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题目:: SRPK1 inhibition in vivo: modulation of VEGF splicing and potential treatment for multiple diseases.
作者:: Oltean(Sebastian),Gammons(Melissa),Hulse(Richard),Hamdollah-Zadeh(Maryam),Mavrou(Athina),Donaldson(Lucy),Salmon(Andrew H),Harper(Steve J),Ladomery(Michael R),Bates(David O)
状态:: 发布时间2012-07-23 , 更新时间 2012-07-23
期刊:: Biochem Soc Trans
摘要:: 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.
语言:: eng
DOI:: 10.1042/BST20120051

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