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- Publisher Website: 10.1021/bi401518b
- Scopus: eid_2-s2.0-84892562573
- PMID: 24354278
- WOS: WOS:000330001400003
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Article: Mechanism of dimerization of a recombinant mature vascular endothelial growth factor C
Title | Mechanism of dimerization of a recombinant mature vascular endothelial growth factor C |
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Authors | |
Issue Date | 2014 |
Citation | Biochemistry, 2014, v. 53, n. 1, p. 7-9 How to Cite? |
Abstract | 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. © 2013 American Chemical Society. |
Persistent Identifier | http://hdl.handle.net/10722/251057 |
ISSN | 2023 Impact Factor: 2.9 2023 SCImago Journal Rankings: 1.042 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Chiu, Joyce | - |
dc.contributor.author | Wong, Jason W H | - |
dc.contributor.author | Gerometta, Michael | - |
dc.contributor.author | Hogg, Philip J. | - |
dc.date.accessioned | 2018-02-01T01:54:27Z | - |
dc.date.available | 2018-02-01T01:54:27Z | - |
dc.date.issued | 2014 | - |
dc.identifier.citation | Biochemistry, 2014, v. 53, n. 1, p. 7-9 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | http://hdl.handle.net/10722/251057 | - |
dc.description.abstract | 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. © 2013 American Chemical Society. | - |
dc.language | eng | - |
dc.relation.ispartof | Biochemistry | - |
dc.title | Mechanism of dimerization of a recombinant mature vascular endothelial growth factor C | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1021/bi401518b | - |
dc.identifier.pmid | 24354278 | - |
dc.identifier.scopus | eid_2-s2.0-84892562573 | - |
dc.identifier.volume | 53 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | 7 | - |
dc.identifier.epage | 9 | - |
dc.identifier.eissn | 1520-4995 | - |
dc.identifier.isi | WOS:000330001400003 | - |
dc.identifier.issnl | 0006-2960 | - |