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Related Concept Videos

Complement System01:27

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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Actin Filament Depolymerization

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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
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Functional analysis of Ficolin-3 mediated complement activation.

Estrid Hein1, Christian Honoré, Mikkel-Ole Skjoedt

  • 1Laboratory of Molecular Medicine, Department of Clinical Immunology, Rigshospitalet, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.

Plos One
|November 19, 2010
PubMed
Summary
This summary is machine-generated.

A new functional assay measures Ficolin-3’s role in complement activation, crucial for understanding infections. This method aids in diagnosing Ficolin-3 deficiencies and related lectin pathway defects.

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Area of Science:

  • Immunology
  • Complement system biology

Background:

  • The lectin complement pathway uses mannose-binding lectin and Ficolins (-1, -2, -3) for recognition.
  • Ficolin-3 deficiency is linked to severe infections, highlighting the need for functional assessment.

Purpose of the Study:

  • Develop a functional ELISA-based assay to evaluate Ficolin-3 mediated complement activation.
  • Create a method suitable for both research and clinical diagnostics.

Main Methods:

  • Utilized acetylated bovine serum albumin (acBSA) as a ligand for Ficolins in microtiter wells.
  • Assessed Ficolin binding and subsequent complement activation via C4, C3, and terminal complement complex (TCC) deposition.
  • Incorporated a classical pathway inhibitor to enhance assay robustness.

Main Results:

  • Serum Ficolin-3 demonstrated calcium-dependent binding to acBSA, unlike Ficolin-1 and Ficolin-2.
  • Complement component deposition (C4, C3, TCC) on acBSA was specifically dependent on Ficolin-3.
  • Functional complement activation correlated significantly with Ficolin-3 serum concentrations.

Conclusions:

  • A novel functional assay for Ficolin-3 mediated complement activation up to TCC formation has been developed.
  • This assay enables the diagnosis of functional and genetic defects in Ficolin-3 and downstream complement components.
  • The method supports research and clinical applications for assessing the lectin complement pathway.