Biology:HSP90B1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Heat shock protein 90kDa beta member 1 (HSP90B1), known also as endoplasmin, gp96, grp94, or ERp99, is a chaperone protein that in humans is encoded by the HSP90B1 gene.[1][2]
HSP90B1 is an HSP90 paralogue that is found in the endoplasmic reticulum. It plays critical roles in folding proteins in the secretory pathway such as Toll-like receptors and integrins.[3][4] It has been implicated as an essential immune chaperone to regulate both innate and adaptive immunity.[5] Tumor-derived HSP90B1 (vitespen) has entered clinical trials for cancer immunotherapy.[6][7][8][9]
grp94 has been shown to be a target for treatment of a plethora of diseases such as glaucoma, multiple myeloma, and metastatic cancer. grp94 includes 5 distinct amino acids in its primary sequence which creates 2 unique sub-pockets, S1 and S2. These sub-pockets have been utilized in current research in order to inhibit the chaperone since its client proteins seem to be up-regulated in cancer cells.[10]
References
- ↑ "Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins". Proceedings of the National Academy of Sciences of the United States of America 87 (15): 5658–62. August 1990. doi:10.1073/pnas.87.15.5658. PMID 2377606. Bibcode: 1990PNAS...87.5658M.
- ↑ "The HSP90 family of genes in the human genome: insights into their divergence and evolution". Genomics 86 (6): 627–37. December 2005. doi:10.1016/j.ygeno.2005.08.012. PMID 16269234.
- ↑ "Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability". Nature Cell Biology 3 (10): 891–6. October 2001. doi:10.1038/ncb1001-891. PMID 11584270.
- ↑ "Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages". Immunity 26 (2): 215–26. February 2007. doi:10.1016/j.immuni.2006.12.005. PMID 17275357.,
- ↑ "gp96--the immune system's Swiss army knife". Nature Immunology 1 (2): 100–1. August 2000. doi:10.1038/77770. PMID 11248798.
- ↑ "Vitespen: a preclinical and clinical review". Future Oncology 5 (6): 763–74. August 2009. doi:10.2217/fon.09.46. PMID 19663726.
- ↑ "HSPPC-96 vaccine in metastatic melanoma patients: from the state of the art to a possible future". Expert Review of Vaccines 8 (11): 1513–26. November 2009. doi:10.1586/erv.09.108. PMID 19863242.
- ↑ "NCT00293423". ClinicalTrials.gov, United States National Institutes of Health. http://clinicaltrials.gov/ct2/show/NCT00293423. "GP96 Heat Shock Protein-Peptide Complex Vaccine in Treating Patients With Recurrent or Progressive Glioma"
- ↑ "Heat-shock protein peptide complex-96 vaccination for recurrent glioblastoma: a phase II, single-arm trial". Neuro-Oncology 16 (2): 274–9. January 2014. doi:10.1093/neuonc/not203. PMID 24335700.
- ↑ "Resorcinol-Based Grp94-Selective Inhibitors" (in EN). ACS Medicinal Chemistry Letters 8 (10): 1013–1018. October 2017. doi:10.1021/acsmedchemlett.7b00193. PMID 29057043.
Further reading
- "Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses". Annual Review of Immunology 20 (1): 395–425. 2001. doi:10.1146/annurev.immunol.20.100301.064801. PMID 11861608.
- "An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response". Frontiers in Bioscience 7 (4): d731–51. March 2002. doi:10.2741/A808. PMID 11861214.
- "Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones". Molecular Cell 28 (1): 41–56. October 2007. doi:10.1016/j.molcel.2007.08.024. PMID 17936703.
- "Mortalin: present and prospective". Experimental Gerontology 37 (10–11): 1157–64. 2003. doi:10.1016/S0531-5565(02)00135-3. PMID 12470827.
- "HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells". The Journal of Experimental Medicine 176 (3): 657–66. September 1992. doi:10.1084/jem.176.3.657. PMID 1512535.
- "Partial separation of platelet and placental adenosine receptors from adenosine A2-like binding protein". Molecular Pharmacology 37 (4): 554–9. April 1990. PMID 2325637.
- "Soluble and membrane-associated human low-affinity adenosine binding protein (adenotin): properties and homology with mammalian and avian stress proteins". Biochemistry 29 (21): 5138–44. May 1990. doi:10.1021/bi00473a020. PMID 2378869.
- "Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors". Molecular and Cellular Biology 9 (5): 2153–62. May 1989. doi:10.1128/mcb.9.5.2153. PMID 2546060.
- "The endoplasmic reticular heat shock protein gp96 is transcriptionally upregulated in interferon-treated cells". The Journal of Experimental Medicine 180 (4): 1565–9. October 1994. doi:10.1084/jem.180.4.1565. PMID 7523574.
- "Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase". The Journal of Biological Chemistry 270 (22): 13524–33. June 1995. doi:10.1074/jbc.270.22.13524. PMID 7768954.
- "p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2". The Journal of Biological Chemistry 271 (9): 4974–7. March 1996. doi:10.1074/jbc.271.9.4974. PMID 8617772.
- "Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum". The Journal of Biological Chemistry 272 (5): 3057–63. January 1997. doi:10.1074/jbc.272.5.3057. PMID 9006956.
- "Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression". Blood 91 (11): 4379–86. June 1998. doi:10.1182/blood.v91.11.4379. PMID 9596688.
- "Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state". The Journal of Biological Chemistry 273 (33): 21368–73. August 1998. doi:10.1074/jbc.273.33.21368. PMID 9694898.
- "Involvement of oxidative reactions and extracellular protein chaperones in the rescue of misassembled thyroglobulin in the follicular lumen". Biochemical and Biophysical Research Communications 255 (2): 438–43. February 1999. doi:10.1006/bbrc.1999.0229. PMID 10049727.
- "The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis". The Journal of Biological Chemistry 274 (40): 28476–83. October 1999. doi:10.1074/jbc.274.40.28476. PMID 10497210.
- "The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme". FEBS Letters 505 (1): 42–6. September 2001. doi:10.1016/S0014-5793(01)02781-8. PMID 11557039.
- "The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway". The Journal of Biological Chemistry 277 (23): 20847–53. June 2002. doi:10.1074/jbc.M200425200. PMID 11912201.
- "Host cell proteins binding to the encapsidation signal epsilon in hepatitis B virus RNA". Archives of Virology 147 (3): 471–91. March 2002. doi:10.1007/s007050200001. PMID 11958450.
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