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Related Concept Videos

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.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily  involved in a...

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Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

Complement component C5a activates ICAM-1 expression on human choroidal endothelial cells.

Jessica M Skeie1, John H Fingert, Stephen R Russell

  • 1Department of Biomedical Engineering, University of Iowa College of Engineering, Iowa City, Iowa, USA.

Investigative Ophthalmology & Visual Science
|May 21, 2010
PubMed
Summary
This summary is machine-generated.

Complement component C5a activates choroidal endothelial cells in age-related macular degeneration (AMD), potentially driving disease progression. This study found C5a receptor presence and its effect on endothelial cells in human choroid.

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Last Updated: Jun 12, 2026

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
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Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry
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Published on: May 19, 2020

Area of Science:

  • Ophthalmology
  • Immunology
  • Cell Biology

Background:

  • The complement system is implicated in age-related macular degeneration (AMD) pathogenesis.
  • Understanding the roles of complement components C3a and C5a in the human choroid is crucial for AMD research.

Purpose of the Study:

  • To investigate the pathophysiologic roles of complement components C3a and C5a in the human choroid of patients with AMD.
  • To determine the presence of C3a and C5a receptors in the human choroid and their functional effects.

Main Methods:

  • Assessed C3a and C5a receptors (C3aR, C5aR) in human RPE/choroid using RT-PCR and immunohistochemistry.
  • Evaluated choroidal endothelial cell migration and proliferation with C5a.
  • Analyzed ICAM-1 expression in human choroid organ cultures treated with C5a.
  • Genotyped AMD patients and controls for SNPs in C5R1 and C3AR1 genes.

Main Results:

  • C5a receptor (C5aR) was detected in human choroid, but C3a receptor (C3aR) was not.
  • C5a did not influence endothelial cell migration or proliferation.
  • Choriocapillaris endothelial cells in organ culture showed increased ICAM-1 mRNA and protein in response to C5a.
  • No significant association was found between AMD and SNP genotypes in C3AR1 and C5R1 genes.

Conclusions:

  • C5a peptides may activate choriocapillaris endothelial cells in AMD.
  • Activation of the choroidal endothelium by C5a could contribute to AMD progression through monocyte recruitment and subsequent pathogenesis.