Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1995-9-7
pubmed:abstractText
The ligand binding activity of the platelet integrin alpha IIb beta 3 is initiated by agonist-generated intraplatelet signals. We studied this process in vitro by expressing recombinant alpha IIb beta 3 in Epstein-Barr virus-immortalized B lymphocytes. We found that phorbol ester stimulation induced the adhesion of lymphocytes expressing alpha IIb beta 3 to immobilized fibrinogen. Moreover, replacement of the transmembrane and cytoplasmic domains of the alpha and beta subunits of alpha IIb beta 3 with those of alpha L beta 2 significantly increased adherence, whereas replacement of only the cytoplasmic domains significantly decreased adherence. This suggests that transmembrane segments are involved in the agonist-induced modulation of alpha IIb beta 3 activity. Similar results were seen when the alpha IIb beta 3 activation-dependent monoclonal antibody PAC-1 was substituted for immobilized fibrinogen. We also found that the adherence of lymphocytes expressing beta 3 with either of the two alpha IIb/alpha L chimeras was similar to that of cells expressing alpha IIb beta 3, whereas the adherence of cells expressing alpha IIb with either of the two beta 3/beta 2 chimeras was substantially decreased, suggesting that the identity of the cytoplasmic domain of beta 3, but not of alpha IIb, is critical for alpha IIb beta 3 function. This report indicates that B lymphocytes contain signal transduction pathways involving protein kinase C that can increase the ligand binding activity of alpha IIb beta 3 and demonstrates the utility of these cells as an expression system for the study of agonist-stimulated alpha IIb beta 3 function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18631-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7543107-Amino Acid Sequence, pubmed-meshheading:7543107-B-Lymphocytes, pubmed-meshheading:7543107-Base Sequence, pubmed-meshheading:7543107-Blood Platelets, pubmed-meshheading:7543107-Cell Adhesion, pubmed-meshheading:7543107-Dose-Response Relationship, Drug, pubmed-meshheading:7543107-Fibrinogen, pubmed-meshheading:7543107-Humans, pubmed-meshheading:7543107-Integrins, pubmed-meshheading:7543107-Lymphocyte Function-Associated Antigen-1, pubmed-meshheading:7543107-Molecular Sequence Data, pubmed-meshheading:7543107-Oligopeptides, pubmed-meshheading:7543107-Platelet Glycoprotein GPIIb-IIIa Complex, pubmed-meshheading:7543107-Protein Binding, pubmed-meshheading:7543107-Protein Conformation, pubmed-meshheading:7543107-Recombinant Fusion Proteins, pubmed-meshheading:7543107-Sequence Alignment, pubmed-meshheading:7543107-Signal Transduction, pubmed-meshheading:7543107-Structure-Activity Relationship, pubmed-meshheading:7543107-Tetradecanoylphorbol Acetate
pubmed:year
1995
pubmed:articleTitle
Agonist-stimulated ligand binding by the platelet integrin alpha IIb beta 3 in a lymphocyte expression system.
pubmed:affiliation
Hematology-Oncology Division, Hospital of the University of Pennsylvania, Philadelphia, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't