Gamma-interferon regulation of class II antigens on acute myelogenous leukemia cell lines

Yunis, Jörge J.; Band, H.A.; Bonneville, Françoise; Yunis, Edmond J.

doi:10.1016/0198-8859(88)90296-0

Cited by 10 publications

(14 citation statements)

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“…These findings are in accordance with results described above, where MAM was capable of interacting with monocytic cells expressing TLR2 and TLR4 (18). Indeed, we consider that the cross-talk that was previously reported between MAM and TLRs in monocytes and macrophages and leading to cell activation (18) is really due to the well-known presence of MHC class II molecules in these cells, in particular the HLA-DR (37). To further confirm our interpretation of these data, macrophages derived from SLJ mice that lack MAM-reactive MHC class II alleles as well as Chinese hamster ovary cells, which do not express any MHC molecules and that were transfected with CD14/TLR2 or CD14/TLR4, were shown to be irresponsive to the stimulation by MAM.…”

Section: Discussionsupporting

confidence: 82%

Coexpression of TLR2 or TLR4 with HLA-DR Potentiates the Superantigenic Activities ofMycoplasma arthritidis–Derived Mitogen

Shio

Hassan

Shah

et al. 2014

The Journal of Immunology

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Mycoplasma arthritidis–derived mitogen (MAM) is a member of the superantigen family that structurally differs from other members while still capable of initiating cognate APC/T cell interaction. In addition to the critical role of MHC class II molecules, it has been suggested that TLR2 and TLR4 may cooperate with MHC class II during MAM-induced responses. In this study, we investigated the direct involvement of TLR2 and TLR4 in MAM binding and presentation to T cells. Our results showed that MAM fails to bind to TLR2- and TLR4-transfected cells. However, coexpression of TLR2 or TLR4 with HLA-DR significantly increases MAM binding and the subsequent T cell activation compared with cells expressing HLA-DR alone. The upregulated MAM binding and activity in HLA-DR/TLR–transfected cells is abrogated by an anti–HLA-DR Ab. Interestingly, we also found that MAM complexed with soluble HLA-DR is capable of binding to both TLR2 and TLR4. The enhancing effect of TLR2 or TLR4 on MAM-induced T cell proliferation was not due to TLR ligand contamination in the MAM preparation. Taken together, these results strongly suggest that binding of MAM to HLA-DR leads to a conformational change in MAM structure allowing its interaction with TLR2 and TLR4 and a better recognition by T cells.

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Section: Discussionsupporting

confidence: 82%

Coexpression of TLR2 or TLR4 with HLA-DR Potentiates the Superantigenic Activities ofMycoplasma arthritidis–Derived Mitogen

Shio

Hassan

Shah

et al. 2014

The Journal of Immunology

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“…Should hXBP-1 associate with c-fos in vivo (as these data suggest), the heterodimeric complex would constitute a new transcriptional activator, which would further expand the combinatorial possibilities for gene regulation by the leucine zipper class of proteins. These data also complement the description of cell lines that express DR and DP but not DQ (42,43) or DQ but not DP or DR (45). These data emphasize the independent regulation of expression ofthe three isotypes of class II MHC antigens.…”

Section: Resultssupporting

confidence: 58%

Transcription of a subset of human class II major histocompatibility complex genes is regulated by a nucleoprotein complex that contains c-fos or an antigenically related protein.

Ono

Bažil

Levi

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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Transcription of a subset of human class II major histocompatibility complex genes is regulated by a nucleoprotein complex that contains c-fos or an antigenically related protein ( Contributed by Jack L. Strominger, December 20, 1990 ABSTRACT Transcriptional regulation of the human major histocompatibility complex class II genes requires at least two upstream elements, the X and Y boxes, located in the -50-to -150-base-pair region of all class II promoters. The DRA and DPB promoters contain phorbol ester-responsive elements overlapping the 3' side of their X boxes. Mutation of this sequence down-regulates the efficiency of the DRA promoter, suggesting that a positive regulator(s) binds to this site. In this report, anti-sense c-os RNA and an anti-c-fos antibody were used to show that the product of the protooncogene c-fos or an antigenically related protein is a component of a complex that binds to the X box and is required for maximal transcription from the DRA and DPB promoters. As c-fos (or its related proteins) cannot bind alone to DNA, these results suggest that it may dimerize with other members of the JUN/AP-I family, such as hXBP1, to participate in the activation of a subset of class II major histocompatibility complex genes.

