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Cutting Edge: Localization of the Host Recognition Functions of Complement Factor H at the Carboxyl-Terminal: Implications for Hemolytic Uremic Syndrome

Michael K. Pangburn
J Immunol November 1, 2002, 169 (9) 4702-4706; DOI: https://doi.org/10.4049/jimmunol.169.9.4702
Michael K. Pangburn
Department of Biochemistry, University of Texas Health Science Center, Tyler, TX, 75708
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  • FIGURE 1.
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    FIGURE 1.

    Schematic representation of factor H indicating the locations of the polyanion and C3b-binding sites. Factor H is composed of 20 homologous domains each possessing a similar core structure (45 ). Approximate locations of polyanion binding sites 1, 2, and 3 (24 25 26 27 28 29 ) are indicated at the top, and of the three C3b-binding sites are indicated at the bottom (21 22 23 24 ).

  • FIGURE 2.
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    FIGURE 2.

    Lysis of C-activating cells (Er) and host-like polyanion-bearing cells (Es) in factor H-depleted human serum replenished with normal human factor H, with recombinant factor H, or with a deletion mutant of recombinant factor H lacking the C-terminal 10 domains. Human serum depleted of factor H was reconstituted with normal molar concentrations of human factor H (top panel), full-length recombinant factor H made in insect cells (middle panel), or a deletion mutant factor H lacking the C-terminal 10 domains, rHΔ11–20 (bottom panel). Various concentrations of the reconstituted sera were incubated with Er or Es cells for 20 min at 37°C. The assays contained 2.5 mM MgEGTA to inhibit classical and lectin pathway activation and restrict activation to the calcium-independent alternative pathway of C. Lysis was subsequently measured by hemoglobin release after centrifugation to remove unlysed cells.

  • FIGURE 3.
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    FIGURE 3.

    Lysis of C-activating cells (Er) and host-like polyanion-bearing cells (Es) in factor H-depleted human serum replenished with one of three recombinant mutants of factor H each lacking a 5-domain region of the 20-domain protein. The assays were performed as described in Fig. 2.

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The Journal of Immunology: 169 (9)
The Journal of Immunology
Vol. 169, Issue 9
1 Nov 2002
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Cutting Edge: Localization of the Host Recognition Functions of Complement Factor H at the Carboxyl-Terminal: Implications for Hemolytic Uremic Syndrome
Michael K. Pangburn
The Journal of Immunology November 1, 2002, 169 (9) 4702-4706; DOI: 10.4049/jimmunol.169.9.4702

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Cutting Edge: Localization of the Host Recognition Functions of Complement Factor H at the Carboxyl-Terminal: Implications for Hemolytic Uremic Syndrome
Michael K. Pangburn
The Journal of Immunology November 1, 2002, 169 (9) 4702-4706; DOI: 10.4049/jimmunol.169.9.4702
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