Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding

Biochem Biophys Res Commun. 1992 Feb 14;182(3):1208-17. doi: 10.1016/0006-291x(92)91860-s.


To clarify the role of CD36 as a TSP receptor and to investigate the mechanisms of the TSP-CD36 interaction, transfection studies were performed using CD36-cDNA in a CDM8 plasmid. Jurkat cells transfected with CD36 cDNA express an 88kD membrane surface protein and acquire the ability to bind thrombospondin. The TSP amino acid sequence, CSVTCG, mediates the interaction of thrombospondin with CD36. CD36 transfectants but not control transfectants bind radiolabeled tyrosinated peptide (YCSVTCG). The hexapeptide inhibits thrombospondin expression on activated human platelets and results in diminished platelet aggregation. CSVTCG-albumin conjugates support CD36-dependent adhesion of tumor cells. We conclude that the CSVTCG repeat sequence is a crucial determinant of CD36 thrombospondin binding.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antigens, CD / genetics
  • Antigens, CD / metabolism*
  • Binding Sites
  • Blood Platelets / metabolism*
  • Blotting, Western
  • CD36 Antigens
  • Cell Adhesion
  • Cell Line
  • Cell Membrane / metabolism
  • Humans
  • Kinetics
  • Melanoma
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Platelet Membrane Glycoproteins / genetics
  • Platelet Membrane Glycoproteins / metabolism*
  • Receptors, Cell Surface / metabolism
  • Thrombospondins
  • Transfection


  • Antigens, CD
  • CD36 Antigens
  • Oligopeptides
  • Platelet Membrane Glycoproteins
  • Receptors, Cell Surface
  • Thrombospondins