HSP90B1: Difference between revisions

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{{Infobox_gene}}
'''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]].<ref name="pmid2377606">{{cite journal |vauthors=Maki RG, Old LJ, Srivastava PK | title = Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 15 | pages = 5658–62 |date=August 1990 | pmid = 2377606 | pmc = 54386 | doi = 10.1073/pnas.87.15.5658| url = | issn = }}</ref><ref name="pmid16269234">{{cite journal |vauthors=Chen B, Piel WH, Gui L, Bruford E, Monteiro A | title = The HSP90 family of genes in the human genome: insights into their divergence and evolution | journal = Genomics | volume = 86 | issue = 6 | pages = 627–37 |date=December 2005 | pmid = 16269234 | doi = 10.1016/j.ygeno.2005.08.012 | url = | issn = }}</ref>
'''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]].<ref name="pmid2377606">{{cite journal | vauthors = Maki RG, Old LJ, Srivastava PK | title = Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 87 | issue = 15 | pages = 5658–62 | date = August 1990 | pmid = 2377606 | pmc = 54386 | doi = 10.1073/pnas.87.15.5658 }}</ref><ref name="pmid16269234">{{cite journal | vauthors = Chen B, Piel WH, Gui L, Bruford E, Monteiro A | title = The HSP90 family of genes in the human genome: insights into their divergence and evolution | journal = Genomics | volume = 86 | issue = 6 | pages = 627–37 | date = December 2005 | pmid = 16269234 | doi = 10.1016/j.ygeno.2005.08.012 }}</ref>


HSP90B1 is an [[hsp90|HSP90]] [[Homology (biology)#Paralogy|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]].<ref name="pmid11584270">{{cite journal |vauthors=Randow F, Seed B |title=Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. |journal=Nat. Cell Biol. |volume=3 |issue= 10 |pages= 891–6 |year= 2001 |pmid= 11584270 |doi= 10.1038/ncb1001-891 }}</ref><ref name="pmid17275357">{{cite journal   |vauthors=Yang Y, etal |title=Heat Shock Protein gp96 Is a Master Chaperone for Toll-like Receptors and Is Important in the Innate Function of Macrophages. |journal=Immunity |volume=26 |issue=2 |pages= 215–226 |year= 2007 |pmid= 17275357 |doi=10.1016/j.immuni.2006.12.005 | pmc=2847270  }},</ref> It has been implicated as an essential immune chaperone to regulate both [[innate immunity|innate]] and [[adaptive immunity|adaptive]] immunity.<ref name="pmid11248798">{{cite journal |vauthors=Schild H, Rammensee HG | title = gp96--the immune system's Swiss army knife | journal = Nat. Immunol. | volume = 1 | issue = 2 | pages = 100–1 |date=August 2000 | pmid = 11248798 | doi = 10.1038/77770 | url = | issn = }}</ref> Tumor-derived HSP90B1 (vitespen) has entered clinical trials for [[cancer immunotherapy]].<ref name="pmid19663726">{{cite journal |vauthors=Wood CG, Mulders P | title = Vitespen: a preclinical and clinical review | journal = Future Oncol | volume = 5 | issue = 6 | pages = 763–74 |date=August 2009 | pmid = 19663726 | doi = 10.2217/fon.09.46 | url = | issn = }}</ref><ref name="pmid19863242">{{cite journal |vauthors=Tosti G, di Pietro A, Ferrucci PF, Testori A | title = HSPPC-96 vaccine in metastatic melanoma patients: from the state of the art to a possible future | journal = Expert Rev Vaccines | volume = 8 | issue = 11 | pages = 1513–26 |date=November 2009 | pmid = 19863242 | doi = 10.1586/erv.09.108 | url = | issn = }}</ref><ref name="NCT00293423_ClinicalTrials.gov">{{cite web | url = http://clinicaltrials.gov/ct2/show/NCT00293423 | title = NCT00293423 | format = | work = | publisher = ClinicalTrials.gov, United States National Institutes of Health | pages = | language = | archiveurl = | archivedate = | quote = GP96 Heat Shock Protein-Peptide Complex Vaccine in Treating Patients With Recurrent or Progressive Glioma | accessdate = 2010-04-10 }}</ref><ref>{{cite journal|last=Bloch|first=O. |author2=Crane, C. A. |author3=Fuks, Y. |author4=Kaur, R. |author5=Aghi, M. K. |author6=Berger, M. S. |author7=Butowski, N. A. |author8=Chang, S. M. |author9=Clarke, J. L. |author10=McDermott, M. W. |author11=Prados, M. D. |author12=Sloan, A. E. |author13=Bruce, J. N. |author14=Parsa, A. T.|title=Heat-shock protein peptide complex-96 vaccination for recurrent glioblastoma: a phase II, single-arm trial|journal=Neuro-Oncology|date=12 December 2013|doi=10.1093/neuonc/not203 |volume=16 |pages=274–279}}</ref>
HSP90B1 is an [[hsp90|HSP90]] [[Homology (biology)#Paralogy|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]].<ref name="pmid11584270">{{cite journal | vauthors = Randow F, Seed B | title = Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability | journal = Nature Cell Biology | volume = 3 | issue = 10 | pages = 891–6 | date = October 2001 | pmid = 11584270 | doi = 10.1038/ncb1001-891 }}</ref><ref name="pmid17275357">{{cite journal | vauthors = Yang Y, Liu B, Dai J, Srivastava PK, Zammit DJ, Lefrançois L, Li Z | title = Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages | journal = Immunity | volume = 26 | issue = 2 | pages = 215–26 | date = February 2007 | pmid = 17275357 | pmc = 2847270 | doi = 10.1016/j.immuni.2006.12.005 }},</ref> It has been implicated as an essential immune chaperone to regulate both [[innate immunity|innate]] and [[adaptive immunity|adaptive]] immunity.<ref name="pmid11248798">{{cite journal | vauthors = Schild H, Rammensee HG | title = gp96--the immune system's Swiss army knife | journal = Nature Immunology | volume = 1 | issue = 2 | pages = 100–1 | date = August 2000 | pmid = 11248798 | doi = 10.1038/77770 }}</ref> Tumor-derived HSP90B1 (vitespen) has entered clinical trials for [[cancer immunotherapy]].<ref name="pmid19663726">{{cite journal | vauthors = Wood CG, Mulders P | title = Vitespen: a preclinical and clinical review | journal = Future Oncology | volume = 5 | issue = 6 | pages = 763–74 | date = August 2009 | pmid = 19663726 | doi = 10.2217/fon.09.46 }}</ref><ref name="pmid19863242">{{cite journal | vauthors = Tosti G, di Pietro A, Ferrucci PF, Testori A | title = HSPPC-96 vaccine in metastatic melanoma patients: from the state of the art to a possible future | journal = Expert Review of Vaccines | volume = 8 | issue = 11 | pages = 1513–26 | date = November 2009 | pmid = 19863242 | doi = 10.1586/erv.09.108 }}</ref><ref name="NCT00293423_ClinicalTrials.gov">{{cite web | url = http://clinicaltrials.gov/ct2/show/NCT00293423 | title = NCT00293423 | format = | work = | publisher = ClinicalTrials.gov, United States National Institutes of Health | pages = | archive-url = | archive-date = | quote = GP96 Heat Shock Protein-Peptide Complex Vaccine in Treating Patients With Recurrent or Progressive Glioma | access-date = 2010-04-10 }}</ref><ref>{{cite journal | vauthors = Bloch O, Crane CA, Fuks Y, Kaur R, Aghi MK, Berger MS, Butowski NA, Chang SM, Clarke JL, McDermott MW, Prados MD, Sloan AE, Bruce JN, Parsa AT | title = Heat-shock protein peptide complex-96 vaccination for recurrent glioblastoma: a phase II, single-arm trial | journal = Neuro-Oncology | volume = 16 | issue = 2 | pages = 274–9 | date = January 2014 | pmid = 24335700 | doi = 10.1093/neuonc/not203 | pmc = 3895386 }}</ref>
 
