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HSP90B1

March 17, 2024

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.[5][6]

HSP90B1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHSP90B1, ECGP, GP96, GRP94, HEL-S-125m, HEL35, TRA1, heat shock protein 90kDa beta family member 1, heat shock protein 90 beta family member 1
External IDsOMIM: 191175 MGI: 98817 HomoloGene: 2476 GeneCards: HSP90B1
Orthologs
SpeciesHumanMouse
Entrez

7184

22027

Ensembl

ENSG00000166598

ENSMUSG00000020048

UniProt

P14625

P08113

RefSeq (mRNA)

NM_003299

NM_011631

RefSeq (protein)

NP_003290

NP_035761

Location (UCSC)Chr 12: 103.93 – 103.95 MbChr 10: 86.53 – 86.54 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[7][8] It has been implicated as an essential immune chaperone to regulate both innate and 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 edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000166598 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020048 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. Bibcode:1990PNAS...87.5658M. doi:10.1073/pnas.87.15.5658. PMC 54386. PMID 2377606.
  6. ^ 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.
  7. ^ 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. S2CID 26559580.
  8. ^ 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.,
  9. ^ 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. S2CID 29571184.
  10. ^ 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.
  11. ^ 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. S2CID 207223461.
  12. ^ "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
  13. ^ 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.
  14. ^ 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 edit

  • 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. doi:10.1146/annurev.immunol.20.100301.064801. 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. doi:10.2741/A808. 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. doi:10.1016/j.molcel.2007.08.024. PMC 2094010. PMID 17936703.
  • Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R (2003). "Mortalin: present and prospective". Experimental Gerontology. 37 (10–11): 1157–64. doi:10.1016/S0531-5565(02)00135-3. PMID 12470827. 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. doi:10.1084/jem.176.3.657. PMC 2119345. 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. doi:10.1021/bi00473a020. 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. doi:10.1128/mcb.9.5.2153. PMC 363009. 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. doi:10.1084/jem.180.4.1565. PMC 2191700. 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. doi:10.1074/jbc.270.22.13524. 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. doi:10.1074/jbc.271.9.4974. 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. doi:10.1074/jbc.272.5.3057. 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. doi:10.1182/blood.v91.11.4379. 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. doi:10.1074/jbc.273.33.21368. 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. doi:10.1006/bbrc.1999.0229. 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. doi:10.1074/jbc.274.40.28476. 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. doi:10.1016/S0014-5793(01)02781-8. PMID 11557039. 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. doi:10.1074/jbc.M200425200. 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. doi:10.1007/s007050200001. PMID 11958450. S2CID 23653290.


 

This article on a gene on human chromosome 12 is a stub. You can help Wikipedia by expanding it.

March 17, 2024
hsp90b1, heat, shock, protein, 90kda, beta, member, known, also, endoplasmin, gp96, grp94, erp99, chaperone, protein, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes4nh9identifiersaliases, ecgp, gp96, grp94, 125m, h. 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 5 6 HSP90B1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes4NH9IdentifiersAliasesHSP90B1 ECGP GP96 GRP94 HEL S 125m HEL35 TRA1 heat shock protein 90kDa beta family member 1 heat shock protein 90 beta family member 1External IDsOMIM 191175 MGI 98817 HomoloGene 2476 GeneCards HSP90B1Gene location Human Chr Chromosome 12 human 1 Band12q23 3Start103 930 107 bp 1 End103 953 931 bp 1 Gene location Mouse Chr Chromosome 10 mouse 2 Band10 C1 10 43 05 cMStart86 526 073 bp 2 End86 541 373 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inright lobe of thyroid glandleft lobe of thyroid glandcorpus epididymispericardiumislet of Langerhansanterior pituitarypylorusAchilles tendoncaput epididymisendometriumTop expressed inmedullary collecting ductabdominal walldermisspermatocyterenal corpusclesupraoptic nucleusseminal vesiculacalvariasomitespermatidMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionnucleotide binding calcium ion binding unfolded protein binding low density lipoprotein particle receptor binding protein binding RNA binding protein phosphatase binding ATP bindingCellular componentcytosol endocytic vesicle lumen endoplasmic reticulum lumen endoplasmic reticulum membrane membrane focal adhesion extracellular matrix melanosome plasma membrane endoplasmic reticulum chaperone complex extracellular region midbody endoplasmic reticulum perinuclear region of cytoplasm extracellular exosome nucleus protein containing complex collagen containing extracellular matrixBiological processresponse to hypoxia response to stress protein folding in endoplasmic reticulum negative regulation of apoptotic process receptor mediated endocytosis response to endoplasmic reticulum stress toll like receptor signaling pathway regulation of phosphoprotein phosphatase activity ATF6 mediated unfolded protein response actin rod assembly retrograde protein transport ER to cytosol sequestering of calcium ion protein folding ubiquitin dependent ERAD pathway protein transport cellular response to ATP post translational protein modification cytokine mediated signaling pathwaySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez718422027EnsemblENSG00000166598ENSMUSG00000020048UniProtP14625P08113RefSeq mRNA NM 003299NM 011631RefSeq protein NP 003290NP 035761Location UCSC Chr 12 103 93 103 95 MbChr 10 86 53 86 54 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseHSP90B1 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 7 8 It has been implicated as an essential immune chaperone to regulate both innate and 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 edit 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 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 Bibcode 1990PNAS 87 5658M doi 10 1073 pnas 87 15 5658 PMC 54386 PMID 2377606 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 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 S2CID 26559580 Yang Y Liu B Dai J Srivastava PK Zammit DJ Lefrancois 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 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 S2CID 29571184 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 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 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 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 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 editSrivastava 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 doi 10 1146 annurev immunol 20 100301 064801 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 doi 10 2741 A808 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 doi 10 1016 j molcel 2007 08 024 PMC 2094010 PMID 17936703 Kaul SC Taira K Pereira Smith OM Wadhwa R 2003 Mortalin present and prospective Experimental Gerontology 37 10 11 1157 64 doi 10 1016 S0531 5565 02 00135 3 PMID 12470827 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 doi 10 1084 jem 176 3 657 PMC 2119345 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 doi 10 1021 bi00473a020 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 doi 10 1128 mcb 9 5 2153 PMC 363009 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 doi 10 1084 jem 180 4 1565 PMC 2191700 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 doi 10 1074 jbc 270 22 13524 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 doi 10 1074 jbc 271 9 4974 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 doi 10 1074 jbc 272 5 3057 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 doi 10 1182 blood v91 11 4379 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 doi 10 1074 jbc 273 33 21368 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 doi 10 1006 bbrc 1999 0229 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 doi 10 1074 jbc 274 40 28476 PMID 10497210 Roher N Sarno S Miro 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 doi 10 1016 S0014 5793 01 02781 8 PMID 11557039 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 doi 10 1074 jbc M200425200 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 doi 10 1007 s007050200001 PMID 11958450 S2CID 23653290 nbsp This article on a gene on human chromosome 12 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title HSP90B1 amp oldid 1142722595, wikipedia, wiki, book, books, library,

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