Interaction of Pulmonary Surfactant Protein C with CD14 and Lipopolysaccharide

Augusto, Luis; Synguélakis, Monique; Johansson, Jan; Pédron, Thierry; Girard, Robert; Chaby, Richard

doi:10.1128/iai.71.1.61-67.2003

Cited by 65 publications

(42 citation statements)

References 42 publications

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“…The a configuration of the terminal phosphate group at the reducing end of the lipid A disaccharide plays a determinant role in LPS recognition. We also demonstrated that CD14 shares with LPS the same binding region on SP-C, and that the interaction with SP-C modifies the conformation of CD14, allowing it to bind LPS more efficiently [118].…”

Section: Lps-binding Proteins In the Lungsmentioning

confidence: 90%

Lipopolysaccharide-binding molecules: transporters, blockers and sensors

Chaby¹

2004

CMLS, Cell. Mol. Life Sci.

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Lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria, can be beneficial to the host by activating the innate immune system, or harmful, by inducing inflammation, disseminated intravascular coagulation, multiple organ failure, shock and often death. On the bacteria, and in host biological fluids and cells, LPS is never free but constantly attached to cognate-binding proteins. Understanding how LPS is transported and further recognized by sensors able to deliver a signal, or by inactivating molecules able to neutralize its biological effects, is an important goal. This review describes the large panel of peptides and proteins reported to associate with LPS, and provides information on their origin, their structure and the location of amino acid residues involved in their interaction with LPS. A better understanding of the mode of recognition of LPS by cognate proteins prompted many laboratories to design on a rational basis synthetic molecules which can be used to detect low amounts of endotoxin, or to act as efficient blockers of in vitro and in vivo responses to LPS.

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Section: Lps-binding Proteins In the Lungsmentioning

confidence: 90%

Lipopolysaccharide-binding molecules: transporters, blockers and sensors

Chaby¹

2004

CMLS, Cell. Mol. Life Sci.

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“…Compared with nonchallenged control mice, LPS treatment significantly increased mRNA levels of LPA 1 and LPA 2 , without altering LPA 3 expression (Fig. 5, AϪC); however, Western blotting showed that LPS challenge increased protein expression of LPA [1][2][3] in lung tissues (Fig. 5, D and E).…”

Section: Involvement Of Lpa 1 In Lps-induced Signaling and Il-6mentioning

confidence: 99%

“…CD14 is known to be expressed in lipid rafts, which are plasma membrane microdomains that are enriched for cholesterol and sphingomyelin and characterized by insolubility in nonionic detergents (8,28). In addition to interaction with LPS, recent studies show that CD14 binds to surfactant proteins (2,4,32) and integrin-␤ 1 (22), suggesting involvement of additional new signaling pathways in CD14-regulated LPS-induced inflammation.…”

mentioning

confidence: 99%

Lysophosphatidic acid receptor 1 modulates lipopolysaccharide-induced inflammation in alveolar epithelial cells and murine lungs

