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Science 26 January 1996:
Vol. 271. no. 5248, pp. 509 - 512
DOI: 10.1126/science.271.5248.509
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Reports

Receptor-Ligand Interaction Between CD44 and Osteopontin (Eta-1)

Georg F. Weber (1),  Samy Ashkar (1),  Melvin J. Glimcher,  Harvey Cantor

The CD44 family of surface receptors regulates adhesion, movement, and activation of normal and neoplastic cells. The cytokine osteopontin (Eta-1), which regulates similar cellular functions, was found to be a protein ligand of CD44. Osteopontin induces cellular chemotaxis but not homotypic aggregation, whereas the inverse is true for the interaction between CD44 and a carbohydrate ligand, hyaluronate. The different responses of cells after CD44 ligation by either osteopontin or hyaluronate may account for the independent effects of CD44 on cell migration and growth. This mechanism may also be exploited by tumor cells to promote metastasis formation.


G. F. Weber and H. Cantor, Division of Immunopathology, Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
S. Ashkar and M. J. Glimcher, Department of Orthopedic Research, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.
(1) These authors contributed equally to this study.


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Osteopontin Plays an Important Role in the Development of Medial Thickening and Neointimal Formation.
K. Isoda, K. Nishikawa, Y. Kamezawa, M. Yoshida, M. Kusuhara, M. Moroi, N. Tada, and F. Ohsuzu (2002)
Circ. Res. 91, 77-82
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Progression of tubulointerstitial injury by osteopontin-induced macrophage recruitment in advanced diabetic nephropathy of transgenic (mRen-2)27 rats.
D. J. Kelly, J. L. Wilkinson-Berka, S. D. Ricardo, A. J. Cox, and R. E. Gilbert (2002)
Nephrol. Dial. Transplant. 17, 985-991
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Hypoxia Differentially Enhances the Effects of Transforming Growth Factor-beta Isoforms on the Synthesis and Secretion of Glycosaminoglycans by Human Lung Fibroblasts.
E. Papakonstantinou, M. Roth, M. Tamm, O. Eickelberg, A. P. Perruchoud, and G. Karakiulakis (2002)
J. Pharmacol. Exp. Ther. 301, 830-837
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Prognostic Significance of the Metastasis-associated Protein Osteopontin in Human Breast Cancer.
P. S. Rudland, A. Platt-Higgins, M. El-Tanani, S. de Silva Rudland, R. Barraclough, J. H. R. Winstanley, R. Howitt, and C. R. West (2002)
Cancer Res. 62, 3417-3427
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Osteopontin as a Potential Diagnostic Biomarker for Ovarian Cancer.
J.-H. Kim, S. J. Skates, T. Uede, K.-k. Wong, J. O. Schorge, C. M. Feltmate, R. S. Berkowitz, D. W. Cramer, and S. C. Mok (2002)
JAMA 287, 1671-1679
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Absence of the CD44 Gene Prevents Sarcoma Metastasis.
G. F. Weber, R. T. Bronson, J. Ilagan, H. Cantor, R. Schmits, and T. W. Mak (2002)
Cancer Res. 62, 2281-2286
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Tumor-derived Osteopontin Is Soluble, Not Matrix Associated.
S. R. Rittling, Y. Chen, F. Feng, and Y. Wu (2002)
J. Biol. Chem. 277, 9175-9182
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Cutting Edge: Attenuated Experimental Autoimmune Encephalomyelitis in Eta-1/Osteopontin-Deficient Mice.
M. Jansson, V. Panoutsakopoulou, J. Baker, L. Klein, and H. Cantor (2002)
J. Immunol. 168, 2096-2099
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Contrasting Expression of Thrombospondin-1 and Osteopontin Correlates with Absence or Presence of Metastatic Phenotype in an Isogenic Model of Spontaneous Human Breast Cancer Metastasis.
V. Urquidi, D. Sloan, K. Kawai, D. Agarwal, A. C. Woodman, D. Tarin, and S. Goodison (2002)
Clin. Cancer Res. 8, 61-74
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The Osteopontin-CD44 Survival Signal Involves Activation of the Phosphatidylinositol 3-Kinase/Akt Signaling Pathway.
Y.-H. Lin and H.-F. Yang-Yen (2001)
J. Biol. Chem. 276, 46024-46030
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