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. <ref>{{cite journal | vauthors = Khandelwal A, Crowley VM, Blagg BS | title = Resorcinol-Based Grp94-Selective Inhibitors | language = EN | journal = ACS Medicinal Chemistry Letters | volume = 8 | issue = 10 | pages = 1013–1018 | date = October 2017 | pmid = 29057043 | pmc = 5641966 | doi = 10.1021/acsmedchemlett.7b00193 | url = https://pubs.acs.org/doi/abs/10.1021/acsmedchemlett.7b00193 }}</ref>


== References ==
== References ==
{{Reflist}}
{{Reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Srivastava P | title = Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses | journal = Annual Review of Immunology | volume = 20 | issue = 1 | pages = 395–425 | year = 2001 | pmid = 11861608 | doi = 10.1146/annurev.immunol.20.100301.064801 }}
| citations =
* {{cite journal | vauthors = Li Z, Dai J, Zheng H, Liu B, Caudill M | title = An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response | journal = Frontiers in Bioscience | volume = 7 | issue =  | pages = d731-51 | date = March 2002 | pmid = 11861214 | doi = 10.2741/A808 }}
*{{cite journal | author=Srivastava P|title=Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. |journal=Annu Rev Immunol |volume=20 |issue= 1|pages= 395–425 |year= 2001 |pmid= 11861608 |doi=10.1146/annurev.immunol.20.100301.064801 }}
* {{cite journal | vauthors = Dollins DE, Warren JJ, Immormino RM, Gewirth DT | title = Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones | journal = Molecular Cell | volume = 28 | issue = 1 | pages = 41–56 | date = October 2007 | pmid = 17936703 | pmc = 2094010 | doi = 10.1016/j.molcel.2007.08.024 }}
*{{cite journal   |vauthors=Li Z, Dai J, Zheng H, etal |title=An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response. |journal=Front. Biosci. |volume=7 |issue=  |pages= d731–51 |year= 2002 |pmid= 11861214 |doi= 10.2741/A808 }}
* {{cite journal | vauthors = Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R | title = Mortalin: present and prospective | journal = Experimental Gerontology | volume = 37 | issue = 10-11 | pages = 1157–64 | year = 2003 | pmid = 12470827 | doi = 10.1016/S0531-5565(02)00135-3 }}
*{{cite journal   |vauthors=Dollins DE, etal |title=Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. |journal=Mol Cell |volume=28 |issue=1 |pages= 41–56 |year= 2007 |pmid= 17936703 |doi=10.1016/j.molcel.2007.08.024 | pmc=2094010  }}
* {{cite journal | vauthors = Schaiff WT, Hruska KA, McCourt DW, Green M, Schwartz BD | title = HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells | journal = The Journal of Experimental Medicine | volume = 176 | issue = 3 | pages = 657–66 | date = September 1992 | pmid = 1512535 | pmc = 2119345 | doi = 10.1084/jem.176.3.657 }}
*{{cite journal |vauthors=Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R |title=Mortalin: present and prospective. |journal=Exp. Gerontol. |volume=37 |issue= 10-11 |pages= 1157–64 |year= 2003 |pmid= 12470827 |doi=10.1016/S0531-5565(02)00135-3 }}
* {{cite journal | vauthors = Zolnierowicz S, Work C, Hutchison K, Fox IH | title = Partial separation of platelet and placental adenosine receptors from adenosine A2-like binding protein | journal = Molecular Pharmacology | volume = 37 | issue = 4 | pages = 554–9 | date = April 1990 | pmid = 2325637 | doi =  }}
