What question did this study set out to answer?

This research aims to understand how PDGF binding affects receptor subunit interactions and phosphorylation processes.

Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit dimerization and intersubunit trans-phosphorylation

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Randomized trial demonstrates PDGF stimulates receptor dimerization and trans-phosphorylation in cells, indicating new mechanisms of signaling.

This research aims to understand how PDGF binding affects receptor subunit interactions and phosphorylation processes.
Cloned and expressed PDGF receptor cDNA variants including alpha and beta subunits.
Performed Scatchard analysis to determine binding affinities of PDGF ligands to receptor subunits.
Between wild-type and kinase-inactive beta-subunits, examined PDGF-induced dimerization and phosphorylation in intact cells.
PDGF-AA and PDGF-AB showed high binding affinities of Kd = 0.06 nM and Kd = 0.05 nM, respectively.
PDGF-BB had a lower affinity of Kd = 0.4 nM but still facilitated substantial binding at physiological concentrations.
Binding of PDGF to receptors promoted receptor subunit dimerization and tyrosine phosphorylation at key sites.

Kelly et al. (1991) studied this question.

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Randomized trial demonstrates PDGF stimulates receptor dimerization and trans-phosphorylation in cells, indicating new mechanisms of signaling.