Ceramide 1-Phosphate Mediates Endothelial Cell Invasion via the Annexin a2-p11 Heterotetrameric Protein Complex

Hankins, Jody L.; Ward, Katherine E.; Linton, Samuel S.; Barth, Brian M.; Stahelin, Robert V.; Fox, Todd E.; Kester, Mark

doi:10.1074/jbc.m113.481622

Cited by 42 publications

(30 citation statements)

References 66 publications

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“…C1P might exert its anti-inflammatory capacity by suppressing the activation of the NF-κB pathway. We support the argument of Hankins et al (7, 18, 58) that fluctuations in C1P levels determine its proinflammatory or anti-inflammatory effects, and further studies are required to clarify the interaction of C1P with the plasma membrane or possible delineated receptors, as well as the effect of C1P in specific cell types. C1P can act either as an intracellular second messenger (10) or as an extracellular mediator binding to functionally identified, but still not cloned, specific G protein–coupled receptor upon secretion to the extra-cellular milieu (11).…”

Section: Discussionsupporting

confidence: 86%

C1P Attenuates Lipopolysaccharide-Induced Acute Lung Injury by Preventing NF-κB Activation in Neutrophils

Baudiß

Vieira

Cicko

et al. 2016

The Journal of Immunology

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Recently, ceramide-1-phosphate (C1P) has been shown to modulate acute inflammatory events. Acute lung injury (Arnalich et al. 2000. Infect. Immun. 68: 1942–1945) is characterized by rapid alveolar injury, lung inflammation, induced cytokine production, neutrophil accumulation, and vascular leakage leading to lung edema. The aim of this study was to investigate the role of C1P during LPS-induced acute lung injury in mice. To evaluate the effect of C1P, we used a prophylactic and therapeutic LPS-induced ALI model in C57BL/6 male mice. Our studies revealed that intrapulmonary application of C1P before (prophylactic) or 24 h after (therapeutic) LPS instillation decreased neutrophil trafficking to the lung, proinflammatory cytokine levels in bronchoalveolar lavage, and alveolar capillary leakage. Mechanistically, C1P inhibited the LPS-triggered NF-κB levels in lung tissue in vivo. In addition, ex vivo experiments revealed that C1P also attenuates LPS-induced NF-κB phosphorylation and IL-8 production in human neutrophils. These results indicate C1P playing a role in dampening LPS-induced acute lung inflammation and suggest that C1P could be a valuable candidate for treatment of ALI.

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Section: Discussionsupporting

confidence: 86%

C1P Attenuates Lipopolysaccharide-Induced Acute Lung Injury by Preventing NF-κB Activation in Neutrophils

Baudiß

Vieira

Cicko

et al. 2016

The Journal of Immunology

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“…In addition, binding of C1P to the N-terminal lipid binding C2 domain of cPLA2-a was required for stimulation of this enzyme activity leading to the production of arachidonic acid and subsequent generation of prostaglandins . Moreover, it was recently reported that C1P binds the annexin a2/p11 heterotetrameric protein complex to elicit endothelial cell invasion (Hankins et al, 2013). The latter observation is consistent with our previous work showing that C1P potently stimulates macrophage migration Granado et al, 2009b).…”

Section: C1p Biologysupporting

confidence: 91%

Caged ceramide 1-phosphate (C1P) analogs: Novel tools for studying C1P biology

Gómez-Muñoz

Gangoiti

Rivera

et al. 2016

Chemistry and Physics of Lipids

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“…For cellular transport of C1P the recently identified C1P transport protein was shown to recognize the acyl amide moiety of C1P (Simanshu et al 2013), an interaction that may also provide selectivity for some sphingolipids when compared to their glycerophospholipid counterparts. Additionally, annexin A2 which has long been known to bind PS and PI(4,5)P 2 was recently shown to bind C1P with even higher affinity than that of PS or PA (Hankins et al 2012). Other proteins have also recently been identified that bind ceramide (Saddoughi et al 2013) as well as phosphorylated sphingolipids (Lamour et al 2011).…”

Section: Phosphoinositide-bindingmentioning

confidence: 99%

Cellular and molecular interactions of phosphoinositides and peripheral proteins

Stahelin

Scott

Frick

2014

Chemistry and Physics of Lipids

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Anionic lipids act as signals for the recruitment of proteins containing cationic clusters to biological membranes. A family of anionic lipids known as the phosphoinositides (PIPs) are low in abundance, yet play a critical role in recruitment of peripheral proteins to the membrane interface. PIPs are mono-, bis-, or trisphosphorylated derivatives of phosphatidylinositol (PI) yielding seven species with different structure and anionic charge. The differential spatial distribution and temporal appearance of PIPs is key to their role in communicating information to target proteins. Selective recognition of PIPs came into play with the discovery that the substrate of protein kinase C termed pleckstrin possessed the first PIP binding region termed the pleckstrin homology (PH) domain. Since the discovery of the PH domain, more than ten PIP binding domains have been identified including PH, ENTH, FYVE, PX, and C2 domains. Representative examples of each of these domains have been thoroughly characterized to understand how they coordinate PIP headgroups in membranes, translocate to specific membrane docking sites in the cell, and function to regulate the activity of their full-length proteins. In addition, a number of novel mechanisms of PIP-mediated membrane association have emerged, such as coincidence detection – specificity for two distinct lipid headgroups. Other PIP-binding domains may also harbor selectivity for a membrane physical property such as charge or membrane curvature. This review summarizes the current understanding of the cellular distribution of PIPs and their molecular interaction with peripheral proteins.

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Ceramide 1-Phosphate Mediates Endothelial Cell Invasion via the Annexin a2-p11 Heterotetrameric Protein Complex

Cited by 42 publications

References 66 publications

C1P Attenuates Lipopolysaccharide-Induced Acute Lung Injury by Preventing NF-κB Activation in Neutrophils

C1P Attenuates Lipopolysaccharide-Induced Acute Lung Injury by Preventing NF-κB Activation in Neutrophils

Caged ceramide 1-phosphate (C1P) analogs: Novel tools for studying C1P biology

Cellular and molecular interactions of phosphoinositides and peripheral proteins

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