*{{cite journal   |vauthors=Schaiff WT, Hruska KA, McCourt DW, etal |title=HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. |journal=J. Exp. Med. |volume=176 |issue= 3 |pages= 657–66 |year= 1992 |pmid= 1512535 |doi=10.1084/jem.176.3.657 | pmc=2119345  }}
* {{cite journal | vauthors = Hutchison KA, Nevins B, Perini F, Fox IH | title = Soluble and membrane-associated human low-affinity adenosine binding protein (adenotin): properties and homology with mammalian and avian stress proteins | journal = Biochemistry | volume = 29 | issue = 21 | pages = 5138–44 | date = May 1990 | pmid = 2378869 | doi = 10.1021/bi00473a020 }}
*{{cite journal |vauthors=Zolnierowicz S, Work C, Hutchison K, Fox IH |title=Partial separation of platelet and placental adenosine receptors from adenosine A2-like binding protein. |journal=Mol. Pharmacol. |volume=37 |issue= 4 |pages= 554–9 |year= 1990 |pmid= 2325637 |doi=  }}
* {{cite journal | vauthors = Chang SC, Erwin AE, Lee AS | title = Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors | journal = Molecular and Cellular Biology | volume = 9 | issue = 5 | pages = 2153–62 | date = May 1989 | pmid = 2546060 | pmc = 363009 | doi =  }}
*{{cite journal |vauthors=Hutchison KA, Nevins B, Perini F, Fox IH |title=Soluble and membrane-associated human low-affinity adenosine binding protein (adenotin): properties and homology with mammalian and avian stress proteins. |journal=Biochemistry |volume=29 |issue= 21 |pages= 5138–44 |year= 1990 |pmid= 2378869 |doi=10.1021/bi00473a020 }}
* {{cite journal | vauthors = Anderson SL, Shen T, Lou J, Xing L, Blachere NE, Srivastava PK, Rubin BY | title = The endoplasmic reticular heat shock protein gp96 is transcriptionally upregulated in interferon-treated cells | journal = The Journal of Experimental Medicine | volume = 180 | issue = 4 | pages = 1565–9 | date = October 1994 | pmid = 7523574 | pmc = 2191700 | doi = 10.1084/jem.180.4.1565 }}
*{{cite journal |vauthors=Chang SC, Erwin AE, Lee AS |title=Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors. |journal=Mol. Cell. Biol. |volume=9 |issue= 5 |pages= 2153–62 |year= 1989 |pmid= 2546060 |doi= | pmc=363009 }}
* {{cite journal | vauthors = Bruneau N, Lombardo D | title = Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase | journal = The Journal of Biological Chemistry | volume = 270 | issue = 22 | pages = 13524–33 | date = June 1995 | pmid = 7768954 | doi = 10.1074/jbc.270.22.13524 }}
*{{cite journal   |vauthors=Anderson SL, Shen T, Lou J, etal |title=The endoplasmic reticular heat shock protein gp96 is transcriptionally upregulated in interferon-treated cells. |journal=J. Exp. Med. |volume=180 |issue= 4 |pages= 1565–9 |year= 1994 |pmid= 7523574 |doi=10.1084/jem.180.4.1565 | pmc=2191700  }}
* {{cite journal | vauthors = Chavany C, Mimnaugh E, Miller P, Bitton R, Nguyen P, Trepel J, Whitesell L, Schnur R, Moyer J, Neckers L | title = p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2 | journal = The Journal of Biological Chemistry | volume = 271 | issue = 9 | pages = 4974–7 | date = March 1996 | pmid = 8617772 | doi = 10.1074/jbc.271.9.4974 }}
*{{cite journal |vauthors=Bruneau N, Lombardo D |title=Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13524–33 |year= 1995 |pmid= 7768954 |doi=10.1074/jbc.270.22.13524 }}
* {{cite journal | vauthors = Kuznetsov G, Chen LB, Nigam SK | title = Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum | journal = The Journal of Biological Chemistry | volume = 272 | issue = 5 | pages = 3057–63 | date = January 1997 | pmid = 9006956 | doi = 10.1074/jbc.272.5.3057 }}
