Augmentation of reverse arthus reaction by mast cells in mice.

Zhang, Yan; Ramos, Bernard F.; Jakschik, Barbara A.

doi:10.1172/jci115385

Cited by 95 publications

(72 citation statements)

References 39 publications

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“…In a model of bacteriainduced inflammation the lack of mast cell-derived TNFa was associated with drastically reduced neutrofil influx, and significantly higher mortality [1,2]. Similar data suggesting the critical role played by mast cellderived TNF-a in certain types of inflammatory response were obtained using reverse Arthus reaction as an animal model of inflammatory state [3,4]. The special role for mast cells as a source of TNF-a might be explained by the presence of preformed cytokine protein in cytoplasmic granules that allows for its immediate release upon stimulation [5].…”

Section: Introductionsupporting

confidence: 62%

Efficient sorting of TNF‐alpha to rodent mast cell granules is dependent on N‐linked glycosylation

et al. 2006

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Mast cells play an important role at the early stages of immunological response to bacterial infections and parasite infestations. One of the major mast cell proinflammatory mediators is TNF‐α. Mast cells are considered the only cells capable of storing TNF‐α in cytoplasmic granules and rapidly releasing it upon activation. To determine what pathway is utilized to direct TNF‐α to cytoplasmic granules and what motifs are responsible for the sorting process, we constructed a fusion protein covering the full sequence of TNF‐α, N‐terminally fused to enhanced green fluorescent protein (EGFP). In rodent mast cells, such protein was sorted to secretory granules, and this process was inhibited by both brefeldin A and monensin. Considering the relationship between lysosomes and secretory granules and following TNF‐α sequence analysis, it was determined whether TNF‐α is sorted through the mannose‐6‐phosphate receptor (MPR)‐dependent pathway. We observed that ammonium chloride and tunicamycin blocked TNF‐α‐EGFP fusion protein delivery to secretory granules. In situ mutagenesis experiments confirmed the necessity of N‐linked glycosylation for efficient sorting of TNF‐α into rodent mast cell granules. In this work we established that TNF‐α travels from the ER to mast cell granules via a brefeldin A‐ and monensin‐sensitive route, utilizing the MPR‐dependent pathway, although this dependency does not seem to be absolute.

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Section: Introductionsupporting

confidence: 62%

Efficient sorting of TNF‐alpha to rodent mast cell granules is dependent on N‐linked glycosylation

et al. 2006

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“…Fc␥RIII signaling may further lead to the adherence of mBMMCs to fibronectin (34). Mast cells have also been shown in a mouse model to play a role in immune complex-induced injury, related to the expression of IgG receptors (35)(36)(37). The relationship of Fc␥RI expression reported in this paper to the expression of Fc␥RII and Fc␥RIII by human mast cells (Fig.…”

Section: Discussionmentioning

confidence: 54%

Expression of a Functional High-Affinity IgG Receptor, FcγRI, on Human Mast Cells: Up-Regulation by IFN-γ

Okayama

Kirshenbaum

Metcalfe

2000

The Journal of Immunology

170

152

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Biologically relevant activation of human mast cells through Fc receptors is believed to occur primarily through the high-affinity IgE receptor FcεRI. However, the demonstration in animal models that allergic reactions do not necessarily require Ag-specific IgE, nor the presence of a functional IgE receptor, and the clinical occurrence of some allergic reactions in situations where Ag-specific IgE appears to be lacking, led us to examine the hypothesis that human mast cells might express the high-affinity IgG receptor FcγRI and in turn be activated through aggregation of this receptor. We thus first determined by RT-PCR that resting human mast cells exhibit minimal message for FcγRI. We next found that IFN-γ up-regulated the expression of FcγRI. This was confirmed by flow cytometry, where FcγRI expression on human mast cells was increased from ∼2 to 44% by IFN-γ exposure. FcεRI, FcγRII, and FcγRIII expression was not affected. Scatchard plots were consisted with these data where the average binding sites for monomeric IgG1 (Ka = 4–5 × 108 M−1) increased from ∼2,400 to 12,100–17,300 per cell. Aggregation of FcγRI on human mast cells, and only after IFN-γ exposure, led to significant degranulation as evidenced by histamine release (24.5 ± 4.4%): and up-regulation of mRNA expression for specific cytokines including TNF-α, GM-CSF, IL-3 and IL-13. These findings thus suggest another mechanism by which human mast cells may be recruited into the inflammatory processes associated with some immunologic and infectious diseases.

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“…Inflammation caused by RPA depends on FcR and complement-mediated mechanisms (42)(43)(44), with early involvement of mast cells (45,46) and later contribution of macrophages (45). Several studies in which the C5aR has been pharmacologically targeted or genetically deleted provide compelling evidence for a critical role of C5a in initiating the inflammatory cascade in immune complex peritonitis (26,47).…”

Section: Discussionmentioning

confidence: 99%

Truncated and Full-Length Thioredoxin-1 Have Opposing Activating and Inhibitory Properties for Human Complement with Relevance to Endothelial Surfaces

King

Nowakowska

Karsten

et al. 2012

The Journal of Immunology

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Thioredoxin (Trx)-1 is a small, ubiquitously expressed redox-active protein with known important cytosolic functions. However, Trx1 is also upregulated in response to various stress stimuli, is found both at the cell surface and secreted into plasma, and has known anti-inflammatory and antiapoptotic properties. Previous animal studies have demonstrated that exogenous Trx1 delivery can have therapeutic effects in a number of disease models and have implicated an interaction of Trx1 with the complement system. We found that Trx1 is expressed in a redox-active form at the surface of HUVEC and acts as an inhibitor of complement deposition in a manner dependent on its Cys-Gly-Pro-Cys active site. Inhibition occurred at the point of the C5 convertase of complement, regulating production of C5a and the membrane attack complex. A truncated form of Trx1 also exists in vivo, Trx80, which has separate nonoverlapping functions compared with the full-length Trx1. We found that Trx80 activates the classical and alternative pathways of complement activation, leading to C5a production, but the inflammatory potential of this was also limited by the binding of inhibitors C4b-binding protein and factor H. This study adds a further role to the known anti-inflammatory properties of Trx1 and highlights the difference in function between the full-length and truncated forms.

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Augmentation of reverse arthus reaction by mast cells in mice.

Abstract: Immune complex-induced injury is an important pathogenic factor in antibody-mediated nephritis, systemic lupus erythematosus, rheumatoid arthritis, and other diseases. In

Cited by 95 publications

References 39 publications

Efficient sorting of TNF‐alpha to rodent mast cell granules is dependent on N‐linked glycosylation

Efficient sorting of TNF‐alpha to rodent mast cell granules is dependent on N‐linked glycosylation

Expression of a Functional High-Affinity IgG Receptor, FcγRI, on Human Mast Cells: Up-Regulation by IFN-γ

Truncated and Full-Length Thioredoxin-1 Have Opposing Activating and Inhibitory Properties for Human Complement with Relevance to Endothelial Surfaces

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