CD36-mediated signal transduction in human monocytes by anti-CD36 antibodies but not by anti-thrombospondin antibodies recognizing cell membrane-bound thrombospondin. Biochem Biophys Res Commun 1991 Feb 28;175(1):263-70
Date
02/28/1991Pubmed ID
1998511DOI
10.1016/s0006-291x(05)81229-xScopus ID
2-s2.0-0026029480 (requires institutional sign-in at Scopus site) 44 CitationsAbstract
Mononuclear cells (MNC) treated with anti-CD36 Fab or F(ab')2 fragments and then stimulated with anti-rabbit (F(ab')2 displayed an oxidative burst, suggesting that the crosslinking of CD36 promotes signal transduction in the absence of an Fc receptor involvement. Moreover, intact anti-TSP mediates a weak oxidative burst in MNC, which was strongly enhanced upon pretreatment of monocytes (but not lymphocytes) with TSP. This response, however, was mediated by Fc receptors, not by an involvement of CD36. Other means of crosslinking cell-bound TSP and exposure of MNC to surface-bound TSP failed to promote an oxidative burst. Crosscompetition tests confirmed that the interaction site(s) of TSP with monocytes are distinct from the signal-promoting sites recognized by polyclonal and 3 monoclonal anti-CD36 antibodies.
Author List
Schüepp BJ, Pfister H, Clemetson KJ, Silverstein RL, Jungi TWAuthor
Roy L. Silverstein MD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ADP-ribosyl CyclaseADP-ribosyl Cyclase 1
Antibodies, Monoclonal
Antigens, CD
Antigens, Differentiation
Cell Membrane
Humans
Immunoglobulin Fab Fragments
In Vitro Techniques
Kinetics
Luminescent Measurements
Membrane Glycoproteins
Monocytes
Platelet Membrane Glycoproteins
Signal Transduction
Thrombospondins
