This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pugin, J.
Right arrow Articles by Tobias, P. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pugin, J.
Right arrow Articles by Tobias, P. S.

 Previous Article  |  Next Article 

Infect Immun, March 1998, p. 1174-1180, Vol. 66, No. 3
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Cell Activation Mediated by Glycosylphosphatidylinositol-Anchored or Transmembrane Forms of CD14dagger

J. Pugin,1 V. V. Kravchenko,2 J.-D. Lee,2 L. Kline,2 R. J. Ulevitch,2 and P. S. Tobias2,*

Division of Medical Intensive Care, University Hospital, 1211 Geneva 14, Switzerland,1 and Department of Immunology, The Scripps Research Institute, La Jolla, California 920372

Received 5 September 1997/Returned for modification 14 October 1997/Accepted 10 December 1997

CD14 is a glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein which functions as a receptor on myeloid cells for ligands derived from microbial pathogens such as lipopolysaccharide (LPS). We have studied the importance of the GPI tail of CD14 in signalling with the promonocytic cell line THP-1 expressing recombinant CD14 in a GPI-anchored form (THP1-wtCD14 cells) or in a transmembrane form (THP1-tmCD14). We found that, like other GPI-anchored molecules, GPI-anchored CD14 was recovered mainly from a Triton X-100-insoluble fraction, whereas transmembrane CD14 was fully soluble in Triton X-100. LPS induced cell activation of THP1-wtCD14 and of THP1-tmCD14 (protein tyrosine kinase phosphorylation, NF-kappa B activation, and cytokine production) in a very similar manner. However, anti-CD14 antibody-induced cross-linking caused a rapid calcium mobilization signal only in GPI-anchored CD14 cells. Studies with pharmacologic inhibitors of intracellular signalling events implicate phospholipase C and protein tyrosine kinases in the genesis of this antibody-induced calcium signal. Our results suggest that GPI anchoring and CD14 targeting to glycolipid-rich membrane microdomains are not required for LPS-mediated myeloid cell activation. GPI anchoring may however be important for other signalling functions, such as those events reflected by antibody cross-linking.

* Corresponding author. Mailing address: The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, CA 92037. Phone: (619) 784-8215. Fax: (619) 784-8239. E-mail: tobias{at}scripps.edu.

dagger Publication 9661-IMM of the Department of Immunology, The Scripps Research Institute.




This article has been cited by other articles:

  • Hajishengallis, G., Wang, M., Liang, S. (2009). Induction of Distinct TLR2-Mediated Proinflammatory and Proadhesive Signaling Pathways in Response to Porphyromonas gingivalis Fimbriae. J. Immunol. 182: 6690-6696 [Abstract] [Full Text]  
  • Lloyd-Jones, K. L., Kelly, M. M., Kubes, P. (2008). Varying Importance of Soluble and Membrane CD14 in Endothelial Detection of Lipopolysaccharide. J. Immunol. 181: 1446-1453 [Abstract] [Full Text]  
  • Cuschieri, J., Billigren, J., Maier, R. V. (2006). Endotoxin tolerance attenuates LPS-induced TLR4 mobilization to lipid rafts: a condition reversed by PKC activation. J. Leukoc. Biol. 80: 1289-1297 [Abstract] [Full Text]  
  • Harokopakis, E., Albzreh, M. H., Martin, M. H., Hajishengallis, G. (2006). TLR2 Transmodulates Monocyte Adhesion and Transmigration via Rac1- and PI3K-Mediated Inside-Out Signaling in Response to Porphyromonas gingivalis Fimbriae.. J. Immunol. 176: 7645-7656 [Abstract] [Full Text]  
  • Hajishengallis, G., Ratti, P., Harokopakis, E. (2005). Peptide Mapping of Bacterial Fimbrial Epitopes Interacting with Pattern Recognition Receptors. J. Biol. Chem. 280: 38902-38913 [Abstract] [Full Text]  
  • Piva, A., Casadei, G., Pagliuca, G., Cabassi, E., Galvano, F., Solfrizzo, M., Riley, R. T., Diaz, D. E. (2005). Activated carbon does not prevent the toxicity of culture material containing fumonisin B1 when fed to weanling piglets. J ANIM SCI 83: 1939-1947 [Abstract] [Full Text]  
  • Whitsett, J. A., Bachurski, C. J., Barnes, K. C., Bunn, P. A. Jr., Case, L. M., Cook, D. N., Crooks, D., Duncan, M. W., Dwyer-Nield, L., Elston, R. C., Fessler, M. B., Franklin, W. A., Friedman, N., Garcia, J. G. N., Geraci, M. W., Glasgow, C., Glasser, S. W., Hardie, W. D., Henning, L. M., Johnson, G. L., Kawkitinarong, K., Keith, R. L., Korfhagen, T. R., Leikauf, G. D., Liggett, S. B., Malcolm, K. C., Malkinson, A. M., Mariani, T. J., McDowell, S. A., McGraw, D. W., Medvedovic, M., Moss, J., Nogee, L. M., Nonas, S., Pacheco-Rodriguez, G., Palmer, L. J., Peters, D. G., Prows, D. R., Redline, S., Regev, A., Sartor, M. A., Schwartz, D. A., Silverman, E. K., Steagall, W. K., Stearman, R. S., Taveira-DaSilva, A., Tichelaar, J. W., Tomlinson, C. R., Tsukada, K., Weaver, T. E., Wert, S. E., Wesselkamper, S. C., Worthen, G. S., Xu, Y., Zerbe, L., Zhang, Y., Zhang, Y., Choi, A. M. K., Kaminski, N. (2004). Functional Genomics of Lung Disease. Am. J. Respir. Cell Mol. Bio. 31: S1-S81 [Full Text]  
  • Sau, K., Mambula, S. S., Latz, E., Henneke, P., Golenbock, D. T., Levitz, S. M. (2003). The Antifungal Drug Amphotericin B Promotes Inflammatory Cytokine Release by a Toll-like Receptor- and CD14-dependent Mechanism. J. Biol. Chem. 278: 37561-37568 [Abstract] [Full Text]  
  • Mambula, S. S., Sau, K., Henneke, P., Golenbock, D. T., Levitz, S. M. (2002). Toll-like Receptor (TLR) Signaling in Response to Aspergillus fumigatus. J. Biol. Chem. 277: 39320-39326 [Abstract] [Full Text]  
  • Yu, H., Maurer, F., Medcalf, R. L. (2002). Plasminogen activator inhibitor type 2: a regulator of monocyte proliferation and differentiation. Blood 99: 2810-2818 [Abstract] [Full Text]  
  • Song, P. I., Abraham, T. A., Park, Y., Zivony, A. S., Harten, B., Edelhauser, H. F., Ward, S. L., Armstrong, C. A., Ansel, J. C. (2001). The Expression of Functional LPS Receptor Proteins CD14 And Toll-Like Receptor 4 in Human Corneal Cells. IOVS 42: 2867-2877 [Abstract] [Full Text]  
  • Funda, D. P., Tuckova, L., Farre, M. A., Iwase, T., Moro, I., Tlaskalova-Hogenova, H. (2001). CD14 Is Expressed and Released as Soluble CD14 by Human Intestinal Epithelial Cells In Vitro: Lipopolysaccharide Activation of Epithelial Cells Revisited. Infect. Immun. 69: 3772-3781 [Abstract] [Full Text]  
  • Tapping, R. I., Akashi, S., Miyake, K., Godowski, P. J., Tobias, P. S. (2000). Toll-Like Receptor 4, But Not Toll-Like Receptor 2, Is a Signaling Receptor for Escherichia and Salmonella Lipopolysaccharides. J. Immunol. 165: 5780-5787 [Abstract] [Full Text]  
  • Farmer, P., Pugin, J. (2000). beta -Adrenergic agonists exert their "anti-inflammatory" effects in monocytic cells through the Ikappa B/NF-kappa B pathway. Am. J. Physiol. Lung Cell. Mol. Physiol. 279: L675-L682 [Abstract] [Full Text]  
  • Cowan, D. B., Poutias, D. N., Del Nido, P. J., McGowan, F. X. Jr (2000). CD14-independent activation of cardiomyocyte signal transduction by bacterial endotoxin. Am. J. Physiol. Heart Circ. Physiol. 279: H619-H629 [Abstract] [Full Text]  
  • Sitrin, R. G., Pan, P. M., Harper, H. A., Blackwood, R. A., Todd, R. F. III (1999). Urokinase Receptor (CD87) Aggregation Triggers Phosphoinositide Hydrolysis and Intracellular Calcium Mobilization in Mononuclear Phagocytes. J. Immunol. 163: 6193-6200 [Abstract] [Full Text]  
  • Sellati, T. J., Bouis, D. A., Caimano, M. J., Feulner, J. A., Ayers, C., Lien, E., Radolf, J. D. (1999). Activation of Human Monocytic Cells by Borrelia burgdorferi and Treponema pallidum Is Facilitated by CD14 and Correlates with Surface Exposure of Spirochetal Lipoproteins. J. Immunol. 163: 2049-2056 [Abstract] [Full Text]  
  • Tapping, R. I., Orr, S. L., Lawson, E. M., Soldau, K., Tobias, P. S. (1999). Membrane-Anchored Forms of Lipopolysaccharide (LPS)-Binding Protein Do Not Mediate Cellular Responses to LPS Independently of CD14. J. Immunol. 162: 5483-5489 [Abstract] [Full Text]  
  • MacKichan, M. L., DeFranco, A. L. (1999). Role of Ceramide in Lipopolysaccharide (LPS)-induced Signaling. LPS INCREASES CERAMIDE RATHER THAN ACTING AS A STRUCTURAL HOMOLOG. J. Biol. Chem. 274: 1767-1775 [Abstract] [Full Text]  
  • Pugin, J., Dunn, I., Jolliet, P., Tassaux, D., Magnenat, J.-L., Nicod, L. P., Chevrolet, J.-C. (1998). Activation of human macrophages by mechanical ventilation in vitro. Am. J. Physiol. Lung Cell. Mol. Physiol. 275: L1040-L1050 [Abstract] [Full Text]  
  • Kitchens, R. L., Wang, P.-y., Munford, R. S. (1998). Bacterial Lipopolysaccharide Can Enter Monocytes Via Two CD14-Dependent Pathways. J. Immunol. 161: 5534-5545 [Abstract] [Full Text]  
  • Poussin, C., Foti, M., Carpentier, J.-L., Pugin, J. (1998). CD14-dependent Endotoxin Internalization via a Macropinocytic Pathway. J. Biol. Chem. 273: 20285-20291 [Abstract] [Full Text]  
  • Becker, M. N., Diamond, G., Verghese, M. W., Randell, S. H. (2000). CD14-dependent Lipopolysaccharide-induced beta -Defensin-2 Expression in Human Tracheobronchial Epithelium. J. Biol. Chem. 275: 29731-29736 [Abstract] [Full Text]  
  • Wang, Z.-M., Liu, C., Dziarski, R. (2000). Chemokines Are the Main Proinflammatory Mediators in Human Monocytes Activated by Staphylococcus aureus, Peptidoglycan, and Endotoxin. J. Biol. Chem. 275: 20260-20267 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»