*{{cite journal   |vauthors=Chavany C, Mimnaugh E, Miller P, etal |title=p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2. |journal=J. Biol. Chem. |volume=271 |issue= 9 |pages= 4974–7 |year= 1996 |pmid= 8617772 |doi= 10.1074/jbc.271.9.4974}}
* {{cite journal | vauthors = Hoshino T, Wang J, Devetten MP, Iwata N, Kajigaya S, Wise RJ, Liu JM, Youssoufian H | title = Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression | journal = Blood | volume = 91 | issue = 11 | pages = 4379–86 | date = June 1998 | pmid = 9596688 | doi =  }}
*{{cite journal |vauthors=Kuznetsov G, Chen LB, Nigam SK |title=Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 3057–63 |year= 1997 |pmid= 9006956 |doi=10.1074/jbc.272.5.3057 }}
* {{cite journal | vauthors = Linnik KM, Herscovitz H | title = 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 | journal = The Journal of Biological Chemistry | volume = 273 | issue = 33 | pages = 21368–73 | date = August 1998 | pmid = 9694898 | doi = 10.1074/jbc.273.33.21368 }}
*{{cite journal   |vauthors=Hoshino T, Wang J, Devetten MP, etal |title=Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression. |journal=Blood |volume=91 |issue= 11 |pages= 4379–86 |year= 1998 |pmid= 9596688 |doi=  }}
* {{cite journal | vauthors = Delom F, Lejeune PJ, Vinet L, Carayon P, Mallet B | title = Involvement of oxidative reactions and extracellular protein chaperones in the rescue of misassembled thyroglobulin in the follicular lumen | journal = Biochemical and Biophysical Research Communications | volume = 255 | issue = 2 | pages = 438–43 | date = February 1999 | pmid = 10049727 | doi = 10.1006/bbrc.1999.0229 }}
*{{cite journal |vauthors=Linnik KM, Herscovitz H |title=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. |journal=J. Biol. Chem. |volume=273 |issue= 33 |pages= 21368–73 |year= 1998 |pmid= 9694898 |doi=10.1074/jbc.273.33.21368 }}
* {{cite journal | vauthors = Reddy RK, Lu J, Lee AS | title = The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis | journal = The Journal of Biological Chemistry | volume = 274 | issue = 40 | pages = 28476–83 | date = October 1999 | pmid = 10497210 | doi = 10.1074/jbc.274.40.28476 }}
*{{cite journal   |vauthors=Delom F, Lejeune PJ, Vinet L, etal |title=Involvement of oxidative reactions and extracellular protein chaperones in the rescue of misassembled thyroglobulin in the follicular lumen. |journal=Biochem. Biophys. Res. Commun. |volume=255 |issue= 2 |pages= 438–43 |year= 1999 |pmid= 10049727 |doi= 10.1006/bbrc.1999.0229 }}
* {{cite journal | vauthors = Roher N, Sarno S, Miró F, Ruzzene M, Llorens F, Meggio F, Itarte E, Pinna LA, Plana M | title = The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme | journal = FEBS Letters | volume = 505 | issue = 1 | pages = 42–6 | date = September 2001 | pmid = 11557039 | doi = 10.1016/S0014-5793(01)02781-8 }}
*{{cite journal |vauthors=Reddy RK, Lu J, Lee AS |title=The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis. |journal=J. Biol. Chem. |volume=274 |issue= 40 |pages= 28476–83 |year= 1999 |pmid= 10497210 |doi=10.1074/jbc.274.40.28476 }}
* {{cite journal | vauthors = Vabulas RM, Braedel S, Hilf N, Singh-Jasuja H, Herter S, Ahmad-Nejad P, Kirschning CJ, Da Costa C, Rammensee HG, Wagner H, Schild H | title = The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway | journal = The Journal of Biological Chemistry | volume = 277 | issue = 23 | pages = 20847–53 | date = June 2002 | pmid = 11912201 | doi = 10.1074/jbc.M200425200 }}
