Abstract

Publisher Summary The diversity of glycan structures in cellular glycoconjugates is reflected in the level of proteins harboring carbohydrate-binding activity. Therefore, distinct oligosaccharide epitopes can be likened to coding units. In regard to lectins linking the sugar code with biological responses, their emerging complexity in human and animal tissues had not been anticipated despite the application of various plant agglutinins as laboratory tools. As experienced with other lectin families, thorough scrutiny for galectins has uncovered a still growing list of members. With functions in cell adhesion and growth control, monitoring the presence of galectins has become a topic of interest in cancer research, pathology, and developmental biology. However, the described situation raises serious problems, especially for the interpretation of immunohistochemical data. Accounts on galectins 4, 7, 8, and 9, with an impact on growth control or other characteristics associated with malignancy, epitomize important lectin functionality beyond these two types, and the functional divergence noted between galectins 1 and 3 in a tumor model with competition for the same ligand emphasizes the requirement for comprehensive monitoring. To address this issue, a convenient and reliable method for profiling the expression of all members of a defined protein family is required. Thus, a routine assay to determine, as an example, the profile of galectin expression using human tumor cell lines as a model is developed.

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