Linked Life Data

8096436

Source:http://linkedlifedata.com/resource/pubmed/id/8096436

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-5-4
pubmed:abstractText
The effect of two mouse mAb (LB-2 and G1B2) against human CD54 (intercellular adhesion molecule-1, ICAM-1) in lymphocyte aggregation and proliferation systems was investigated. The LB-2 mAb, but not G1B2, inhibited phorbol ester-induced aggregation of B lymphoblastoid cells. In addition, LB-2, but not G1B2, induced aggregation and proliferation of peripheral blood mononuclear cells (PBMC) in cultures containing FCS. The Fab fragment of LB-2 always (10/10 donors) induced proliferation while the intact mAb was active in 3/11 donors. When cultures contained human serum (HS), LB-2 and its Fab fragment induced proliferation in 1/9 and 1/4 donors, respectively. Addition of HS to FCS cultures inhibited proliferation induced by LB-2 Fab, indicating the presence of an inhibitory factor in human serum. Addition of anti-CD18 mAb to cultures stimulated by LB-2 Fab caused partial inhibition of proliferation but did not prevent aggregate formation. A combination of anti-CD18 and anti-CD29 mAb resulted in a nearly complete inhibition of proliferation but did not inhibit aggregate formation. In these experiments it was found that the anti-CD29 mAb 4B4 in itself induced cell aggregation of PBMC and enhanced aggregation induced by the anti-CD3 mAb OKT3. Both LB-2 and G1B2 showed significant inhibition (> 60%) of proliferation when human PBMC were stimulated by the antigen PPD in the presence of HS, but not when stimulated by staphylococcal enterotoxin A (SEA) or IL-2. This study describes two mAb against separate epitopes on CD54 which are differentially involved in cell aggregation or induction of proliferation but are of similar importance in antigen-specific responses. Furthermore, the new finding that the LB-2 mAb or its Fab fragment can induce cell aggregation and proliferation defines a signaling function of CD54 which may work independent of crosslinking or costimulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0008-8749
pubmed:author
pubmed:issnType
Print
pubmed:volume
147
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12-24
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Regulation of lymphocyte aggregation and proliferation through adhesion molecule CD54 (ICAM-1).
pubmed:affiliation
Kabi Pharmacia AB, Uppsala, Sweden.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't