INTERACTION OF INTERLEUKIN-7 (IL-7) WITH GLYCOSAMINOGLYCANS AND ITS BIOLOGICAL RELEVANCE

We have investigated the binding of interleukin 7 (IL-7) to sulfated glycosaminoglycans and evaluated its biological consequences. IL-7 binds to heparin and heparan sulfate, to a lesser extent to dermatan sulfate and does not bind to chondroitin sulfate. It was eluted from heparin by 0.3-0.6 M NaCl and from heparan sulfate by <0.3 M NaCI. We also measured the affinity of IL-7 for heparin using an affinity co-electrophoresis method and found an affinity of 25 nM. In spite of these findings, IL-7 does not bind to the S17 cell line which supports lymphopoiesis. However, addition of heparin to cultures of an IL-7-dependent pre-B cell line (2E8) inhibited IL-7-stimulated proliferation and IL-7 complexed with heparin was more resistant than free IL-7 to protease treatment. Taken together, these results suggest that heparin may act as a carrier for IL-7, blocking its interaction with target cells and protecting it from degradation during transit.