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

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-...

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Bibliographic Details
Published in:Biochemistry (Easton) 2014-01, Vol.53 (1), p.7-9
Main Authors: Chiu, Joyce, Wong, Jason W. H, Gerometta, Michael, Hogg, Philip J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Cysteine - chemistry
Disulfides - chemistry
Humans
Oxidation-Reduction
Protein Multimerization
Recombinant Proteins - metabolism
Vascular Endothelial Growth Factor C - metabolism
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi401518b