Interaction of interleukin 7 (IL-7) with glycosaminoglycans and its biological relevance
書誌事項
- 公開日
- 1995-05
- 権利情報
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- https://www.elsevier.com/tdm/userlicense/1.0/
- DOI
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- 10.1006/cyto.1995.0041
- 公開者
- Elsevier BV
この論文をさがす
説明
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 by0.3 M NaCl. 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.
収録刊行物
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- Cytokine
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Cytokine 7 (4), 325-330, 1995-05
Elsevier BV