HSP90B1
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| Location (UCSC) | Chr 12: 103.93 – 103.95 Mb | Chr 10: 86.53 – 86.54 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
Heat shock protein 90kDa beta member 1 (HSP90B1), known also as endoplasmin, gp96, grp94, or ERp99, is a
HSP90B1 is an
adaptive immunity.[9] Tumor-derived HSP90B1 (vitespen) has entered clinical trials for cancer immunotherapy.[10][11][12][13]
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.[14]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000166598 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020048 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 2377606.
- PMID 16269234.
- S2CID 26559580.
- PMID 17275357.,
- S2CID 29571184.
- PMID 19663726.
- S2CID 207223461.
- ^ "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
- PMID 24335700.
- PMID 29057043.
Further reading
- Srivastava P (2001). "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. PMID 11861608.
- Li Z, Dai J, Zheng H, Liu B, Caudill M (March 2002). "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. PMID 11861214.
- Dollins DE, Warren JJ, Immormino RM, Gewirth DT (October 2007). "Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones". Molecular Cell. 28 (1): 41–56. PMID 17936703.
- Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R (2003). "Mortalin: present and prospective". Experimental Gerontology. 37 (10–11): 1157–64. S2CID 44450296.
- Schaiff WT, Hruska KA, McCourt DW, Green M, Schwartz BD (September 1992). "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. PMID 1512535.
- Zolnierowicz S, Work C, Hutchison K, Fox IH (April 1990). "Partial separation of platelet and placental adenosine receptors from adenosine A2-like binding protein". Molecular Pharmacology. 37 (4): 554–9. PMID 2325637.
- Hutchison KA, Nevins B, Perini F, Fox IH (May 1990). "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. PMID 2378869.
- Chang SC, Erwin AE, Lee AS (May 1989). "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. PMID 2546060.
- Anderson SL, Shen T, Lou J, Xing L, Blachere NE, Srivastava PK, Rubin BY (October 1994). "The endoplasmic reticular heat shock protein gp96 is transcriptionally upregulated in interferon-treated cells". The Journal of Experimental Medicine. 180 (4): 1565–9. PMID 7523574.
- Bruneau N, Lombardo D (June 1995). "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. PMID 7768954.
- Chavany C, Mimnaugh E, Miller P, Bitton R, Nguyen P, Trepel J, Whitesell L, Schnur R, Moyer J, Neckers L (March 1996). "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. PMID 8617772.
- Kuznetsov G, Chen LB, Nigam SK (January 1997). "Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum". The Journal of Biological Chemistry. 272 (5): 3057–63. PMID 9006956.
- Hoshino T, Wang J, Devetten MP, Iwata N, Kajigaya S, Wise RJ, Liu JM, Youssoufian H (June 1998). "Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression". Blood. 91 (11): 4379–86. PMID 9596688.
- Linnik KM, Herscovitz H (August 1998). "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. PMID 9694898.
- Delom F, Lejeune PJ, Vinet L, Carayon P, Mallet B (February 1999). "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. PMID 10049727.
- Reddy RK, Lu J, Lee AS (October 1999). "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. PMID 10497210.
- Roher N, Sarno S, Miró F, Ruzzene M, Llorens F, Meggio F, Itarte E, Pinna LA, Plana M (September 2001). "The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme". FEBS Letters. 505 (1): 42–6. S2CID 52949128.
- 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 (June 2002). "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. PMID 11912201.
- Shin HJ, Kim SS, Cho YH, Lee SG, Rho HM (March 2002). "Host cell proteins binding to the encapsidation signal epsilon in hepatitis B virus RNA". Archives of Virology. 147 (3): 471–91. S2CID 23653290.
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