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Volume 272, Number 6, Issue of February 7, 1997 pp. 3330-3335
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Cripto Enhances the Tyrosine Phosphorylation of Shc and Activates Mitogen-activated Protein Kinase (MAPK) in Mammary Epithelial Cells

(Received for publication, June 19, 1996, and in revised form, November 7, 1996)

Subha Kannan a , Marta De Santis a , Matthias Lohmeyer b , David J. Riese IIc , Gilbert H. Smith a , Nancy Hynes e , Masaharu Seno a , Ralf Brandt a , Caterina Bianco a , Graziella Persico f , Nicholas Kenney g , Nicola Normanno h , Isabel Martinez-Lacaci a , Fortunato Ciardiello j , David F. Stern c , William J. Gullick b and David S. Salomon a

From the a Tumor Growth Factor Section, Laboratory of Tumor Immunology and Biology, NIC, National Institutes of Health, Bethesda, Maryland 20892, the b ICRF Oncology Unit, Hammersmith Hospital, London, United Kingdom, the c Department of Pathology, BML-350, Yale University School of Medicine, New Haven, Connecticut 06520-8023, the e Friedrich Meischer-Institut, CH-4002 Basel, Switzerland, the f Istituto Internazionale di Genetica e Biofisca, Naples, Italy, the g Vincent T. Lombardi Cancer Research Center, Georgetown University, Washington, D. C. 20007, the h Oncologia Sperimentale d Istituto Nazionale Per lo Studio e La Cura, Dei Tumori-Fondazione Pascale, Naples, Italy, and the j Cattedra di Oncologia Medica, II Facoltá di Medicina e Chirurgia, Universitá degli Studi di Napoli Federico II, 80131 Naples, Italy

Cripto-1 (CR-1), a recently discovered protein of the epidermal growth factor (EGF) family, was found to interact with a high affinity, saturable binding site(s) on HC-11 mouse mammary epithelial cells and on several different human breast cancer cell lines. This receptor exhibits specificity for CR-1, since other EGF-related peptides including EGF, transforming growth factor alpha , heparin-binding EGF-like growth factor, amphiregulin, epiregulin, betacellulin, or heregulin beta 1 that bind to either the EGF receptor or to other type 1 receptor tyrosine kinases such as erb B-3 or erb B-4 fail to compete for binding. Conversely, CR-1 was found not to directly bind to or to activate the tyrosine kinases associated with the EGFR, erb B-2, erb B-3, or erb B-4 either alone or in various pairwise combinations which have been ectopically expressed in Ba/F3 mouse pro-B lymphocyte cells. However, exogenous CR-1 could induce an increase in the tyrosine phosphorylation of 185- and 120-kDa proteins and a rapid (within 3-5 min) increase in the tyrosine phosphorylation of the SH2-containing adaptor proteins p66, p52, and p46 Shc in mouse mammary HC-11 epithelial cells and in human MDA-MB-453 and SKBr-3 breast cancer cells. CR-1 was also found to promote an increase in the association of the adaptor Grb2-guanine nucleotide exchange factor-mouse son of sevenless (mSOS) signaling complex with tyrosine-phosphorylated Shc in HC-11 cells. Finally, CR-1 was able to increase p42erk-2 mitogen-activated protein kinase (MAPK) activity in HC-11 cells within 5-10 min of treatment. These data demonstrate that CR-1 can function through a receptor which activates intracellular components in the ras/raf/MEK/MAPK pathway.


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