Contribution of CD14 and TLR4 to changes of the PI(4,5)P2 level in LPS-stimulated cells

Płóciennikowska, Agnieszka; Hromada-Judycka, Aneta; Dembińska, Justyna; Roszczenko, Paula; Ciesielska, Anna; Kwiatkowska, Katarzyna

doi:10.1189/jlb.2vma1215-577r

Cited by 25 publications

(22 citation statements)

References 48 publications

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“…CD14 exerts its effect on cell surfaces together with TLRs, which can also recognize PAMPs. CD14 can recognize LPS together with MD2/TLR4 and can recognize PGN, LTA or lipoprotein together with TLR2 . In addition, CD14 is a common receptor of TLR7 and TLR9 .…”

Section: Discussionmentioning

confidence: 99%

The outer membrane protein Tp92 of Treponema pallidum induces human mononuclear cell death and IL‐8 secretion

Luo

Zhang

Gan

et al. 2018

J Cellular Molecular Medi

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Treponema pallidum is the pathogen that causes syphilis, a sexually transmitted disease; however, the pathogenic mechanism of this organism remains unclear. Tp92 is the only T. pallidum outer membrane protein that has structural features similar to the outer membrane proteins of other Gram‐negative bacteria, but the exact functions of this protein remain unknown. In the present study, we demonstrated that the recombinant Tp92 protein can induce human mononuclear cell death. Tp92 mediated the human monocytic cell line derived from an acute monicytic leukemia patient (THP‐1) cell death by recognizing CD14 and/or TLR2 on cell surfaces. After the stimulation of THP‐1 cells by the Tp92 protein, Tp92 may induce atypical pyroptosis of THP‐1 cells via the pro‐caspase‐1 pathway. Meanwhile, this protein caused the apoptosis of THP‐1 cells via the receptor‐interacting protein kinase 1/caspase‐8/aspase‐3 pathway. Tp92 reduced the number of monocytes among peripheral blood mononuclear cells. Interestingly, further research showed that Tp92 failed to increase the tumour necrosis factor‐α, interleukin (IL)‐1β, IL‐6, IL‐10, IL‐18 and monocyte chemotactic protein 1 (MCP)‐1 levels but slightly elevated the IL‐8 levels via the Nuclear Factor (NF)‐κB pathway in THP‐1 cells. The data suggest that Tp92 recognizes CD14 and TLR2, transfers the signal to a downstream pathway, and activates NF‐κB to mediate the production of IL‐8. This mechanism may help T. pallidum escape recognition and elimination by the host innate immune system.

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Section: Discussionmentioning

confidence: 99%

The outer membrane protein Tp92 of Treponema pallidum induces human mononuclear cell death and IL‐8 secretion

Luo

Zhang

Gan

et al. 2018

J Cellular Molecular Medi

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“…Plasma membrane rafts of resting cells are now considered to be extremely labile nanometer-sized structures formed due to interactions of sphingolipids and cholesterol, with a contribution of cell-surface GPI-anchored proteins and S-palmitoylated transmembrane/peripheral proteins and their oligomerization. These dynamic nanodomains can merge together upon cell stimulation into more stable platforms, thereby causing local accumulation of distinct receptors, proteins engaged in their signaling pathways, and lipids involved in these signaling cascades, such as sphingolipids and phosphatidylinositols [82,88,[96][97][98][99][100][101].…”

Section: Association Of Flotillins With Rafts Facilitates Endocytosismentioning

confidence: 99%

Flotillins: At the Intersection of Protein S-Palmitoylation and Lipid-Mediated Signaling

Kwiatkowska

Matveichuk

Fronk

et al. 2020

IJMS

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Flotillin-1 and flotillin-2 are ubiquitously expressed, membrane-associated proteins involved in multifarious cellular events from cell signaling, endocytosis, and protein trafficking to gene expression. They also contribute to oncogenic signaling. Flotillins bind the cytosolic leaflet of the plasma membrane and endomembranes and, upon hetero-oligomerization, serve as scaffolds facilitating the assembly of multiprotein complexes at the membrane–cytosol interface. Additional functions unique to flotillin-1 have been discovered recently. The membrane-binding of flotillins is regulated by S-palmitoylation and N-myristoylation, hydrophobic interactions involving specific regions of the polypeptide chain and, to some extent, also by their oligomerization. All these factors endow flotillins with an ability to associate with the sphingolipid/cholesterol-rich plasma membrane domains called rafts. In this review, we focus on the critical input of lipids to the regulation of the flotillin association with rafts and thereby to their functioning. In particular, we discuss how the recent developments in the field of protein S-palmitoylation have contributed to the understanding of flotillin1/2-mediated processes, including endocytosis, and of those dependent exclusively on flotillin-1. We also emphasize that flotillins affect directly or indirectly the cellular levels of lipids involved in diverse signaling cascades, including sphingosine-1-phosphate and PI(4,5)P2. The mutual relations between flotillins and distinct lipids are key to the regulation of their involvement in numerous cellular processes.

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“…The response to LPS, found in sarcomere, lysosomes, early endosomes, and Golgi apparatus (19), also includes TIR domaincontaining adaptor-inducing IFN-␤ (TRIF) and TRIF-related adaptor molecule (TRAM) signaling. Some studies suggest that these two pathways are sequentially activated after stimulation of the Myd88 pathway where it initiates a TRIF/TRAM-dependent response, leading to type I IFN production (34).…”

Section: Bacteriamentioning

confidence: 99%

Epithelial immunity: priming defensive responses in the intestinal mucosa

Pardo-Camacho

González‐Castro

Rodiño-Janeiro

et al. 2018

American Journal of Physiology-Gastrointestinal and Liver Physi

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As the largest interface between the outside and internal milieu, the intestinal epithelium constitutes the first structural component facing potential luminal threats to homeostasis. This single-cell layer is the epicenter of a tightly regulated communication network between external and internal factors that converge to prime defensive responses aimed at limiting antigen penetration and the maintenance of intestinal barrier function. The defensive role developed by intestinal epithelial cells (IEC) relies largely on the variety of receptors they express at both extracellular (apical and basolateral) and intracellular compartments, and the capacity of IEC to communicate with immune and nervous systems. IEC recognize pathogen-associated molecules by innate receptors that promote the production of mucus, antimicrobial substances, and immune mediators. Epithelial cells are key to oral tolerance maintenance and also participate in adaptive immunity through the expression of immunoglobulin (Ig) receptors and by promoting local Ig class switch recombination. In IEC, different types of antigens can be sensed by multiple immune receptors that share signaling pathways to assure effective responses. Regulated defensive activity maintains intestinal homeostasis, whereas a breakdown in the control of epithelial immunity can increase the intestinal passage of luminal content and microbial invasion, leading to inflammation and tissue damage. In this review, we provide an updated overview of the type of immune receptors present in the human intestinal epithelium and the responses generated to promote effective barrier function and maintain mucosal homeostasis.

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Contribution of CD14 and TLR4 to changes of the PI(4,5)P2 level in LPS-stimulated cells

Cited by 25 publications

References 48 publications

The outer membrane protein Tp92 of Treponema pallidum induces human mononuclear cell death and IL‐8 secretion

The outer membrane protein Tp92 of Treponema pallidum induces human mononuclear cell death and IL‐8 secretion

Flotillins: At the Intersection of Protein S-Palmitoylation and Lipid-Mediated Signaling

Epithelial immunity: priming defensive responses in the intestinal mucosa

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