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At least 1,171 records · Page 65Linked to original sources
PubMed1999

Serum levels of soluble intercellular adhesion molecule-1, vascular cell adhesion molecule-1, and interleukin-2 receptor in patients with vernal keratoconjunctivitis and allergic conjunctivitis.

BACKGROUND: Vernal keratoconjunctivitis (VKC) is characterized by severe ocular allergic inflammation that may have a poor visual prognosis. Due to the high frequency of the presence of atopic dermatitis (AD) in VKC, most systemic parameters are dependent on the clinical severity of AD. METHODS: Serum levels of sICAM-1, sVCAM-1, and sIL-2R were measured by enzyme-linked immunoassay using samples from 30 VKC patients, 30 allergic conjunctivitis (AC) patients, and 20 normal subjects, to determine whether the concentrations of these molecules are elevated. RESULTS: Circulating sICAM-1 and sIL-2R levels were increased in patients with VKC with AD compared with those in VKC without AD, AC, and normal controls. Serum levels of sVCAM-1 in VKC patients with and without AD were significantly higher than those in controls. No significant difference was found in the levels of sVCAM-1 between patients with VKC with and without AD. In VKC patients with AD, the sIL-2R level correlated significantly with severity of AD, whereas no such correlation was found for sICAM-1 and sVCAM-1. CONCLUSIONS: These results suggest that serum sVCAM-1 can be used as a marker to differentiate VKC from nonproliferative ocular allergic diseases, and specific immunologic features of VKC may underlie the upregulation of serum sVCAM-1.

Adolescent↗
PubMed2001

CD84 functions as a homophilic adhesion molecule and enhances IFN-gamma secretion: adhesion is mediated by Ig-like domain 1.

CD84 is a member of the CD2 subset of the Ig superfamily of cell surface molecules. Its cytoplasmic tail binds to Src homology 2 domain-containing protein 1A (signaling lymphocytic activation molecule-associated protein), a protein encoded by the X-linked lymphoproliferative disease gene. It is preferentially expressed on B lymphocytes, monocytes, and platelets. We show that it is also expressed on thymocytes and T cells. CD84 was positive on CD4-CD8- thymocytes, and its expression decreased with cell maturation. It is expressed on mature T cells preferentially on CD45RO+. To identify the CD84 ligand, we generated a soluble Ig fusion protein containing the human CD84 extracellular domains (CD84-Ig). Because receptor-ligand interactions occur between several members of this subfamily, we assayed CD84-Ig binding with all members of the CD2 family. CD84-Ig bound to CD84-transfected cells, whereas no binding was detected with cells expressing other CD2 subfamily receptors, showing that CD84 binds to itself. Anti-CD84 mAbs recognizing epitopes wholly within domain 1 of CD84 blocked the binding of the CD84-Ig fusion protein to CD84-transfected cells and platelets. Data from CD84 domain human/mouse chimeras further revealed that only the first extracellular domain of the molecule is involved in the ligand receptor recognition. The CD84-CD84 interaction was independent of its cytoplasmic tail. Finally, concurrent ligation of human CD84 with mAbs or CD84-Ig and CD3 enhanced IFN-gamma secretion in human lymphocytes. Thus, CD84 is its own ligand and acts as a costimulatory molecule.

Animals↗