Axl receptor tyrosine kinase stimulated by the vitamin K-dependent protein encoded by growth-arrest-specific gene 6

• Published in: Nature (London) Vol. 373; no. 6515; pp. 623 - 626
• Main Authors: Varnum, Brian C, Young, Cynthia, Elliott, Gary, Garcia, Andy, Bartley, Timothy D, Fridell, Yih-Woei, Hunt, Robert W, Trail, Geraldine, Clogston, Chris, Toso, Robert J, Yanagihara, Donna, Bennett, Larry, Sylber, Maura, Merewether, Lee Anne, Tseng, Alice, Escobar, Eva, Liu, Edison T, Yamane, Harvey K
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 16.02.1995; Nature Publishing Group
• Subjects: Amino Acid Sequence; Animals; Biological and medical sciences; Cell physiology; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes; CHO Cells; Cricetinae; Cross-Linking Reagents; Deoxyribonucleic acid; DNA; Enzyme Activation; Fundamental and applied biological sciences. Psychology; Genes; Humans; Intercellular Signaling Peptides and Proteins; Leukemia; Ligands; Molecular and cellular biology; Molecular Sequence Data; Oncogene Proteins - metabolism; Protein Binding; Proteins; Proteins - isolation & purification; Proteins - metabolism; Proto-Oncogene Proteins; Receptor Protein-Tyrosine Kinases - metabolism; Recombinant Proteins; Tumor Cells, Cultured; Vitamin K - metabolism; Vitamins; Cell line; Enzyme; Ligand; Gene product; Transferases; Cell cycle; Cell transformation; In vitro; Protein-tyrosine kinase; Biological receptor
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/373623a0

The Axl receptor tyrosine kinase was identified as a protein encoded by a transforming gene from primary human myeloid leukaemia cells by DNA-mediated transformation of NIH 3T3 cells. Axl is the founding member of a family of related receptors that includes Eyk, encoded by a chicken proto-oncogene originally described as a retroviral transforming gene, and c-Mer, encoded by a human proto-oncogene expressed in neoplastic B- and T-cell lines. The transforming activity of Axl demonstrates that the receptor can drive cellular proliferation. The function of Axl in non-transformed cells and tissues is unknown, but may involve the stimulation of cell proliferation in response to an appropriate signal, namely a ligand that activates the receptor. We report here the purification of an Axl stimulatory factor, and its identification as the product of growth-arrest-specific gene 6 (ref. 6). This is, to our knowledge, the first description of a ligand for the Axl family of receptors.