Treatment of murine collagen‐induced arthritis by the stress protein BiP via interleukin‐4–producing regulatory T cells: A novel function for an ancient protein

Brownlie, Rebecca J.; Myers, Linda K.; Wooley, Paul H.; Corrigall, Valerie; Bodman‐Smith, Mark; Panayi, G. S.; Thompson, Stephen

doi:10.1002/art.21654

Cited by 76 publications

(80 citation statements)

References 29 publications

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“…Overproduction of IL-4 in NIT-GRP78-primed lymphocytes might then down-regulate the killing ability of Th1. Brownlie et al investigated the immunosuppressive function of GRP78 in arthritis, and found that GRP78 could suppress active collagen-induced arthritis by the induction of regulatory cells that act predominantly via IL-4 [28]. The results of the lowest necrosis in NIT-GRP78 cells cultured with NIT-GRP78-expanded lymphocytes, but a moderate necrosis cultured with NIT-EGFP-expanded lymphocytes, indicate that GRP78 might exert a protective and immunorepressive dual ability.…”

Section: Discussionmentioning

confidence: 99%

The immunosuppressive and protective ability of glucose-regulated protein 78 for improvement of alloimmunity in β cell transplantation

Wang

Liu

et al. 2007

Clinical and Experimental Immunology

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SummaryAn insulinoma cell line, NIT-1, transfected with glucose-regulated protein 78 (GRP78) was established, namely NIT-GRP78, and used to study the immunosuppressive and protective ability of GRP78. In extended cytotoxic T lymphocyte (CTL) killing assay, NIT-1-primed lymphocytes were more cytotoxic in killing b cells than NIT-GRP78-primed lymphocytes. Severe necrosis was observed only when the NIT-1-primed lymphocytes were cultured with NIT-1 b cells, but not with NIT-GRP78 cells. In addition, an increase of interleukin (IL)-4 secretion from b cell-primed splenocytes when GRP78 presence was observed in cytokine enzyme-linked immunosorbent assay (ELISA). Diabetic mice reached normoglycaemia promptly and gained weight after transplantation of either NIT-1 or NIT-GRP78 cells. However, the recipient mice transplanted with NIT-GRP78 cells lived much longer than those recipients transplanted with NIT-1 cells, which was due apparently to prolonged insulin production by the transplanted NIT-GRP78 cells. In fact, we observed a significant increase of insulin concentration after glucose stimulation of diabetic mice received NIT-GRP78 cells at day 7 post-transplantation. From the results we propose that GRP78 could have a dual function in both protecting NIT-1 cells from CTL-mediated lysis and stimulating a population of T helper 2 cells to down-regulate the immune response to the transplanted b cells.

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Section: Discussionmentioning

confidence: 99%

The immunosuppressive and protective ability of glucose-regulated protein 78 for improvement of alloimmunity in β cell transplantation

Wang

Liu

et al. 2007

Clinical and Experimental Immunology

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“…Treatment of macrophages with SubAB inhibits LPS-induced MCP-1 and TNF-␣ expression and protects mice from LPS-induced sepsis and the development of experimental arthritis (28). Administration of BiP may also reduce collageninduced arthritis and is being considered a potential therapeutic agent in patients with rheumatoid arthritis (12). Reducing agents also protect cells from ER stress (32).…”

Section: Modulators Of Er Stressmentioning

confidence: 98%

The endoplasmic reticulum stress response and diabetic kidney disease

Cunard

Sharma

2011

American Journal of Physiology-Renal Physiology

118

112

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The endoplasmic reticulum (ER) folds and modifies proteins; however, during conditions of cellular stress, unfolded proteins accumulate in the ER and activate the unfolded protein response (UPR). The UPR, also referred to as the ER stress response, activates three distinct signaling cascades that are designed to globally reduce transcription and translation. The three major arms of the mammalian UPR include 1) protein kinase RNA (PKR)-like ER kinase (PERK), 2) inositol-requiring protein-1 (IRE1α), and 3) activating transcription factor-6 (ATF6) pathways. The PERK pathway rapidly attenuates protein translation, whereas the ATF6 and IRE1α cascades transcriptionally upregulate ER chaperone genes that promote proper folding and ER-associated degradation (ERAD) of proteins. This integrated response in turn allows the folding machinery of the ER to catch up with the backlog of unfolded proteins. The ER stress response plays a role in a number of pathophysiological processes, including pancreatic β-cell failure and apoptosis. The goals of the current review are to familiarize investigators with cellular and tissue activation of this response in the rodent and human diabetic kidney. Additionally, we will review therapeutic modulators of the ER stress response and discuss their efficacy in models of diabetic kidney disease. The ER stress response has both protective and deleterious features. A better understanding of the molecular pathways regulated during this process in a cell- and disease-specific manner could reveal novel therapeutic strategies in chronic renal diseases, including diabetic kidney disease.

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“…However, it has recently become apparent that certain molecular chaperones such as HSP10 [17] and BiP [18] act to inhibit the pro-inflammatory actions of myeloid cells. Indeed, HSP10 has recently been shown to inhibit joint inflammation in patients with rheumatoid arthritis [19].…”

Section: Introductionmentioning

confidence: 99%

Differential Regulation of Circulating Levels of Molecular Chaperones in Patients Undergoing Treatment for Periodontal Disease

et al. 2007

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BackgroundEvidence is emerging that molecular chaperones, in addition to their intracellular protein folding actions, can act as intercellular signaling proteins with an ability to modulate leukocyte function. Recent evidence has also shown that these proteins can exist in the circulation and may be involved in disease pathogenesis. We have used periodontitis and its treatment as a model of inflammation in the human to determine its effects on levels of circulating HSP10, HSP60 and BiP.Methodology/Principal FindingsA group of periodontal patients and matched controls were examined at the beginning of the study and then at 1 day and 6 months following periodontal or control therapy. Plasma levels of HSP10, HSP60 and BiP were measured by immunoassay and related to other plasma measures of inflammation. Periodontal patients had significantly less circulating levels of HSP10 or BiP compared with the controls. In contrast, more periodontal patients had intermediate levels of HSP60. Treatment of the periodontitis caused an increase in plasma levels of HSP10 although it had no effect on BiP. Treatment had no influence of HSP60 levels. Plasma HSP10 levels after therapy correlated with markers of periodontal clinical improvement.Conclusions/SignificanceCirculating levels of molecular chaperones are influenced by local inflammation. HSP10 is known to be an anti-inflammatory factor. The marked decrease of this circulating protein in active inflammation and its recovery post-treatment suggests that it may have a role in controlling periodontal inflammation.

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Treatment of murine collagen‐induced arthritis by the stress protein BiP via interleukin‐4–producing regulatory T cells: A novel function for an ancient protein

Cited by 76 publications

References 29 publications

The immunosuppressive and protective ability of glucose-regulated protein 78 for improvement of alloimmunity in β cell transplantation

The immunosuppressive and protective ability of glucose-regulated protein 78 for improvement of alloimmunity in β cell transplantation

The endoplasmic reticulum stress response and diabetic kidney disease

Differential Regulation of Circulating Levels of Molecular Chaperones in Patients Undergoing Treatment for Periodontal Disease

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