Aberrant glycosylation is a well-recognized phenomenon that occurs on the surface of
tumor cells, and the overexpression of a number of
ligands (such as TF, sialyl Tn, and
sialyl Lewis X) has been correlated to a worse prognosis for the patient. These unique
carbohydrate structures play an integral role in cell-cell communication and have also been associated with more metastatic
cancer phenotypes, which can result from binding to
lectins present on cell surfaces. The most well studied
metastasis-associated
lectins are the
galectins and
selectins, which have been correlated to adhesion, neoangiogenesis, and immune-cell evasion processes. In order to slow the rate of metastatic lesion formation, a number of approaches have been successfully developed which involve interfering with the
tumor lectin-substrate binding event. Through the generation of inhibitors, or by attenuating
lectin and/or
carbohydrate expression, promising results have been observed both in vitro and in vivo. This article briefly summarizes the involvement of
lectins in the metastatic process and also describes different approaches used to prevent these undesirable
carbohydrate-
lectin binding events, which should ultimately lead to improvement in current
cancer therapies.