Linked Life Data

11714819

Source:http://linkedlifedata.com/resource/pubmed/id/11714819

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2001-11-20
pubmed:abstractText
The adherence of Plasmodium falciparum-infected RBC (IRBC) to postcapillary venular endothelium is an important determinant of the pathogenesis of severe malaria complications. Cytoadherence of IRBC to endothelial cells involves specific receptor/ligand interactions. The glycoprotein CD36 expressed on endothelial cells is the major receptor involved in this interaction. Treatment of CD36-expressing cells with reducing agents, such as DTT and N-acetylcysteine, was followed by CD36 conformational change monitorable by the appearance of the Mo91 mAb epitope. Only a fraction of the surface expressed CD36 molecules became Mo91 positive, suggesting the presence of two subpopulations of molecules with different sensitivities to reduction. The Mo91 epitope has been localized on a peptide (residues 260-279) of the C-terminal, cysteine-rich region of CD36. Treatment with reducing agents inhibited the CD36-dependent cytoadherence of IRBC to CD36-expressing cells and dissolved pre-existent CD36-mediated IRBC/CD36-expressing cell aggregates. CD36 reduction did not impair the functionality of CD36, since the reactivity of other anti-CD36 mAbs as well as the binding of oxidized low density lipoprotein, a CD36 ligand, were maintained. The modifications induced by reduction were reversible. After 14 h CD36 was reoxidized, the cells did not express the Mo91 epitope, and cytoadherence to IRBC was restored. The results indicate that IRBCs bind only to a redox-modulated fraction of CD36 molecules expressed on the cell surface. The present data indicate the therapeutic potential of reducing agents, such as the nontoxic drug N-acetylcysteine, to prevent or treat malaria complications due to IRBC cytoadhesion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
167
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6510-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11714819-Acetylcysteine, pubmed-meshheading:11714819-Amino Acid Sequence, pubmed-meshheading:11714819-Animals, pubmed-meshheading:11714819-Antibodies, Monoclonal, pubmed-meshheading:11714819-Antigen-Antibody Reactions, pubmed-meshheading:11714819-Antigens, CD36, pubmed-meshheading:11714819-COS Cells, pubmed-meshheading:11714819-Cell Adhesion, pubmed-meshheading:11714819-Cell Line, pubmed-meshheading:11714819-Chemical Fractionation, pubmed-meshheading:11714819-Cysteine, pubmed-meshheading:11714819-Dithiothreitol, pubmed-meshheading:11714819-Endothelium, Vascular, pubmed-meshheading:11714819-Epitopes, pubmed-meshheading:11714819-Erythrocyte Aggregation, pubmed-meshheading:11714819-Erythrocytes, pubmed-meshheading:11714819-Humans, pubmed-meshheading:11714819-Molecular Sequence Data, pubmed-meshheading:11714819-Oxidation-Reduction, pubmed-meshheading:11714819-Plasmodium falciparum, pubmed-meshheading:11714819-Protein Conformation, pubmed-meshheading:11714819-Reducing Agents, pubmed-meshheading:11714819-U937 Cells
pubmed:year
2001
pubmed:articleTitle
Cytoadherence of Plasmodium falciparum-infected erythrocytes is mediated by a redox-dependent conformational fraction of CD36.
pubmed:affiliation
DIBIT, San Raffaele Scientific Institute, Milan, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't