*{{cite journal   |vauthors=Roher N, Sarno S, Miró F, etal |title=The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme. |journal=FEBS Lett. |volume=505 |issue= 1 |pages= 42–6 |year= 2001 |pmid= 11557039 |doi=10.1016/S0014-5793(01)02781-8 }}
* {{cite journal | vauthors = Shin HJ, Kim SS, Cho YH, Lee SG, Rho HM | title = Host cell proteins binding to the encapsidation signal epsilon in hepatitis B virus RNA | journal = Archives of Virology | volume = 147 | issue = 3 | pages = 471–91 | date = March 2002 | pmid = 11958450 | doi = 10.1007/s007050200001 }}
*{{cite journal   |vauthors=Vabulas RM, Braedel S, Hilf N, etal |title=The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20847–53 |year= 2002 |pmid= 11912201 |doi= 10.1074/jbc.M200425200 }}
*{{cite journal   |vauthors=Shin HJ, Kim SS, Cho YH, etal |title=Host cell proteins binding to the encapsidation signal epsilon in hepatitis B virus RNA. |journal=Arch. Virol. |volume=147 |issue= 3 |pages= 471–91 |year= 2002 |pmid= 11958450 |doi=10.1007/s007050200001 }}
}}
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[[Category:Molecular chaperones]]
[[Category:Endoplasmic reticulum resident proteins]]

Latest revision as of 15:56, 18 October 2018

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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

  1. ↑ Maki RG, Old LJ, Srivastava PK (August 1990). "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. doi:10.1073/pnas.87.15.5658. PMC 54386. PMID 2377606.
  2. ↑ Chen B, Piel WH, Gui L, Bruford E, Monteiro A (December 2005). "The HSP90 family of genes in the human genome: insights into their divergence and evolution". Genomics. 86 (6): 627–37. doi:10.1016/j.ygeno.2005.08.012. PMID 16269234.
  3. ↑ Randow F, Seed B (October 2001). "Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability". Nature Cell Biology. 3 (10): 891–6. doi:10.1038/ncb1001-891. PMID 11584270.
  4. ↑ Yang Y, Liu B, Dai J, Srivastava PK, Zammit DJ, Lefrançois L, Li Z (February 2007). "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. doi:10.1016/j.immuni.2006.12.005. PMC 2847270. PMID 17275357.,
  5. ↑ Schild H, Rammensee HG (August 2000). "gp96--the immune system's Swiss army knife". Nature Immunology. 1 (2): 100–1. doi:10.1038/77770. PMID 11248798.
  6. ↑ Wood CG, Mulders P (August 2009). "Vitespen: a preclinical and clinical review". Future Oncology. 5 (6): 763–74. doi:10.2217/fon.09.46. PMID 19663726.
  7. ↑ Tosti G, di Pietro A, Ferrucci PF, Testori A (November 2009). "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. doi:10.1586/erv.09.108. PMID 19863242.
  8. ↑ "NCT00293423". ClinicalTrials.gov, United States National Institutes of Health. Retrieved 2010-04-10. GP96 Heat Shock Protein-Peptide Complex Vaccine in Treating Patients With Recurrent or Progressive Glioma
  9. ↑ Bloch O, Crane CA, Fuks Y, Kaur R, Aghi MK, Berger MS, Butowski NA, Chang SM, Clarke JL, McDermott MW, Prados MD, Sloan AE, Bruce JN, Parsa AT (January 2014). "Heat-shock protein peptide complex-96 vaccination for recurrent glioblastoma: a phase II, single-arm trial". Neuro-Oncology. 16 (2): 274–9. doi:10.1093/neuonc/not203. PMC 3895386. PMID 24335700.
  10. ↑ Khandelwal A, Crowley VM, Blagg BS (October 2017). "Resorcinol-Based Grp94-Selective Inhibitors". ACS Medicinal Chemistry Letters. 8 (10): 1013–1018. doi:10.1021/acsmedchemlett.7b00193. PMC 5641966. PMID 29057043.

Further reading


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