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Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation.

Publication ,  Journal Article
Fong, AM; Erickson, HP; Zachariah, JP; Poon, S; Schamberg, NJ; Imai, T; Patel, DD
Published in: J Biol Chem
February 11, 2000

Fractalkine (FKN), a CX(3)C chemokine/mucin hybrid molecule on endothelium, functions as an adhesion molecule to capture and induce firm adhesion of a subset of leukocytes in a selectin- and integrin-independent manner. We hypothesized that the FKN mucin domain may be important for its function in adhesion, and tested the ability of secreted alkaline phosphatase (SEAP) fusion proteins containing the entire extracellular region (FKN-SEAP), the chemokine domain (CX3C-SEAP), or the mucin domain (mucin-SEAP) to support firm adhesion under flow. CX3C-SEAP induced suboptimal firm adhesion of resting peripheral blood mononuclear cells, compared with FKN-SEAP, and mucin-SEAP induced no firm adhesion. CX3C-SEAP and FKN-SEAP bound to CX(3)CR1 with similar affinities. By electron microscopy, fractalkine was 29 nm in length with a long stalk (mucin domain), and a globular head (CX(3)C). To test the function of the mucin domain, a chimeric protein replacing the mucin domain with a rod-like segment of E-selectin was constructed. This chimeric protein gave the same adhesion of peripheral blood mononuclear cells as intact FKN, both when immobilized on glass and when expressed on the cell surface. This implies that the function of the mucin domain is to provide a stalk, extending the chemokine domain away from the endothelial cell surface to present it to flowing leukocytes.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

February 11, 2000

Volume

275

Issue

6

Start / End Page

3781 / 3786

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Recombinant Fusion Proteins
  • Mucins
  • Microscopy, Electron
  • Membrane Proteins
  • Leukocytes
  • Kinetics
  • Humans
  • Flow Cytometry
  • E-Selectin
 

Citation

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Fong, A. M., Erickson, H. P., Zachariah, J. P., Poon, S., Schamberg, N. J., Imai, T., & Patel, D. D. (2000). Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation. J Biol Chem, 275(6), 3781–3786. https://doi.org/10.1074/jbc.275.6.3781
Fong, A. M., H. P. Erickson, J. P. Zachariah, S. Poon, N. J. Schamberg, T. Imai, and D. D. Patel. “Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation.J Biol Chem 275, no. 6 (February 11, 2000): 3781–86. https://doi.org/10.1074/jbc.275.6.3781.
Fong AM, Erickson HP, Zachariah JP, Poon S, Schamberg NJ, Imai T, et al. Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation. J Biol Chem. 2000 Feb 11;275(6):3781–6.
Fong, A. M., et al. “Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation.J Biol Chem, vol. 275, no. 6, Feb. 2000, pp. 3781–86. Pubmed, doi:10.1074/jbc.275.6.3781.
Fong AM, Erickson HP, Zachariah JP, Poon S, Schamberg NJ, Imai T, Patel DD. Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation. J Biol Chem. 2000 Feb 11;275(6):3781–3786.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

February 11, 2000

Volume

275

Issue

6

Start / End Page

3781 / 3786

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Recombinant Fusion Proteins
  • Mucins
  • Microscopy, Electron
  • Membrane Proteins
  • Leukocytes
  • Kinetics
  • Humans
  • Flow Cytometry
  • E-Selectin