Zhao

et al. 2011

American Journal of Physiology-Lung Cellular and Molecular Phys

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-Lysophosphatidic acid (LPA), a bioactive phospholipid, plays an important role in lung inflammation by inducing the release of chemokines and lipid mediators. Our previous studies have shown that LPA induces the secretion of interleukin-8 and prostaglandin E 2 in lung epithelial cells. Here, we demonstrate that LPA receptors contribute to lipopolysaccharide (LPS)-induced inflammation. Pretreatment with LPA receptor antagonist Ki16425 or downregulation of LPA receptor 1 (LPA 1) by small-interfering RNA (siRNA) attenuated LPS-induced phosphorylation of p38 MAPK, I-B kinase, and I-B in MLE12 epithelial cells. In addition, the blocking of LPA 1 also suppressed LPS-induced IL-6 production. Furthermore, LPS treatment promoted interaction between LPA 1 and CD14, a LPS coreceptor, in a time-and dose-dependent manner. Disruption of lipid rafts attenuated the interaction between LPA 1 and CD14. Mice challenged with LPS increased plasma LPA levels and enhanced expression of LPA receptors in lung tissues. To further investigate the role of LPA receptors in LPSinduced inflammation, wild-type, or LPA 1-deficient mice, or wildtype mice pretreated with Ki16425 were intratracheally challenged with LPS for 24 h. Knock down or inhibition of LPA 1 decreased LPS-induced IL-6 release in bronchoalveolar lavage (BAL) fluids and infiltration of cells into alveolar space compared with wild-type mice. However, no significant differences in total protein concentration in BAL fluids were observed. These results showed that knock down or inhibition of LPA1 offered significant protection against LPS-induced lung inflammation but not against pulmonary leak as observed in the murine model for lung injury. lysophospholipid; signal transduction; lipopolysaccharide; inflammation; acute lung injury; lysophosphatidic acid receptor 1; interleukin-6 ACUTE LUNG INJURY (ALI) is characterized by acute respiratory failure resulting from destruction of the epithelium-capillary interface, inflammation, and extravasations of protein-rich fluid (14,26,35). The lung epithelium is the site of first contact for both inflammatory and inhaled physical environmental stimuli, acting as a physical barrier between lung interstitium and environment (30,34). Disruption of epithelial barrier integrity results in paracellular leakage of relatively large proteins, such as albumin and immunoglobulin G, into alveolar spaces (15,18,19). Thus, the epithelium not only functions as a barrier but also secretes cytokines, chemokines, and lipid mediators to attract and activate a number of resident and infiltrating cells that play a role in airway inflammation (21, 25). Our previous studies have shown that bronchial epithelial cells release interleukin (IL)-8 (7, 43, 48), IL-6 (49), and prostaglandin E 2 (PGE 2 ) (17, 47) in response to bioactive lipid mediators and lipopolysaccharide (LPS), resulting in the infiltration of neutrophils into alveolar space (7, 47). The LPS-induced murine model of lung injury has been widely used to investigate mechanisms of ALI (18,31,40). Intratra...

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“…The hydrophobic proteins, SP-B and SP-C, are involved in organization and adsorption at the air-liquid interface (61), whereas the more hydrophilic proteins, SP-A and SP-D, do not have a primary role in the reduction of surface tension but are important components of antibody-independent innate lung immunity (22). It is known that each of the individual compo-nents in pulmonary surfactant (phospholipids, SP-A, SP-B, SP-C, and SP-D) can, by varying degrees, modulate host inflammatory mechanisms (5,21,27,61).…”

mentioning

confidence: 99%

Enhanced Lung Injury and Delayed Clearance ofPneumocystis cariniiin Surfactant Protein A-Deficient Mice: Attenuation of Cytokine Responses and Reactive Oxygen-Nitrogen Species

et al. 2004

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Surfactant protein A (SP-A Increases in SP-D content, gamma interferon, interleukin-4, interleukin-5, and tumor necrosis factor alpha in BAL fluid occurred but were attenuated in PCP-infected SP-A؊/؊ mice compared to WT mice. There were increases in total BAL NO levels in both infected groups, but nitrite levels were higher in SP-A ؊/؊ mice, indicating a reduction in production of higher oxides of nitrogen that was also reflected in lower levels of 3-nitrotyrosine staining in the SP-A ؊/؊ group. We conclude that despite increases in inflammatory cells, SP-A-deficient mice infected with P. carinii exhibit an enhanced susceptibility to the organism and attenuated production of proinflammatory cytokines and reactive oxygen-nitrogen species. These data support the concept that SP-A is a local effector molecule in the lung host defense against P. carinii in vivo.

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Interaction of Pulmonary Surfactant Protein C with CD14 and Lipopolysaccharide

Cited by 65 publications

References 42 publications

Lipopolysaccharide-binding molecules: transporters, blockers and sensors

Lipopolysaccharide-binding molecules: transporters, blockers and sensors

Lysophosphatidic acid receptor 1 modulates lipopolysaccharide-induced inflammation in alveolar epithelial cells and murine lungs

Enhanced Lung Injury and Delayed Clearance ofPneumocystis cariniiin Surfactant Protein A-Deficient Mice: Attenuation of Cytokine Responses and Reactive Oxygen-Nitrogen Species

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