We performed comprehensive analysis of the cell surface glycomic signature of human embryonic stem cells (hESCs) and human induced pluripotent stem cells (hiPSCs). We clarified the characteristic feature of the glycome of hESCs/hiPSCs, and identified a lectin termed rBC2LCN that reacts with hESCs/hiPSCs. We then developed a technology to detect and eliminate hESCs/hiPSCs resided in cell therapy products (CTPs) using rBC2LCN. More recently, we developed a technique to detect deviated cells, cells that have deviated from the undifferentiated state of hiPSCs. Here, we would like to introduce glycan-based quality control technologies of the hESCs/hiPSCs that we’ve developed so far.
Galectin is a well-known molecular entity but remains difficult to understand. Although it appears on a wide variety of stages, it is seldom the main actor; its role seems to be supporting but indispensable. It acts with a wide variety of partners whatever their identity (protein, lipid, or proteoglycan) or position, as long as they are wearing a favorite costume (glycan). Therefore, almost all (more than 10,000) extracellular proteins can be its partners, although its relationships with them are not so intimate. This wide and shallow sociality makes the essential nature of galectin difficult to understand. With these aspects in mind, I would like to review some basic points concerning galectin and its weak interactions.
