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Related Experiment Videos

Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding.

A S Asch1, S Silbiger, E Heimer

  • 1Specialized Center for Research in Thrombosis, Cornell University Medical College, New York, NY 10021.

Biochemical and Biophysical Research Communications
|February 14, 1992
PubMed
Summary

The CSVTCG sequence in thrombospondin (TSP) is key for binding to CD36. This interaction influences platelet aggregation and tumor cell adhesion, highlighting CD36

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Area of Science:

  • Molecular biology
  • Cell biology
  • Biochemistry

Background:

  • CD36 is a receptor involved in various cellular processes.
  • Thrombospondin (TSP) is a matricellular protein with diverse biological functions.
  • The precise interaction mechanism between TSP and CD36 remains to be fully elucidated.

Purpose of the Study:

  • To define the role of CD36 as a thrombospondin (TSP) receptor.
  • To investigate the molecular mechanisms underlying the TSP-CD36 interaction.

Main Methods:

  • Transfection studies using CD36 cDNA in Jurkat cells.
  • Binding assays with radiolabeled peptides and TSP.
  • Analysis of platelet aggregation and tumor cell adhesion.

Main Results:

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  • CD36-transfected cells expressed an 88kD surface protein and bound TSP.
  • The TSP amino acid sequence CSVTCG mediated TSP-CD36 binding.
  • The hexapeptide YCSVTCG inhibited TSP expression on platelets and reduced platelet aggregation.
  • CSVTCG-albumin conjugates promoted CD36-dependent tumor cell adhesion.

Conclusions:

  • The CSVTCG repeat sequence is a critical determinant for thrombospondin (TSP) binding to CD36.
  • This interaction has functional implications for platelet function and tumor cell behavior.