Document Detail


Ultrastructure and function of the fractalkine mucin domain in CX(3)C chemokine domain presentation.
MedLine Citation:
PMID:  10660527     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
A M Fong; H P Erickson; J P Zachariah; S Poon; N J Schamberg; T Imai; D D Patel
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  275     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2000 Feb 
Date Detail:
Created Date:  2000-03-16     Completed Date:  2000-03-16     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3781-6     Citation Subset:  IM    
Affiliation:
Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA.
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MeSH Terms
Descriptor/Qualifier:
Alkaline Phosphatase / genetics,  ultrastructure
Cell Adhesion
Cell Adhesion Molecules / metabolism,  ultrastructure
Centrifugation, Density Gradient
Chemokine CX3CL1
Chemokines, CX3C*
Chemokines, CXC / analysis,  metabolism*
E-Selectin / genetics,  ultrastructure
Flow Cytometry
Humans
Kinetics
Leukocytes / metabolism
Membrane Proteins / analysis,  metabolism*
Microscopy, Electron
Mucins / metabolism*,  ultrastructure
Recombinant Fusion Proteins / ultrastructure
Tumor Cells, Cultured
Grant Support
ID/Acronym/Agency:
AR39162/AR/NIAMS NIH HHS; CA47056/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/CX3CL1 protein, human; 0/Cell Adhesion Molecules; 0/Chemokine CX3CL1; 0/Chemokines, CX3C; 0/Chemokines, CXC; 0/E-Selectin; 0/Membrane Proteins; 0/Mucins; 0/Recombinant Fusion Proteins; EC 3.1.3.1/Alkaline Phosphatase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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