TY - GEN
T1 - Galectin-3C
T2 - Human lectin for treatment of cancer
AU - Jarvis, Gary A.
AU - Mirandola, Leonardo
AU - Yuefei, Yu
AU - Cobos, Everardo
AU - Chiriva-Internati, Maurizio
AU - John, Constance M.
PY - 2012/12/18
Y1 - 2012/12/18
N2 - A summary is provided of the compelling data supporting galectin-3, as a target for cancer therapy, and for the clinical development of a truncated form of human galectin-3, termed galectin-3C, for cancer. Lacking the N-terminal domain of galectin-3 that facilitates its multimerization when bound to carbohydrate ligands, galectin-3C functions as an inhibitor of the galectin-3 crosslinking mediated by the N-terminal domain that can be induced by multivalent oligosaccharides and glycoconjugates intra- or extracellularly, on cell surfaces, or in extracellular matrices. Numerous studies show that galectin-3 plays a key role in tumorigenicity and metastasis and is a novel target for the development of cancer therapeutics. Data presented indicate that galectin-3C can be localized in a carbohydrate-dependent manner similar to most information reported regarding galectin-3. Exogenous galectin-3C facilitated anoikis in human breast cells, illustrating an effect it is expected to produce in vivo by reducing cell-cell or cell-ECM adhesion of metastatic cells. Based on the activity of galectin-3, we postulate that galectin-3C also inhibits the metastatic process by preventing integrin activation and focal adhesion turnover. The data described provide evidence of the important functions of galectin-3 in the processes of metastasis and tumorigenicity, and the potential therapeutic effect of inhibiting the activity of galectin-3 with galectin-3C. Galectin-3 has a complex, multi-faceted role that is critical in the relationship between the cells of various types of malignancies and the microenvironment, and further development of galectin-3C as a clinical candidate for cancer treatment is warranted.
AB - A summary is provided of the compelling data supporting galectin-3, as a target for cancer therapy, and for the clinical development of a truncated form of human galectin-3, termed galectin-3C, for cancer. Lacking the N-terminal domain of galectin-3 that facilitates its multimerization when bound to carbohydrate ligands, galectin-3C functions as an inhibitor of the galectin-3 crosslinking mediated by the N-terminal domain that can be induced by multivalent oligosaccharides and glycoconjugates intra- or extracellularly, on cell surfaces, or in extracellular matrices. Numerous studies show that galectin-3 plays a key role in tumorigenicity and metastasis and is a novel target for the development of cancer therapeutics. Data presented indicate that galectin-3C can be localized in a carbohydrate-dependent manner similar to most information reported regarding galectin-3. Exogenous galectin-3C facilitated anoikis in human breast cells, illustrating an effect it is expected to produce in vivo by reducing cell-cell or cell-ECM adhesion of metastatic cells. Based on the activity of galectin-3, we postulate that galectin-3C also inhibits the metastatic process by preventing integrin activation and focal adhesion turnover. The data described provide evidence of the important functions of galectin-3 in the processes of metastasis and tumorigenicity, and the potential therapeutic effect of inhibiting the activity of galectin-3 with galectin-3C. Galectin-3 has a complex, multi-faceted role that is critical in the relationship between the cells of various types of malignancies and the microenvironment, and further development of galectin-3C as a clinical candidate for cancer treatment is warranted.
UR - http://www.scopus.com/inward/record.url?scp=84905234507&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84905234507&partnerID=8YFLogxK
U2 - 10.1021/bk-2012-1115.ch012
DO - 10.1021/bk-2012-1115.ch012
M3 - Conference contribution
AN - SCOPUS:84905234507
SN - 9780841228801
T3 - ACS Symposium Series
SP - 195
EP - 232
BT - Galectins and Disease Implications for Targeted Therapeutics
PB - American Chemical Society
ER -