Maturation of Human Monocyte-Derived Dendritic Cells Studied by Microarray Hybridization

Dietz, Allan B.; Bulur, Peggy A.; Knutson, Gaylord J.; Matasić, Richard; Vuk‐Pavlović, Stanimir

doi:10.1006/bbrc.2000.3372

Cited by 124 publications

(87 citation statements)

References 62 publications

(31 reference statements)

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“…We observed a significant increase in TNFRI mRNA in iDC-3d compared to monocytes. Moreover, consistent with a previous report [30], we found the mRNA level for the TNFRI gene remained stable in immature and mature DC. The transcript for chemokine receptor CCR5 was detected at a high level in iDC-3d.…”

Section: The Kinetics Of Gene Expression During the Differentiation Asupporting

confidence: 93%

Transcriptional profiles during the differentiation and maturation of monocyte-derived dendritic cells, analyzed using focused microarrays

Wei-xue

Fei

Zhu³

et al. 2009

Cellular and Molecular Biology Letters

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Dendritic cells (DC) are professional antigen-presenting cells capable of initiating primary immune responses. They have been intensively studied and are used in both basic immunology research and clinical immunotherapy. However, the genetic pathways leading to DC differentiation and maturation remain poorly understood. Using focused microarrays with oligonucletotide probes for 120 genes encoding co-stimulatory molecules, chemokines, chemokine receptors, cytokines, cytokine receptors, TLRs, and several other related molecules, we analyzed the kinetics of gene expression for the overall differentiation process of monocytes into mature DC. In parallel, we compared the transcriptional profiles in DC maturation in the presence of LPS, TNF-α or trimeric CD40L. We found similar transcriptional profiles for early immature DC and immature DC, respectively generated by culturing monocytes with GM-CSF and IL-4 for three or six days. We identified sets of common and stimulispecific genes, the expression of which changed following stimulation with LPS, TNF-α or CD40L. A dynamic analysis of the entire DC differentiation and maturation process showed that some important inflammatory and constitutive chemokines are transcribed in both immature and mature DC. light on the transcriptional kinetics of DC differentiation and maturation, and this method may also prove useful for identifying novel marker genes involved in DC functions.

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Section: The Kinetics Of Gene Expression During the Differentiation Asupporting

confidence: 93%

Transcriptional profiles during the differentiation and maturation of monocyte-derived dendritic cells, analyzed using focused microarrays

Wei-xue

Fei

Zhu³

et al. 2009

Cellular and Molecular Biology Letters

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“…44 and data not shown) have detected gal-1 expression in DCs. Importantly, gal-1 may be an autocrine regulatory factor for endothelial cells and DCs as it is for T cells.…”

Section: Discussionmentioning

confidence: 76%

Novel Innate Immune Functions for Galectin-1: Galectin-1 Inhibits Cell Fusion by Nipah Virus Envelope Glycoproteins and Augments Dendritic Cell Secretion of Proinflammatory Cytokines

Levroney

Aguilar

Fulcher

et al. 2005

The Journal of Immunology

150

162

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Galectin-1 (gal-1), an endogenous lectin secreted by a variety of cell types, has pleiotropic immunomodulatory functions, including regulation of lymphocyte survival and cytokine secretion in autoimmune, transplant disease, and parasitic infection models. However, the role of gal-1 in viral infections is unknown. Nipah virus (NiV) is an emerging pathogen that causes severe, often fatal, febrile encephalitis. The primary targets of NiV are endothelial cells. NiV infection of endothelial cells results in cell-cell fusion and syncytia formation triggered by the fusion (F) and attachment (G) envelope glycoproteins of NiV that bear glycan structures recognized by gal-1. In the present study, we report that NiV envelope-mediated cell-cell fusion is blocked by gal-1. This inhibition is specific to the Paramyxoviridae family because gal-1 did not inhibit fusion triggered by envelope glycoproteins of other viruses, including two retroviruses and a pox virus, but inhibited fusion triggered by envelope glycoproteins of the related Hendra virus and another paramyxovirus. The physiologic dimeric form of gal-1 is required for fusion inhibition because a monomeric gal-1 mutant had no inhibitory effect on cell fusion. gal-1 binds to specific N-glycans on NiV glycoproteins and aberrantly oligomerizes NiV-F and NiV-G, indicating a mechanism for fusion inhibition. gal-1 also increases dendritic cell production of proinflammatory cytokines such as IL-6, known to be protective in the setting of other viral diseases such as Ebola infections. Thus, gal-1 may have direct antiviral effects and may also augment the innate immune response against this emerging pathogen.

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“…This multivalence of galectin-9 could, as suggested by our data, cross-link L. major to mononuclear phagocytic cells and work as a macrophage receptor. Galectin-9 is expressed abundantly in T lymphocytes, dendritic cells, lymphatic epithelial cells, as well as various lymphatic tissues, and its expression and secretion increase substantially in antigen-activated peripheral blood mononuclear cells (46,65,66). A few days after the infection, Leishmania are drained into lymph nodes where activated lymphocytes likely secrete galectin-9, and it is possible that galectin-9 influences the development of manifestation through its paracrine mediation of L. major-macrophage interaction although further study is necessary to investigate the potential roles of galectin-9 as a Leishmania receptor.…”

Section: Discussionmentioning

confidence: 99%

Specific Recognition of Leishmania major Poly-β-galactosyl Epitopes by Galectin-9

Pelletier

Hashidate

Urashima

et al. 2003

Journal of Biological Chemistry

101

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Leishmania parasites are the causative agents of leishmaniasis, manifesting itself in a species-specific manner. The glycan epitopes on the parasite are suggested to be involved in the Leishmania pathogenesis. One of such established species-unique glycan structures is the poly-␤-galactosyl epitope (Gal␤1-3) n found on L. major, which can develop cutaneous infections with strong inflammatory responses. Interestingly, the polygalactosyl epitope is also suggested to be involved in the development of the parasites in its host vector, sand fly. Thus, the recognition of the galactosyl epitope by lectins expressed in host or sand fly should be implicated in the species-specific manifestations of leishmaniasis and in the parasite life cycle, respectively. We recently reported that one host ␤-galactoside-binding protein, galectin-3, can distinguish L. major from the other species through its binding to the poly-␤-galactosyl epitope, proposing a role for galectin-3 as an immunomodulator that could influence the L. major-specific immune responses in leishmaniasis. Here we report that galectin-9 can also recognize L. major by binding to the L. major-specific polygalactosyl epitope. Frontal affinity analysis with different lengths of poly-␤-galactosyllactose revealed that the galectin-9 affinity for polygalactose was enhanced in proportion to the number of Gal␤1-3 units present. Even though both galectins have comparable affinities toward the polygalactosyl epitopes, only galectin-9 can promote the interaction between L. major and macrophages, suggesting distinctive roles for the galectins in the L. major-specific development of leishmaniasis in the host.

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Maturation of Human Monocyte-Derived Dendritic Cells Studied by Microarray Hybridization

Cited by 124 publications

References 62 publications

Transcriptional profiles during the differentiation and maturation of monocyte-derived dendritic cells, analyzed using focused microarrays

Transcriptional profiles during the differentiation and maturation of monocyte-derived dendritic cells, analyzed using focused microarrays

Novel Innate Immune Functions for Galectin-1: Galectin-1 Inhibits Cell Fusion by Nipah Virus Envelope Glycoproteins and Augments Dendritic Cell Secretion of Proinflammatory Cytokines

Specific Recognition of Leishmania major Poly-β-galactosyl Epitopes by Galectin-9

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