Extensive Repertoire of Membrane-bound and Soluble Dendritic Cell-specific ICAM-3-grabbing Nonintegrin 1 (DC-SIGN1) and DC-SIGN2 Isoforms

Mummidi, Srinivas; Catano, Gabriel; Lam, LeeAnn; Hoefle, Angelina; Telles, Vanessa; Begum, Kazi; Jiménez, Fabio; Ahuja, Seema S.; Ahuja, Sunil K.

doi:10.1074/jbc.m009807200

Cited by 97 publications

(85 citation statements)

References 98 publications

(98 reference statements)

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“…Tissue-specific Activity of the DC-SIGN Promoter-Besides MDDC and ⌬⌬M⌽ (6 -10), DC-SIGN expression can be seen on THP-1 myeloid cells but not on lymphoid or erythroleukemic cell lines like Jurkat or K562 cells (10,35) (Fig. 1, A and B).…”

Section: Resultsmentioning

confidence: 99%

PU.1 Regulates the Tissue-specific Expression of Dendritic Cell-specific Intercellular Adhesion Molecule (ICAM)-3-grabbing Nonintegrin

Domínguez-Soto¹,

Puig‐Kröger²,

Vega

et al. 2005

Journal of Biological Chemistry

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Dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) is a cell surface C-type lectin expressed on myeloid dendritic cells and certain tissue macrophages, which mediates antigen capture for processing and presentation and participates in intercellular interactions with naive T lymphocytes or endothelial cells. In their strategy to evade immunosurveillance, numerous pathogenic microorganisms, including human immunodeficiency virus and Mycobacterium, bind to DC-SIGN in order to gain access to dendritic cells. We present evidence that PU.1 dictates the basal and cell-specific activity of DC-SIGN gene-regulatory region through in vivo occupancy of two functional Ets elements, whose integrity is required for PU.1 responsiveness and for the cooperative actions of PU.1 and other transcription factors (Myb, RUNX) on the DC-SIGN gene proximal regulatory region. In addition, protein analysis and gene profiling experiments indicate that DC-SIGN and PU.1 are coordinately expressed upon classical and alternative macrophage activation and during dendritic cell maturation. Moreover, small interfering RNA-mediated reduction of PU.1 expression results in diminished DC-SIGN cellular levels. Altogether, these results indicate that PU.1 is involved in the myeloid-specific expression of DC-SIGN in myeloid cells, a contribution that can be framed within the role that PU.1 has on the acquisition of the antigen uptake molecular repertoire by dendritic cells and macrophages.

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Section: Resultsmentioning

confidence: 99%

PU.1 Regulates the Tissue-specific Expression of Dendritic Cell-specific Intercellular Adhesion Molecule (ICAM)-3-grabbing Nonintegrin

Domínguez-Soto¹,

Puig‐Kröger²,

Vega

et al. 2005

Journal of Biological Chemistry

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“…Like other members of the C-type lectin superfamily, numerous DC-SIGN mRNA species have been identified in MDDC that would encode molecules lacking a transmembrane domain or containing shortened or alternative "neck" and cytoplasmic domains (26). Although the subcellular location and recognition properties of these potential isoforms remain unknown, it is tempting to speculate that they might exhibit altered recognition and/or signaling capabilities, thus modulating the functionality of the prototypical membranebound DC-SIGN molecules.…”

Section: Fig 5 Dc-sign-dependent Functions Exhibited By Bryostatin mentioning

confidence: 99%

“…Preliminary experiments indicated that DC-SIGN mRNA was optimally amplified after 35 cycles of denaturation (95°C, 45 s), annealing (62°C, 45 s), and extension (72°C, 1 min), followed by a 10-min extension step at 72°C. Oligonucleotides used for DC-SIGN mRNA amplification (CD209sense: 5Ј-GGGAATTCAGAGTGGGGTGA-CATGAGTGAC-3Ј and CD209antisense: 5Ј-CCCCAAGCTTGTGAAGT-TCTGCTACGCAGGAG-3Ј) (15) include the whole coding region of the prototypical DC-SIGN isoform A (DC-SIGN A) (1,26). Amplification of DC-SIGN isoforms was accomplished using the primer pairs CD209sense/CD209antisense, CD209soluble/CD209antisense, and CD209ALTCYT/CD209antisense.…”

