Chemokines are a group of small molecules that regulate cell migration and behavior in diverse contexts. The chemokine CXCL12 binds with the receptor CXCR4 and has been found to be closely related to the malignant growth of more than twenty different human neoplasms. Recent studies have shown that the chemokine CXCL14 also binds to CXCR4 with high affinity and inhibits the CXCL12-mediated chemotaxis of leukemia-derived cells. The functions of these chemokines are mediated by glycosaminoglycans (GAGs) such as heparin which are critical regulators of cell migration during organogenesis and immunosurveillance.  This study will investigate the binding of CXCL12 and CXCL14 to heparin and heparan sulfate oligosaccharides using Affinity Capillary Electrophoresis (ACE). ACE has many benefits for determining binding constants for chemokine-GAG interaction including low sample consumption and easy automation. Knowledge of the binding constants is useful in identifying high affinity binding GAG oligosaccharides responsible for mediating chemokine function.

Studying the binding interactions of the chemokines CXCL12 and CXCL14 to heparin and heparan sulfate using affinity capillary electrophoresis

249th National Meeting (2015)

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