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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...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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.
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Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

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Related Experiment Video

Updated: Jul 14, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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Function, structure and therapeutic potential of complement C5a receptors.

P N Monk1, A-M Scola, P Madala

  • 1Academic Neurology Unit, School of Medicine and Biomedical Science, University of Sheffield, Sheffield, UK. p.monk@shef.ac.uk

British Journal of Pharmacology
|July 3, 2007
PubMed
Summary

Complement fragment C5a, a pro-inflammatory molecule, interacts with receptors C5aR and C5L2. Research highlights C5aR as a therapeutic target for various conditions beyond immunity.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Pharmacology

Background:

  • Complement fragment C5a is a pro-inflammatory mediator generated during complement cascade activation.
  • It binds to C5a receptors (C5aR and C5L2) found on immune and other cell types.
  • While known for inflammatory roles, C5a's broader physiological functions are increasingly recognized.

Purpose of the Study:

  • To review recent advancements in C5a receptor research.
  • To evaluate C5aR as a potential therapeutic target.
  • To discuss the implications of a non-signaling C5a receptor.

Main Methods:

  • Utilized receptor knockout mice, antibodies, and receptor antagonists.
  • Employed molecular modeling and structure-activity relationship studies.
  • Analyzed species-dependent ligand potency on C5aR.

Main Results:

  • Significant progress in understanding C5a physiology through various research tools.
  • Identified ligand binding sites and activation mechanisms for C5aR.
  • C5a implicated in developmental biology, neurodegeneration, tissue regeneration, and hematopoiesis.

Conclusions:

  • C5aR represents a promising therapeutic target.
  • Further research into C5a and its receptors can yield novel treatments.
  • The role of the non-signaling C5L2 receptor warrants further investigation.