Turn Plasma Proteins into Weapons against HIV-1. PLoS ONE 8(6): e66073. doi:10.1371/journal.pone.0066073

2. Ciplys, E., Au Ynait, A., Slibinskas, R. (2014). Generation of human ER chaperone BiP in yeast Saccharomyces cerevisiae. Microb Cell Fact. 13(1):22. doi: 10.1186/1475-2859-13-22