posted on 2014-01-14, 00:00authored byJoyce Chiu, Jason
W. H. Wong, Michael Gerometta, Philip J. Hogg
The
vascular endothelial growth factors (VEGFs) and their tyrosine
kinase receptors play a pivotal role in angiogenesis and lymphangiogenesis
during development and in pathologies such as tumor growth. The VEGFs
function as disulfide-linked antiparallel homodimers. The lymphangiogenic
factors, VEGF-C and VEGF-D, exist as monomers and dimers, and dimerization
is regulated by a unique unpaired cysteine. In this study, we have
characterized the redox state of this unpaired cysteine in a recombinant
mature monomeric and dimeric VEGF-C by mass spectrometry. Our findings
indicate that the unpaired cysteine regulates dimerization via thiol–disulfide
exchange involving the interdimer disulfide bond.