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J Biol Chem, Vol. 274, Issue 13, 8624-8629, March 26, 1999

Cripto-1 Indirectly Stimulates the Tyrosine Phosphorylation of erb B-4 through a Novel Receptor

Caterina BiancoDagger , Subha Kannan§, Marta De SantisDagger , Masaharu Seno, Careen K. Tangparallel , Isabel Martinez-LacaciDagger , Nancy KimDagger , Brenda Wallace-JonesDagger , Marc E. Lippmanparallel , Andreas D. EbertDagger , Christian WechselbergerDagger , and David S. SalomonDagger

From the Dagger  Tumor Growth Factor Section, Laboratory of Tumor Immunology and Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892, § MacMaster University, Hamilton, Ontario, L8S 4K1 Canada,  Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, 3-1-1 Tsushima-Naka, Okayama 700-8530 Japan, and parallel  Lombardi Cancer Center, Department of Biochemistry, Georgetown University Medical Center, Washington, D. C. 20007-2197

Cripto-1 (CR-1) is a recently discovered protein of the epidermal growth factor family that fails to directly bind to any of the four known erb B type 1 receptor tyrosine kinases. The present study demonstrates that CR-1 indirectly induces tyrosine phosphorylation of erb B-4 but not of the epidermal growth factor-related receptors erb B-2 and erb B-3 in different mouse and human mammary epithelial cell lines. In addition, down-regulation of erb B-4 in NMuMG mouse mammary epithelial cells and in T47D human breast cancer cells, using an anti-erb B-4 blocking antibody or a hammerhead ribozyme vector targeted to erb B-4 mRNA, impairs the ability of CR-1 to fully activate mitogen-activated protein kinase. Finally, chemical cross-linking of 125I-CR-1 to mouse and human mammary epithelial cell membranes results in the labeling of two specific bands with a molecular weight of 130 and 60 kDa, suggesting that the CR-1 receptor represents a novel receptor structurally unrelated to any of the known type I receptor tyrosine kinases. In conclusion, these data demonstrate that CR-1, upon binding to an unknown receptor, can enhance the tyrosine kinase activity of erb B-4 and that a functional erb B-4 receptor is required for CR-1-induced MAPK activation.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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