Linked Life Data

11958132

Source:http://linkedlifedata.com/resource/pubmed/id/11958132

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-4-17
pubmed:abstractText
Vascular endothelial growth factor receptor 1 (Flt1) plays an important role in angiogenesis. It was hypothesized that, upon binding to VEGF, Flt1 tyrosine kinase underwent dimerization and initiated the signal transduction in VEGF/VEGF receptor system. In this report, a soluble active Flt1 tyrosine kinase domain expressed in E. coli was obtained, and its properties were partly characterized. The cDNA of Flt1 tyrosine kinase domain was obtained from the total RNA extracted from human liver cancer tissues by using RT-PCR, and was cloned to vector pGEX-KG. A soluble active GST-fusion protein of Flt1 tyrosine kinase domain (GST-F) was obtained from E. coli BL21 (DE3) pLysS. Although it was reported that GST-F contains no phosphorylation site, it did autophosphorylate in vitro. Mg2+ and Mn2+ were essential for the activity. It was also found that GST-F phosphorylated a synthesized substrate PolyE4Y, but not MBP and Src-related-peptide. The optimal Mg2+ and Mn2+ concentration for polyE4Y phosphorylation was 15 mmol/L and 0.5 mmol/L, respectively. This work is helpful for developing the new anti-cancer drugs.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0582-9879
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-44
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
[Cloning, expression and characterization of human vascular endothelial growth factor receptor 1 tyrosine kinase].
pubmed:affiliation
National Center for Drug Screening, Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031.
pubmed:publicationType
Journal Article, English Abstract