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“…HL-60 promyelocytic cells do not synthesize episialin/MUC1, but expression of several genes can be induced by IFN-␥, including the Fc receptor and MHC molecules (47,48). Although bandshift experiments revealed that in these cells STAT1 is strongly activated and binds to the STAT site in the episialin/MUC1 promoter upon IFN-␥ treatment (Fig.…”

Section: Induction Of Endogenous Episialin/muc1 By Cytokines Inmentioning

confidence: 99%

A STAT-responsive Element in the Promoter of the Episialin/MUC1 Gene Is Involved in Its Overexpression in Carcinoma Cells

Gaemers¹,

Vos²,

Volders

et al. 2001

Journal of Biological Chemistry

123

118

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The mucin-like glycoprotein episialin (MUC1) is highly overproduced by a number of human carcinomas. We have shown previously in a variety of mammalian cell lines that overexpression of this very large transmembrane molecule diminishes cellular adhesion, suggesting that episialin/MUC1 overexpression may play an important role in tumor invasion and metastasis. By using in situ hybridization, we show here that episialin/ MUC1 mRNA expression can be increased more than 10-fold in breast carcinoma cells relative to the expression in adjacent normal breast epithelium. In search of the molecular mechanism of this overexpression, we observed that the episialin/MUC1 promoter contains a candidate binding site for transcription factors of the STAT family ϳ500 base pairs upstream of the transcription start site. Cytokines and/or growth factors such as interleukin-6 or interferon-␥ can activate STATs. In the human breast carcinoma cell line T47D, both compounds are able to stimulate transcription of a luciferase reporter gene under the control of a 750-base pair MUC1 promoter fragment proximal to the transcription start site. The observed increase is entirely mediated by the single STAT-binding site, since mutation of this site abolishes stimulation of the reporter by interleukin-6 and interferon-␥. In addition, mutation of the STAT site also decreased the promoter activity in nonstimulated T47D cells, suggesting that the STAT-binding site is among the elements that are involved in the overexpression of MUC1 in tumor cells. Episialin/MUC11 (also known as MUC1, PEM, CA 15-3 antigen, or EMA) is a transmembrane molecule with a large extracellular mucin-like domain. In normal cells episialin/ MUC1 is exclusively present at the apical side of the cell, but in carcinoma cells normal polarization is lost and episialin/MUC1 co-localizes with adhesion molecules such as integrins and cadherins. The long and relatively rigid extracellular domain of episialin/MUC1 can shield these adhesion molecules and diminish cellular adhesion, if present at a sufficiently high density on the cell surface (1-3). Overexpression of episialin/MUC1 in carcinoma cells has been frequently reported (4 -6) and is expected to have a similar effect on cellular behavior as loss of E-cadherin, the major epithelial cell-cell adhesion molecule, which has been shown to promote invasion and metastasis of carcinoma cells (for review see Refs. 7-9). Therefore, we have proposed that episialin/MUC1 also plays an important role in invasion and metastasis in vivo (10). Indeed, transgenic mice overexpressing episialin/MUC1 develop more aggressive lung tumors than nontransgenic mice, 2 whereas episialin/MUC1 null mice show a slower rate of tumor progression (11).Recent reports have shown that episialin overexpression in various types of neoplasia correlates with poor survival (12)(13)(14). Episialin/MUC1 is also the antigen that is measured in the CA 15-3 assay (the main blood marker to detect recurrence of breast cancer), and it is a molecule that is widely considered as ...

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Gamma-interferon regulation of class II antigens on acute myelogenous leukemia cell lines

Cited by 10 publications

References 0 publications

Coexpression of TLR2 or TLR4 with HLA-DR Potentiates the Superantigenic Activities ofMycoplasma arthritidis–Derived Mitogen

Coexpression of TLR2 or TLR4 with HLA-DR Potentiates the Superantigenic Activities ofMycoplasma arthritidis–Derived Mitogen

Transcription of a subset of human class II major histocompatibility complex genes is regulated by a nucleoprotein complex that contains c-fos or an antigenically related protein.

A STAT-responsive Element in the Promoter of the Episialin/MUC1 Gene Is Involved in Its Overexpression in Carcinoma Cells

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