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CD36 forms covalently associated dimers and multimers in platelets and transfected COS-7 cells
R F Thorne1, C J Meldrum, S J Harris
1Cancer Research Unit, Faculty of Medicine and Health Sciences, University of Newcastle, NSW, Australia. rthorne@mail.newcastle.edu.au
Biochemical and Biophysical Research Communications
|December 17, 1997
Summary
Platelet CD36 forms homodimers and multimers via cysteine bonds in its extracellular domain. This CD36 multimerization may play a role in cell function.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- CD36 is a transmembrane glycoprotein found on various cell surfaces.
- Understanding CD36 structure and interactions is crucial for cell signaling research.
Purpose of the Study:
- To investigate the molecular complexes of CD36 on platelets.
- To determine the nature and formation mechanism of CD36 multimers.
Main Methods:
- Immunoblotting
- Gel filtration
- Native PAGE
- Transfected COS-7 cell experiments
- Site-directed mutagenesis
Main Results:
- Platelet CD36 exists in high molecular weight complexes beyond its monomeric form.
- These complexes are CD36 homodimers and -multimers.
- Multimer formation is mediated by intermolecular cysteine bridges, primarily involving extracellular cysteines.
Conclusions:
- CD36 undergoes multimerization through disulfide bonds.
- The extracellular domain cysteines are critical for CD36 multimer formation.
- Further research is needed to elucidate the physiological significance of CD36 multimerization.