Section: Methodsmentioning

confidence: 99%

“…DC-SIGN mRNA species have been detected in MDDC, which encode membrane-bound, potentially soluble isoforms and isoforms with an alternative cytoplasmic tail (26). To characterize the DC-SIGN mRNA isoforms expressed upon differentiation in the presence of IL-4, RT-PCR analysis was performed on THP-1 cells treated with either PMA or PMA plus IL-4.…”

Section: Il-4 Alters the Pattern Of Dc-sign Isoforms And Favors The Amentioning

confidence: 99%

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Regulated Expression of the Pathogen Receptor Dendritic Cell-specific Intercellular Adhesion Molecule 3 (ICAM-3)-grabbing Nonintegrin in THP-1 Human Leukemic Cells, Monocytes, and Macrophages

Puig‐Kröger

Serrano‐Gómez

Caparrós

et al. 2004

Journal of Biological Chemistry

107

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“…The pattern of cellular expression of DC-SIGN is somewhat controversial. The term "DC-specific" DC-SIGN is also expressed on brain microvascular endothelial cells, certain tissue macrophages, can be induced on monocyte-derived macrophages under certain conditions and can even be found on rare CD14 + cells, resembling monocytes in blood [52][53][54][55] . Pathogenic microbes have evolved means to bypass these sentinels [56][57][58][59][60][61][62][63][64][65][66][67] .…”

Section: Questions To Be Answeredmentioning

confidence: 99%

DC-SIGN: Binding receptor for HCV?

Feng

Wang²,

Nie³

et al. 2004

WJG

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DC-SIGN, a dendritic Cell-specific adhesion receptor and a type II transmembrane mannose-binding C-type lectin, is very important in the function of DC, both in mediating naive T cell interactions through ICAM-3 and as a rolling receptor that mediates the DC-specific ICAM-2-dependent migration processes. It can be used by viral and bacterial pathogens including Human Immunodeficiency Virus (HIV), HCV, Ebola Virus, CMV and Mycobacterium tuberculosis to facilitate infection. Both DC-SIGN and DC-SIGNR can act either in cis, by concentrating virus on target cells, or in trans, by transmission of bound virus to a target cell expressing appropropriate entry receptors. Recent work showed that DC-SIGN are highaffinity binding receptors for HCV. Besides playing a role in entry into DC, HCV E2 interaction with DC-SIGN might also be detrimental for the interaction of DC with T cells during antigen presentation. The clinical strategies that target DC-SIGN may be successful in restricting HCV dissemination and pathogenesis as well as directing the migration of DCs to manipulate appropriate immune responses in autoimmunity and tumorigenic situations.

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Extensive Repertoire of Membrane-bound and Soluble Dendritic Cell-specific ICAM-3-grabbing Nonintegrin 1 (DC-SIGN1) and DC-SIGN2 Isoforms

Cited by 97 publications

References 98 publications

PU.1 Regulates the Tissue-specific Expression of Dendritic Cell-specific Intercellular Adhesion Molecule (ICAM)-3-grabbing Nonintegrin

PU.1 Regulates the Tissue-specific Expression of Dendritic Cell-specific Intercellular Adhesion Molecule (ICAM)-3-grabbing Nonintegrin

Regulated Expression of the Pathogen Receptor Dendritic Cell-specific Intercellular Adhesion Molecule 3 (ICAM-3)-grabbing Nonintegrin in THP-1 Human Leukemic Cells, Monocytes, and Macrophages

DC-SIGN: Binding receptor for HCV?

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