A new class of membrane-bound chemokine with a CX3C motif (original) (raw)
- Letter
- Published: 13 February 1997
- Kevin B. Bacon2,
- Gary Hardiman1,
- Wei Wang2,
- Ken Soo2,
- Devora Rossi2,
- David R. Greaves na1,
- Albert Zlotnik2 &
- …
- Thomas J. Schall2
Nature volume 385, pages 640–644 (1997)Cite this article
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Abstract
Chemokines direct the trafficking of white blood cells in immune surveillance, playing a key role in inflammatory and infectious diseases such as AIDS1–5. All chemokines studied so far are secreted proteins of relative molecular mass ∼7K–15K and fall into three families that are defined by a cysteine signature motif: CXC, CC and C (refs 3, 6, 7), where C is a cysteine and X any amino-acid residue. We report here the identification and characterization of a fourth human chemokine type, derived from non-haemopoietic cells and bearing a new CX3C fingerprint. Unlike other chemokine types, the polypeptide chain of the human CX3C chemokine is predicted to be part of a 373-aminoacid protein that carries the chemokine domain on top of an extended mucin-like stalk. This molecule can exist in two forms: either membrane-anchored or as a shed 95K glycoprotein. The soluble CX3C chemokine has potent chemoattractant activity for T cells and monocytes, and the cell-surface-bound protein, which is induced on activated primary endothelial cells, promotes strong adhesion of those leukocytes. The structure, biochemical features, tissue distribution and chromosomal localization of CX3C chemokine all indicate that it represents a unique class of chemokine that may constitute part of the molecular control of leukocyte traffic at the endothelium.
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References
- Strieter, R. M. et al. J. Immunol. 156, 3583–3586 (1996).
CAS PubMed Google Scholar - Baggiolini, M. & Dahinden, C. A. Immunol. Today 104, 27–29 (1994).
Google Scholar - Schall, T. J. & Bacon, K. B. Curr. Opin. Immunol. 6, 865–873 (1994).
Article CAS Google Scholar - Weiss, R. A. & Clapham, P. R. Nature 381, 647–648 (1996).
Article ADS CAS Google Scholar - Pemack, B. P. & Schall, T. J. Nature Med. 2, 1174–1178 (1996).
Article Google Scholar - Clore, G. M. & Gronenborn, A. M. FASEB J. 9, 57–62 (1995).
Article CAS Google Scholar - Wells, T. N. et al. J. Leuk. Biol. 59, 53–60 (1996).
Article CAS Google Scholar - Altschul, S. F., Boguski, M. S., Gish, W. & Wootton, J. C. Nature Genet. 6, 119–129 (1994).
Article CAS Google Scholar - Kelner, G. S. et al. Science 266, 1395–1399 (1994).
Article ADS CAS Google Scholar - Lennon, G., Auffray, C., Polymeropoulos, M. & Soares, M. B. Genomics 33, 151–152 (1996).
Article CAS Google Scholar - Gendler, S. J. & Spicer, A. P. Annu. Rev. Physiol. 57, 607–634 (1995).
Article CAS Google Scholar - Hansen, J. E. et al. Biochem. J. 308, 601–813 (1995).
Article Google Scholar - Shimizu, Y. & Shaw, S. Nature 366, 630–631 (1993).
Article ADS CAS Google Scholar - Bernfield, M. et al. Annu. Rev. Cell. Biol. 8, 365–393 (1992).
Article CAS Google Scholar - Vyas, P., Vickers, M. A., Picketts, D. J. & Higgs, D. R. Genomics 29, 679–689 (1995).
Article CAS Google Scholar - Springer, T. A. Cell 76, 301–314 (1994).
Article CAS Google Scholar - Lasky, L. A. Science 258, 964–969 (1992).
Article ADS CAS Google Scholar - Butcher, E. C. & Picker, L. J. Science 272, 60–66 (1996).
Article ADS CAS Google Scholar - Webb, L. M. C., Ehrengruber, M. U., Clark-Lewis, I., Baggiolini, M. & Rot, A. Proc. Natl Acad. Sci. USA 90, 7158–7162 (1993).
Article ADS CAS Google Scholar - Tanaka, Y., Adams, D. H. & Shaw, S. Immunol. Today 361, 79–82 (1993).
CAS Google Scholar - Witt, D. P. & Lander, A. D. Curr. Biol. 4, 394–400 (1994).
Article CAS Google Scholar - Schall, T. J., Bacon, K., Toy, K. J. & Goeddel, D. V. Nature 347, 669–671 (1990).
Article ADS CAS Google Scholar - Dawson, P. E., Muir, T. W., Clark-Lewis, I. & Kent, S. B. Science 266, 776–779 (1994).
Article ADS CAS Google Scholar
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Author notes
- David R. Greaves: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
Authors and Affiliations
- Departments of Molecular Biology, DNAX Research Institute, 901 California Avenue, Palo Alto, California, 94304, USA
J. Fernando Bazan & Gary Hardiman - Departments of Immunology, DNAX Research Institute, 901 California Avenue, Palo Alto, California, 94304, USA
Kevin B. Bacon, Wei Wang, Ken Soo, Devora Rossi, Albert Zlotnik & Thomas J. Schall
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- J. Fernando Bazan
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Bazan, J., Bacon, K., Hardiman, G. et al. A new class of membrane-bound chemokine with a CX3C motif.Nature 385, 640–644 (1997). https://doi.org/10.1038/385640a0
- Received: 27 August 1996
- Accepted: 17 January 1997
- Issue Date: 13 February 1997
- DOI: https://doi.org/10.1038/385640a0