Linked Life Data

7898938

Source:http://linkedlifedata.com/resource/pubmed/id/7898938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-4-25
pubmed:abstractText
The FLT4 gene encodes a tyrosine kinase receptor related to the two identified receptors for vascular endothelial growth factor (VEGF), FLT1 and FLK1/KDR. Two isoforms of FLT4, differing by their C-terminal ends, have been identified. The long form has 65 additional amino acid residues. We have shown that FLT4 is a highly glycosylated, relatively stable, cell surface associated kinase of approximately 180 kDa. In order to study the signal transduction molecules associated with the FLT4 pathway, and in the absence of a known ligand, we constructed two chimeric molecules (FF4S and FF4L) made of the extracellular region of the CSF1 receptor (Fms gene product) and of the transmembrane and intracellular regions of either form of FLT4. These two chimeric forms were expressed in Rat 2 transfectants. We assayed the ligand-induced capacity of the FF4 short and long forms to sustain growth of Rat 2 cells in semisolid medium. In a soft agar assay, only the long form was able to induce the growth of Rat 2 cells upon ligand treatment. The two forms of FLT4 therefore have different functional capacities. We looked for association and/or phosphorylation of phospholipase C gamma (PLC gamma) and phosphatidylinositol-3'-phosphate (PI3K), after stimulation of the FF4 molecules by CSF1. Finally, we have studied the expression of the Flt4 gene in mouse embryos and in the adult by in situ hybridization. Flt4 transcripts were found at day 12.5 post-coïtum and thereafter, including the adult mouse, predominantly in the pericardium, pleural membranes and in the lung.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
973-84
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7898938-Amino Acid Sequence, pubmed-meshheading:7898938-Animals, pubmed-meshheading:7898938-Macrophage Colony-Stimulating Factor, pubmed-meshheading:7898938-Mice, pubmed-meshheading:7898938-Mice, Inbred C3H, pubmed-meshheading:7898938-Mice, Inbred C57BL, pubmed-meshheading:7898938-Molecular Sequence Data, pubmed-meshheading:7898938-Rats, pubmed-meshheading:7898938-Receptor, Macrophage Colony-Stimulating Factor, pubmed-meshheading:7898938-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:7898938-Receptors, Cell Surface, pubmed-meshheading:7898938-Receptors, Growth Factor, pubmed-meshheading:7898938-Receptors, Vascular Endothelial Growth Factor, pubmed-meshheading:7898938-Recombinant Fusion Proteins, pubmed-meshheading:7898938-Type C Phospholipases, pubmed-meshheading:7898938-Vascular Endothelial Growth Factor Receptor-3
pubmed:year
1995
pubmed:articleTitle
Biochemical characterization of two isoforms of FLT4, a VEGF receptor-related tyrosine kinase.
pubmed:affiliation
Laboratoire d'Oncologie Moléculaire, U.119 Inserm, Marseille, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't