earticle

영어

Multiple earlier studies have shown that interactions between glycans and carbohydrate binding proteins (lectins) displayed on cells surfaces are involved in many important physiological and pathological processes. For example, cell surface lectins in the immune system recognize glycans expressed on the exterior of pathogens and these interactions lead to stimulation of immune responses to pathogens. Mouse SIGN-R1 (SIGN-related 1) is a homolog of human DC-SIGN that is expressed largely on macrophages. This lectin recognizes mannose-rich or fucosylated glycans in a Ca2+-dependent manner. When SIGN-R1 interacts with glycans on host cells, bacteria or viruses, glycan antigens are internalized into cells via lectin-mediated endocytosis to induce immune activation. As a consequence, the lectin hasbecome fascinating markers for recognition and targeting of specific cells to regulate cellular functions and for carbohydrate-based drug discovery. To investigate glycan binding properties of cell surface lectins, we have utilized carbohydrate microarrays which allow high-throughput screening of cell-glycan interactions. Glycan microarrays used in this study were constructed by immobilizing a variety of unmodified carbohydrates onto hydrazide-coated glass slides. SIGN-R1 expressing cells pretreated with Hoechst 33342 were loaded on the glycan microarrays to evaluate the binding properties of the lectin. In addition, purified SIGN-R1 was also applied tothe microarrays for the purpose of comparison. The present study demonstrates the potential of glycan microarrays for profiling of binding specificities of cell surface lectins.