期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 13, 页码 5052-5057出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1202653110
关键词
antifreeze glycoprotein; PC3-luciferase cells; galectin-3 knockout PC3-luciferase cells; TF antigen; surface plasmon resonance
资金
- US Army Medical Research and Materiel Command [W81XWH-07-1-0565]
- University of Maryland
- National Institutes of Health (NIH) [CA133935, CA141970, GM070589]
- Council of Higher Education (Turkey)
- NIH [CA105005]
Cancer metastasis and immune suppression are critical issues in cancer therapy. Here, we show that a beta-galactoside-binding lectin [galectin-3 (gal3)] that recognizes the Thomsen-Friedenreich disaccharide (TFD, Gal beta 1,3GalNAc) present on the surface of most cancer cells is involved in promoting angiogenesis, tumor-endothelial cell adhesion, and metastasis of prostate cancer cells, as well as evading immune surveillance through killing of activated T cells. To block gal3-mediated interactions, we purified a glycopeptide from cod (designated TFD100) that binds gal3 with picomolar affinity. TFD100 blocks gal3-mediated angiogenesis, tumor-endothelial cell interactions, and metastasis of prostate cancer cells in mice at nanomolar levels. Moreover, apoptosis of activated T cells induced by either recombinant gal3 or prostate cancer patient serum-associated gal3 was inhibited at nanomolar concentration of TFD100. Because the gal3-TFD interaction is a key factor driving metastasis in most epithelial cancers, this high-affinity TFD100 should be a promising anti-metastatic agent for the treatment of various cancers, including prostate adenocarcinoma.
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