Identification of Genes Responsive to Solar Simulated UV Radiation in Human Monocyte-Derived Dendritic Cells

Fuente, Hortensia de la; Lamana, Amalia; Mittelbrunn, Marı́a; Pérez‐Gala, S.; González, Salvador; García‐Diez, Amaro; Vega, Miguel A.; Sánchez-Madrid, Francisco

doi:10.1371/journal.pone.0006735

Cited by 18 publications

(16 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, investigations using a combination of UVA+UVB radiation to simulate sun exposure on human dendritic cells reduced expression of the GAL1 and GAL3 genes, in addition to other mediators related to the inflammatory response 45. Thus, the data indicate an immunosuppressive role of CXL on keratocytes, aiding in the regulation of the inflammatory process and stabilisation of the corneal stroma degradation.…”

Section: Discussionmentioning

confidence: 83%

Evaluation of galectin-1 and galectin-3 as prospective biomarkers in keratoconus

et al. 2018

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 83%

Evaluation of galectin-1 and galectin-3 as prospective biomarkers in keratoconus

et al. 2018

View full text Add to dashboard Cite

show abstract

“…The source of the Gal-9 need not be the TG itself and could arrive via the blood stream from other sites. Raised levels of galectins that include Gal-9 have been reported in some stress situations (36–39), conditions where some heat shock proteins are elevated as well in some acute infections (40) that include HSV (41, 42). So called stress situations are a well recognized prequel to HSV reactivation, which can result in disease, or be without lesions (43, 44).…”

Section: Discussionmentioning

confidence: 99%

Influence of Galectin-9/Tim-3 Interaction on Herpes Simplex Virus-1 Latency

Reddy

Sehrawat

Suryawanshi

et al. 2011

The Journal of Immunology

View full text Add to dashboard Cite

After herpes simplex virus type 1 (HSV-1) infection, CD8+ T cells accumulate in the trigeminal ganglion (TG) and participate in the maintenance of latency. However, the mechanisms underlying intermittent virus reactivation are poorly understood. In this study, we demonstrate the role of an inhibitory interaction between Tim-3 expressing CD8+ T cells and galectin 9 (Gal-9) that could influence HSV-1 latency and reactivation. Accordingly, we show that the majority of Kb-gB tetramer specific CD8+T cells in the TG of HSV-1 infected mice express Tim-3, a molecule that delivers negative signals to CD8+ T cells upon engagement of its ligand Gal-9. Gal-9 was also up-regulated in the TG when replicating virus was present as well during latency. This could set the stage for Gal-9/Tim-3 interaction and this inhibitory interaction was responsible for reduced CD8+ T cell effector function in WT mice. Additionally, TG cell cultures exposed to recombinant Gal-9 in the latent phase caused apoptosis of majority of CD8+ T cells. Further, Gal-9 KO TG cultures showed delayed and reduced viral reactivation as compared to wild type cultures demonstrating the greater efficiency of CD8+ T cells to inhibit virus reactivation in the absence of Gal-9. Moreover, the addition of recombinant Gal-9 to ex vivo TG cultures induced enhanced viral reactivation compared to untreated controls. Our results demonstrate that the host homeostatic mechanism mediated by Gal-9/Tim-3 interaction on CD8+ T cells can influence the outcome of HSV-1 latent infection and manipulating Gal-9 signals might represent therapeutic means to inhibit HSV-1 reactivation from latency.

show abstract

“…Integrin-binding by TSPs is important for their activities in cell attachment, spreading, and migration. The best-characterized interaction is that of the Increased TSP-5/COMP synthesis by chondrocytes and synovial fibroblasts Recklies et al 1998 Ultraviolet B Decreased TSP-1 transcript in keratinocytes; increased TSP-1 transcript in dendritic cells Howell et al 2004;de la Fuente et al 2009 single RGD motif of TSP-1 with integrin avb3 and, to a lesser extent, with aIIbb3 (Table 4) Lawler and Hynes 1989). The availability of this RGD motif for integrinbinding is promoted by incomplete calcium ion loading or reduction of disulfide bonds within the type 3 repeats (Sun et al 1992;Kvansakul et al 2004).…”

Section: Major Binding Partnersmentioning

confidence: 99%

The Thrombospondins

Adams¹,

Lawler²

2011

Cold Spring Harbor Perspectives in Biology

381

397

View full text Add to dashboard Cite

Thrombospondins are evolutionarily conserved, calcium-binding glycoproteins that undergo transient or longer-term interactions with other extracellular matrix components. They share properties with other matrix molecules, cytokines, adaptor proteins, and chaperones, modulate the organization of collagen fibrils, and bind and localize an array of growth factors or proteases. At cell surfaces, interactions with an array of receptors activate celldependent signaling and phenotypic outcomes. Through these dynamic, pleiotropic, and context-dependent pathways, mammalian thrombospondins contribute to wound healing and angiogenesis, vessel wall biology, connective tissue organization, and synaptogenesis. We overview the domain organization and structure of thrombospondins, key features of their evolution, and their cell biology. We discuss their roles in vivo, associations with human disease, and ongoing translational applications. In many respects, we are only beginning to appreciate the important roles of these proteins in physiology and pathology.T hrombospondins (TSPs) comprise a conserved family of extracellular, oligomeric, multidomain, calcium-binding glycoproteins. In general, basal metazoa and protostomes encode a single TSP in their genomes and deuterostomes have multiple TSP genes. The TSPs of mammals have many complex tissue-specific roles, including activities in wound healing and angiogenesis, vessel wall biology, connective tissue organization, and synaptogenesis. These activities derive mechanistically from interactions with cell surfaces, growth factors, cytokines, or components of the extracellular matrix (ECM) that collectively regulate many aspects of cell phenotype. Emerging evidence on the functions of TSPs in invertebrates suggests that ancient functions include bridging activities in cell-cell and cell-ECM interactions. Knowledge of TSP domain structures provides a rational basis for understanding their roles in vivo and associations with human disease and is assisting ongoing translational applications. DOMAIN ARCHITECTURE AND DOMAIN STRUCTURESThe domain architectures of representative TSP polypeptides are shown in Figure 1A. The invariant carboxy-terminal regions comprise a series of EGF-like domains, thirteen calcium-binding type 3 repeats, and a carboxy-terminal domain structurally homologous to the L-type lectin

show abstract

Identification of Genes Responsive to Solar Simulated UV Radiation in Human Monocyte-Derived Dendritic Cells

Cited by 18 publications

References 49 publications

Evaluation of galectin-1 and galectin-3 as prospective biomarkers in keratoconus

Evaluation of galectin-1 and galectin-3 as prospective biomarkers in keratoconus

Influence of Galectin-9/Tim-3 Interaction on Herpes Simplex Virus-1 Latency

The Thrombospondins

Contact Info

Product

Resources

About