Neutrophil influx into an inflammatory site inhibited by a soluble homing receptor-IgG chimaera
Article Abstract:
Inflammation caused by aggregation of neutrophils (a type of white blood cell) occurs in several clinical conditions, including adult respiratory distress (severe breathing difficulty) and the injury that can result when blood flow is restored to a damaged area (reperfusion injury). If neutrophils are prevented from attaching to certain cells, their ability to provoke an inflammatory response should in principle be reduced. A molecule constructed in such a way as to block adhesion between neutrophils and endothelial cells was evaluated in animals. Mice were given this chimera (made by combining an immunoglobulin with a homing receptor) by intravenous injection, and they subsequently showed a greatly reduced response to thioglycollate, a substance that induces neutrophil-mediated inflammation. This was probably the result of the chimera's ability to bind to cells' homing receptors, preventing white blood cells from binding. Additional experiments were performed to learn more about the chimera's appropriate dose levels and time course. A discussion is presented of the therapeutic possibilities of agents that block cell adhesion for treating inflammatory responses. (Consumer Summary produced by Reliance Medical Information, Inc.)
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1991
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How integrins are activated
Article Abstract:
Scientist Fenczik's research showing that the T-cell activation marker CD98 controls integrin-mediated cell adhesion might be useful in anti-viral compound studies. Evidence using biochemistry models suggests that cross-linking of CD98 causes integrins to come together in high-density complex formation. Further research may show that the inhibition of CD98 activity results in reduced inflammation at the site of infection.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin
Article Abstract:
The activity of the high endothelial venule-associated, mucin-like glycoprotein GlyCAM-1 as a ligand for L-selectin requires sulphation. This is shown in a study using chlorate to metabolically inhibit sulphation. Previous research has shown that sialylation is also required and fucosylation is suspected to play an important role.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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