Induction of heat shock protein gp96 by immune cytokines

Chen, Y. G.; Ashok, Badithe T.; Liu, X.; Garikapaty, V.; Mittelman, Abraham; Tiwari, Raj K.

doi:10.1379/1466-1268(2003)008<0242:iohspg>2.0.co;2

Cited by 16 publications

(16 citation statements)

References 49 publications

(53 reference statements)

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“…gp96 (5 Ag) was loaded and resolved on a 12% SDS-PAGE gel (5,24). After 2 hours, the proteins were transferred at 200 mA for 2 hours on to a polyvinylidene difluoride membrane (PVDF, Millipore, Bedford, MA).…”

Section: Silver Staining and Western Blot Analysis Of Gp96mentioning

confidence: 99%

“…The proteins were transferred at 200 mA for 2 hours onto a PVDF membrane (Millipore; refs. 5,24). Detection of glycosylated gp96 using ConA-HRP was modified from the method used by Cala (21).…”

Section: In Vivo Glycosylation Of Gp96mentioning

confidence: 99%

“…The ability of gp96 to associate with cell-specific peptides led to the concept of using autologous gp96 as vaccines to treat disease (5,6). One particular area for the potential use of gp96 as a vaccine is in cancer therapy (5,6).…”

Section: Introductionmentioning

confidence: 99%

“…One particular area for the potential use of gp96 as a vaccine is in cancer therapy (5,6). Purified gp96-peptide complex(es) isolated from specific cancer tissues is able to elicit a cancerspecific immune response and tumor regression which has been observed in several animal models as well as human clinical trials (6)(7)(8)(9).…”

Section: Introductionmentioning

confidence: 99%

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Differences in Glycosylation Patterns of Heat Shock Protein, gp96: Implications for Prostate Cancer Prevention

et al. 2005

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Heat shock protein gp96 induces a tumor-specific protective immunity in a variety of experimental tumor models. Because the primary sequences of the glycoprotein, gp96 are identical between tumor and normal tissues, the peptides associated with gp96 and/or the posttranslational modifications of gp96, determine its immunogenicity. Gp96-associated peptides constitute the antigenic repertoire of the source tissue; thus, purified gp96-peptide complexes have clinical significance as autologous cancer vaccines. However, the role of altered glycosylation and its contribution in the biological as well as immunologic activity of gp96 still remains uncharacterized. We examined the cancer-specific glycosylation patterns of gp96. To this end, monosaccharide compositions of gp96 were compared between normal rat prostate and two cancerous rat prostate tissues, nonmetastatic/androgen-dependent Dunning G and metastatic/androgen-independent MAT-LyLu, as well as two human nonmetastatic prostate cancer cell lines, androgen-dependent LnCaP and androgen-independent DU145. Marked differences were observed between the gp96 monosaccharide compositions of the normal and cancerous tissues. Furthermore, gp96 molecules from more aggressive cellular transformations were found to carry decreasing quantities of several monosaccharides as well as sum total content of neutral and amino sugars. We believe that the unique glycosylation patterns contribute to cellular phenotype and that the posttranslational modifications of gp96 may affect its functional attributes. (Cancer Res 2005; 65(14): 6466-75)

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Section: Silver Staining and Western Blot Analysis Of Gp96mentioning

confidence: 99%

Section: In Vivo Glycosylation Of Gp96mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Differences in Glycosylation Patterns of Heat Shock Protein, gp96: Implications for Prostate Cancer Prevention

et al. 2005

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“…were unaffected by IFN- treatment in HepG2 cells although it was previously reported to upregulate Grp94 [27].…”

Section: Osm Induces the Expression Of Grp78 In Hepg2 Cellsmentioning

confidence: 79%

Oncostatin M up-regulates the ER chaperone Grp78/BiP in liver cells

Vollmer

Haan

Behrmann

2010

Biochemical Pharmacology

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International audienceOSM, a cytokine of the IL-6 type cytokine family, regulates inflammatory processes (acute phase, tissue remodeling, angiogenesis), cell differentiation and proliferation. Inflammation is discussed to favor carcinogenesis and the inflammatory cytokine OSM was lately described to upregulate HIF-1α, whose upregulation is also observed in many cancers. In this study we demonstrate that OSM, and to a lesser degree by IL-6, induces the expression of Grp78/BiP, an ER chaperone associated with tumor development and poor prognosis in cancer. In contrast, IFN-γ or TNF-α.had no effect on Grp78 expression. The up-regulation seems to be specific to liver cells, as it occurs in hepatocytes and hepatoma cells but not in prostate, melanoma, breast or kidney cells. OSM does not lead to up-regulation of Grp94, enhanced XBP-1 mRNA splicing or phosphorylation of eIF2α, indicating that it is not associated to a general ER stress response. Analysis of the underlying mechanism showed that Grp78 is up-regulated by transcriptional processes which are to the greater part, though not completely, dependent on MEK/Erk activation

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Fas Signaling in Macrophages Promotes Chronicity in K/BxN Serum–Induced Arthritis

Huang

Birkett

Koessler

et al. 2013

Arthritis & Rheumatology

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Objective A non-apoptotic role for Fas signaling has been implicated in the regulation of inflammation and innate immunity. These studies were performed to elucidate the role of Fas signaling on macrophages in the development of arthritis. Methods K/BxN serum transfer arthritis was induced in a mouse line with Fas conditionally deleted in the myeloid lineage (Fasf/f, LyzMcre). The arthritis was assessed clinically and histologically. IL-1β, CXCL5, IL-10, IL-6 and gp96 expression was determined by ELISA. Bone marrow derived macrophages were activated by IL-1β and gp96. Cells were analyzed for phenotype and apoptosis by flow cytometry. Results The onset of arthritis in Fasf/f, LyzMcre mice was comparable to that observed in control mice, however, resolution was accelerated during the chronic phase. The attenuated arthritis was associated with reduced articular expression of the endogenous TLR2 ligand gp96 and the neutrophil chemokine CXCL5, and the enhanced expression of IL-10. Activation with IL-1β or gp96 induced increased IL-10 in Fas deficient, compared with control, macrophages. IL-10 suppressed IL-1β plus gp96 induced IL-6 and CXCL5. IL-1β-mediated activation of ERK, which regulates IL-10 expression, was increased in Fas-deficient macrophages. Conclusions Together, our observations suggest that impaired Fas signaling results in the enhanced expression of anti-inflammatory IL-10 and reduced gp96, which are associated with accelerated resolution of inflammation in the chronic phase of arthritis. These observations suggest that strategies to reduce endogenous TLR ligands and increase IL-10 may be beneficial in patients with RA.

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Induction of heat shock protein gp96 by immune cytokines

Cited by 16 publications

References 49 publications

Differences in Glycosylation Patterns of Heat Shock Protein, gp96: Implications for Prostate Cancer Prevention

Differences in Glycosylation Patterns of Heat Shock Protein, gp96: Implications for Prostate Cancer Prevention

Oncostatin M up-regulates the ER chaperone Grp78/BiP in liver cells

Fas Signaling in Macrophages Promotes Chronicity in K/BxN Serum–Induced Arthritis

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