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Abstract
SRPK1 (serine-arginine protein kinase 1) is a protein kinase that specifically phosphorylates proteins containing serine-arginine-rich domains. Its substrates include a family of SR proteins that are key regulators of mRNA AS (alternative splicing). VEGF (vascular endothelial growth factor), a principal angiogenesis factor contains an alternative 3′ splice site in the terminal exon that defines a family of isoforms with a different amino acid sequence at the C-terminal end, resulting in anti-angiogenic activity in the context of VEGF165-driven neovascularization. It has been shown recently in our laboratories that SRPK1 regulates the choice of this splice site through phosphorylation of the splicing factor SRSF1 (serine/arginine-rich splicing factor 1). The present review summarizes progress that has been made to understand how SRPK1 inhibition may be used to manipulate the balance of pro- and anti-angiogenic VEGF isoforms in animal models in vivo and therefore control abnormal angiogenesis and other pathophysiological processes in multiple disease states. ©The Authors Journal compilation ©2012 Biochemical Society.
Original language | English |
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Pages (from-to) | 831-835 |
Number of pages | 5 |
Journal | Biochemical Society Transactions |
Volume | 40 |
Issue number | 4 |
DOIs | |
Publication status | Published - 1 Aug 2012 |
Keywords
- Age-related macular degeneration
- Diabetic nephropathy
- Hepatitis C virus
- Serine-arginine protein kinase 1 (SRPK1)
- Serine/arginine-rich splicing factor 1 (SRSF1)
- Vascular endothelial growth factor (VEGF)
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Projects
- 1 Finished
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The endothelial surface layer in diabetic microangiopathy
Salmon, A. H. J.
31/12/09 → 31/12/14
Project: Research