Complement factor H in its alternative identity as adrenomedullin-binding protein 1
Robert B Sim1, Janez Ferluga2, Hanan Al-Rashidi3
1Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, UK; Department of Infection, Immunity and Inflammation, University of Leicester, University Rd, Leicester, LE1 9HN, UK.
Molecular Immunology
|November 25, 2015
Summary
Complement factor H binds the peptide adrenomedullin, potentially protecting it from breakdown. This interaction is novel and may have therapeutic implications for vascular diseases.
Area of Science:
- Biochemistry
- Immunology
- Vascular Biology
Background:
- Complement factor H is a well-studied regulator of the complement system.
- Adrenomedullin is a peptide with potential therapeutic applications in vascular diseases.
- The interaction between complement factor H and adrenomedullin is not well understood.
Purpose of the Study:
- To investigate the binding interaction between complement factor H and adrenomedullin.
- To explore the role of complement factor H in protecting adrenomedullin from proteolytic degradation.
- To assess the potential therapeutic relevance of this interaction.
Main Methods:
- Biochemical assays to study protein binding.
- Proteolytic degradation assays.
- In vivo studies using animal models (implied).
Main Results:
- Complement factor H binds to adrenomedullin.
- This binding appears to protect adrenomedullin from proteolytic degradation.
- The binding interaction is described as unusual.
Conclusions:
- Complement factor H has a previously unrecognized role as a binding protein for adrenomedullin.
- The interaction warrants further investigation due to its unusual nature and potential therapeutic implications.
- Factor H may enhance the stability and efficacy of adrenomedullin as a therapeutic agent for vascular conditions.
Related Concept Videos
01:31Immunoglobulin-like Cell Adhesion Molecules
4.6K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
4.6K
01:27Complement System
12.6K
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...
12.6K
01:57Protein Complexes with Interchangeable Parts
3.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.1K