Increased survival and reduced renal injury in MRL/lpr mice treated with a human Fcγ receptor II (CD32) peptide

Xi, Jun; Zhang, Gai P.; Qiao, Songlin; Guo, Jun; Wang, Xuan N.; Yang, Yan; Zhang, Li N.; Miao, X.W.; Zhao, Dong; Zhi, Yu; Cai, Shu J.; Luo, Jun; Deng, Ruiguang

doi:10.1111/j.1365-2567.2012.03553.x

Cited by 10 publications

(6 citation statements)

References 41 publications

(76 reference statements)

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“…Because there was no cancer cell-derived IgG in platelets and RP215 cannot bind to B lymphocytes-derived IgG, we confirmed that FcγRIIa interacted with cancer cell-derived IgG. Furthermore, treatment with a small molecule inhibitor, huRII6, that was shown to be a potent competitive inhibitor of IgG binding to recombinant FcγRIIa 40 reduced the expression of CD62P compared to the expression level after control peptide treatment (Fig. 8b, d).…”

Section: Resultssupporting

confidence: 57%

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Cancer cell-derived immunoglobulin G activates platelets by binding to platelet FcγRIIa

et al. 2019

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Tumor-associated thrombosis is the second leading risk factor for cancer patient death, and platelets activity is abnormal in cancer patients. Discovering the mechanism of platelet activation and providing effective targets for therapy are urgently needed. Cancer cell- derived IgG has been reported to regulate development of tumors. However, studies on the functions of cancer cell-derived IgG are quite limited. Here we investigated the potential role of cancer cell-derived IgG in platelet activation. We detected the expression of CD62P on platelets by flow cytometry and analyzed platelet function by platelets aggregation and ATP release. The content of IgG in cancer cell supernatants was detected by enzyme-linked immune sorbent assay. The distribution of cancer-derived IgG in cancer cells was analyzed by immunofluorescence assay. Western blot was performed to quantify the relative expression of FcγRIIa, syk, PLCγ2. The interaction between cancer cell-derived IgG and platelet FcγRIIa was analyzed by co-immunoprecipitation. The results showed that higher levels of CD62P were observed in cancer patients’ platelets compared with that of healthy volunteers. Cancer cell culture supernatants increased platelet CD62P and PAC-1 expression, sensitive platelet aggregation and ATP release in response to agonists, while blocking FcγRIIa or knocking down IgG reduced the activation of platelets. Coimmunoprecipitation results showed that cancer cell-derived IgG interacted directly with platelet FcγRIIa. In addition, platelet FcγRIIa was highly expressed in liver cancer patients. In summary, cancer cell-derived IgG interacted directly with FcγRIIa and activated platelets; targeting this interaction may be an approach to prevent and treat tumor-associated thrombosis.

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Section: Resultssupporting

confidence: 57%

“…8). Peptide huRII6 ( 154 CTGNIGYTLFSSK 166 ), which corresponds to the putative F-G loop of FcγRIIa, can interact with human IgG, inhibiting the binding of human IgG to soluble huFcγRIIa 40 . We found that platelets treated with huRII6 had a lower aggregation ability than the control group (Fig.…”

Section: Discussionmentioning

confidence: 99%

Cancer cell-derived immunoglobulin G activates platelets by binding to platelet FcγRIIa

et al. 2019

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“…13,22,30,49–51 Although it has been taken for granted that the host immune system would not be able to recognize embryonic stem cells because of their undifferentiated nature and the lack of expression of major histocompatibity complex (MHC) on their membrane, data from our flow cytometry studies (Fig. 3A) show that these cells can still be recognized and attacked by the host immune system (via IgG binding) for non-autologous transplantation.…”

Section: Resultsmentioning

confidence: 93%

“…To encapsulate cells for transplantation, besides allowing efficient transport of nutrients, oxygen, and metabolic products (including wastes and therapeutic agents), the microcapsule should have a shell permeability capable of blocking the humoral component of the immune system such as immunoglobulin G (IgG) as IgG binding to target cells could further induce undesired inammatory and immune responses that can cause cell death and implant failure. 13,22,30,[49][50][51] Although it has been taken for granted that the host immune system would not be able to recognize embryonic stem cells because of their undifferentiated nature and the lack of expression of the major histocompatibility complex (MHC) on their membranes, data from our ow cytometry studies (Fig. 3A) show that these cells can still be recognized and attacked by the host immune system (via IgG binding) for non-autologous transplantation.…”

Section: Capability Of the Aca Microcapsules For Immunoisolationmentioning

confidence: 94%

A novel core–shell microcapsule for encapsulation and 3D culture of embryonic stem cells

et al. 2013

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In this study, we report the preparation of a novel microcapsule of ~ 100 μm with a liquid (as compared to solid-like alginate hydrogel) core and an alginate-chitosan-alginate (ACA) shell for encapsulation and culture of embryonic stem (ES) cells in the miniaturized 3D space of the liquid core. Murine R1 ES cells cultured in the microcapsules were found to survive (> 90%) well and proliferate to form either a single aggregate of pluripotent cells or embryoid body (EB) of more differentiated cells in each microcapsule within 7 days, dependent on the culture medium used. This novel microcapsule technology allows massive production of the cell aggregates or EBs of uniform size and controllable pluripotency, which is important for the practical application of stem cell based therapy. Moreover, the semipermeable ACA shell was found to significantly reduce immunoglobulin G (IgG) binding to the encapsulated cells by up to 8.2 times, compared to non-encapsulated cardiac fibroblasts, mesenchymal stem cells, and ES cells. This reduction should minimize inflammatory and immune responses induced damage to the cells implanted in vivo becasue IgG binding is an important first step of the undesired host responses. Therefore, the ACA microcapsule with selective shell permeability should be of importance to advance the emerging cell-based medicine.

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“…While CD32 treatment did not reverse nephritis, there was a delayed onset of proteinuria and increased survival time [ 33 ]. A synthetic peptide from the membrane-proximal extracellular domain of Fc gamma receptor II was found to be a competitive inhibitor of IgG binding recombinant Fc receptor II in vitro and increased survival while decreasing proteinuria in MRL/lpr mice in vivo [ 34 ]. Taken together, glomerular deposition of C1q in the context of immune complexes, complement activation, and functional Fc gamma receptors appear to be necessary to cause renal damage [ 35 ].…”

Section: Complement and Lupus Nephritismentioning

confidence: 99%

The Pathogenesis of Lupus Nephritis

Grande¹

2014

J Clin Cell Immunol

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Lupus nephritis is a serious potential feature of systemic lupus erythematous (SLE). Though SLE typically cycles through periods of flares and remission, patients often eventually succumb to end-stage kidney or cardiovascular damage. This review of the pathogenesis of lupus nephritis examines the role of the complement cascade; the significance of autoantibodies, the breaking of tolerance, and the implications of altered apoptosis in breaking tolerance; and the contributions of adaptive immunity and cross-talk with the innate immune system in driving renal damage. Delineation of basic mechanisms underlying the development of acute and chronic renal damage in lupus nephritis can result in the continued development of more specific and effective treatments.

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Increased survival and reduced renal injury in MRL/lpr mice treated with a human Fcγ receptor II (CD32) peptide

Cited by 10 publications

References 41 publications

Cancer cell-derived immunoglobulin G activates platelets by binding to platelet FcγRIIa

Cancer cell-derived immunoglobulin G activates platelets by binding to platelet FcγRIIa

A novel core–shell microcapsule for encapsulation and 3D culture of embryonic stem cells

The Pathogenesis of Lupus Nephritis

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