4.4 Article

Mechanism of Dimerization of a Recombinant Mature Vascular Endothelial Growth Factor C

Journal

BIOCHEMISTRY
Volume 53, Issue 1, Pages 7-9

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/bi401518b

Keywords

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Funding

  1. National Health and Medical Research Council
  2. Cancer Council New South Wales

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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.

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