Molecular cloning and characterization of a novel receptor protein tyrosine kinase from human placenta.
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Ziegler SF, Bird TA, Schneringer JA, Schooley KA, Baum PR
Molecular cloning and characterization of a novel receptor protein tyrosine kinase from human placenta.
Oncogene. 1993 Mar;8(3):663-70.
- PubMed ID
- 8382358 [ View in PubMed]
- Abstract
Using a polymerase chain reaction-based approach we have isolated and characterized a cDNA (HPK-6) from human placental RNA encoding a novel receptor protein tyrosine kinase. This receptor tyrosine kinase has a unique extracellular domain, with an immunoglobulin-like domain at the amino terminus followed by three EGF-like cysteine repeats and three fibronectin type III repeats, giving the HPK-6 gene extracellular domain a novel combination of structural motifs. A comparison of the HPK-6 sequence with other receptor tyrosine kinases shows that the HPK-6 gene is the human homolog of the murine tek gene and very closely related to the recently described receptor tyrosine kinase tie. The HPK-6 gene is expressed predominantly in placenta and lung, with a lower level in umbilical vein endothelial cells, brain and kidney. The HPK-6 cDNA, when transfected into COS-7 cells, encodes a 140-kDa protein with in vitro kinase activity.