B61 is a ligand for the ECK receptor protein-tyrosine kinase
| Autor: | Richard A. Lindberg, Gary M. Fox, Robin Elliott, Ming Zhang, Vann P. Parker, Brian Varnum, Anne Colombero, James D. Skrine, Yosef Yarden, Geraldine Trail, William J. Boyle, Tony Hunter, Timothy D. Bartley, Robert J. Toso, Andrew A. Welcher, Paige Holst, Elsa Fernandez, Brenda Guthrie, Robert W. Hunt, Hsieng Sen Lu |
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| Rok vydání: | 1994 |
| Předmět: |
Molecular Sequence Data
CHO Cells Biology Ligands EPH receptor B2 Tropomyosin receptor kinase C Cell Line Affinity chromatography Cricetinae Enzyme-linked receptor Animals Humans Amino Acid Sequence Cloning Molecular Orphan receptor Multidisciplinary Receptor EphA2 Autophosphorylation Membrane Proteins Proteins Ephrin-A1 Protein-Tyrosine Kinases Ligand (biochemistry) Recombinant Proteins Biochemistry Tyrosine kinase |
| Zdroj: | Nature. 368(6471) |
| ISSN: | 0028-0836 |
| Popis: | A protein ligand for the ECK receptor protein-tyrosine kinase has been isolated by using the extracellular domain (ECK-X) of the receptor as an affinity reagent. Initially, concentrated cell culture supernatants were screened for receptor binding activity using immobilized ECK-X in a surface plasmon resonance detection system. Subsequently, supernatants from selected cell lines were fractionated directly by receptor affinity chromatography, resulting in the single-step purification of B61, a protein previously identified as the product of an early response gene induced by tumour necrosis factor-alpha. We report here that recombinant B61 induces autophosphorylation of ECK in intact cells, consistent with B61 being an authentic ligand for ECK. ECK is a member of a large orphan receptor protein-tyrosine kinase family headed by EPH, and we suggest that ligands for other members of this family will be related to B61, and can be isolated in the same way. |
| Databáze: | OpenAIRE |
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