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Corticotropin-releasing factor binding protein dimerizes after association with ligand
R J Woods1, K M Kennedy, J M Gibbins
1Department of Biochemistry and Physiology, University of Reading, Whiteknights, Berks, United Kingdom.
Endocrinology
|August 1, 1994
Summary
Plasma CRF-binding protein (BP) forms a dimer when binding to CRF, increasing its affinity. This dimerization is suggested to be the in vivo mechanism for CRF uptake at receptor sites.
Area of Science:
- Endocrinology
- Biochemistry
Background:
- Plasma CRF-binding protein (BP) levels decrease in late pregnancy.
- This decrease may be due to ligand association, as seen after synthetic CRF injection in males.
Purpose of the Study:
- To investigate the physicochemical properties of CRF-binding protein (BP).
- To understand the interaction between CRF and BP.
Main Methods:
- Gel filtration under physiological conditions.
- Used natural and recombinant BP.
- Studied interaction with CRF and other ligands.
Main Results:
- CRF binding to BP causes an increase in molecular weight, indicating dimer formation.
- The BP-CRF dimer is more stable with serum or higher-affinity ligands.
- Dimeric BP exhibits higher ligand affinity than monomeric BP.
Conclusions:
- CRF-binding protein (BP) dimerization is a key event upon CRF binding.
- This dimerization likely facilitates in vivo clearance of CRF via specific receptor uptake.