Suppression by<i>Candida albicans</i>β‐Glucan of Cytokine Release from Activated Human Monocytes and from T Cells in the Presence of Monocytes

Nakagawa, Yukari; Ohno, Naohito; Murai, Toshimi

doi:10.1086/368334

Cited by 52 publications

(40 citation statements)

References 8 publications

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“…Similar findings have been described earlier (Kikkert et al, 2007). Conversely, others have found that glucans from C. albicans suppress the LPS-induced IL-6 response (Nakagawa et al, 2003). The biological activity of (1,3)-β-glucans in vertebrates is complex and relates to their origin, size, molecular structure, purity, and cell type or receptor(s) involved (for reviews see Brown, 2006;Goodridge et al, 2009;Reid et al, 2009;Tsoni and Brown, 2008).…”

Section: Referencessupporting

confidence: 73%

Monocyte Activation Test (MAT) reliably detects pyrogens in parenteral formulations of human serum albumin

Perdomo-Morales

Pardo-Ruíz²,

Spreitzer³

et al. 2011

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Section: Referencessupporting

confidence: 73%

Monocyte Activation Test (MAT) reliably detects pyrogens in parenteral formulations of human serum albumin

Perdomo-Morales

Pardo-Ruíz²,

Spreitzer³

et al. 2011

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“…In some donors, a potentially activated CD3 low CD4 low T cell population was observed that had higher levels of bGR surface expression (data not shown). The presence of bGR has not previously been defined on lymphocytes, although we had detected Dectin-1 mRNA expression in B and T cell lines [10], and there are some reports that their activities can be influenced by these carbohydrates [31,32]. In addition to the recognition of b-glucans, the bGR on these cells may also be involved in mediating interactions with other lymphocytes through recognition of the unidentified endogenous ligand [9,10,13].…”

Section: Distribution Of the Bgr In Human Peripheral Blood Cellsmentioning

confidence: 71%

The human β‐glucan receptor is widely expressed and functionally equivalent to murine Dectin‐1 on primary cells

et al. 2005

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We identified the C-type-lectin-like receptor, Dectin-1, as the major receptor for fungal b-glucans on murine macrophages and have demonstrated that it plays a significant role in the cellular response to these carbohydrates. Using two novel, isoform-specific mAb, we show here that human Dectin-1, the b-glucan receptor (bGR), is widely expressed and present on all monocyte populations as well as macrophages, DC, neutrophils and eosinophils. This receptor is also expressed on B cells and a subpopulation of T cells, demonstrating that human Dectin-1 is not myeloid restricted. Both major functional bGR isoforms -bGR-A and bGR-B -were expressed by these cell populations in peripheral blood; however, only bGR-B was significantly expressed on mature monocyte-derived macrophages and immature DC, suggesting cell-specific control of isoform expression. Inflammatory cells, recruited in vivo using a new skin-window technique, demonstrated that Dectin-1 expression was not significantly modulated on macrophages during inflammation, but is decreased on recruited granulocytes. Despite previous reports detailing the involvement of other b-glucan receptors on mature human macrophages, we have demonstrated that Dectin-1 acted as the major b-glucan receptor on these cells and contributed to the inflammatory response to these carbohydrates.

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“…Sherwood et al (44) showed that glucan-phosphate attenuated the induction of LPS tolerance. In addition, ␤-glucan was able to suppress endotoxin-(TLR4)-induced release of proinflammatory cytokine and affect the NF-B pathway (30,43).…”

Section: Discussionmentioning

confidence: 99%

Short fungal fractions of β-1,3 glucans affect platelet activation

Vancraeyneste

Charlet

Guérardel

et al. 2016

American Journal of Physiology-Heart and Circulatory Physiology

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Platelets are capable of binding, aggregating, and internalizing microorganisms, which enhances the elimination of pathogens from the blood. The yeast Candida albicans is a pathobiont causing life-threatening invasive infections. Its cell wall contains ␤-1,3 glucans that are known to trigger a wide range of host cell activities and to circulate during infection. We studied the effect of ␤-1,3 glucan fractions (BGFs) consisting of diglucosides (Glc2), tetraglucosides (Glc4), and pentaglucosides (Glc5) on human platelets, their mechanisms of action, and their possible impact on host defenses. The effect of BGFs on the coagulation process was determined by measuring thrombin generation. Platelets pretreated with BGFs were analyzed in terms of activation, receptor expression, aggregation, and adhesion to neutrophils and to C. albicans. The results show that BGFs affected the endogenous thrombin potential in a concentration-dependent manner. For platelet activation, BGFs at a low concentration (2 mol/l) reduced ATP release and prevented the phosphorylation of protein kinase C. BGFs diminished the expression of P-selectin and the activation of ␣ IIb␤3. BGFs decreased platelet aggregation and the interaction between thrombin-stimulated platelets and neutrophils, fibrinogen, and C. albicans. GLc5 decreased ATP release and TGF-␤1 production in response to TLR4 upregulation in thrombin-stimulated platelets, but TLR4 blockage abolished the effect of BGFs on platelets. This study provides evidence that fungal pentaglucosides modulate platelet activity mediated via TLR4 stimulation and reduce platelet-neutrophil interaction.

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Suppression byCandida albicansβ‐Glucan of Cytokine Release from Activated Human Monocytes and from T Cells in the Presence of Monocytes

Cited by 52 publications

References 8 publications

Monocyte Activation Test (MAT) reliably detects pyrogens in parenteral formulations of human serum albumin

Monocyte Activation Test (MAT) reliably detects pyrogens in parenteral formulations of human serum albumin

The human β‐glucan receptor is widely expressed and functionally equivalent to murine Dectin‐1 on primary cells

Short fungal fractions of β-1,3 glucans affect platelet activation

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