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Polyelectrolyte Complex for Heparin Binding Domain Osteogenic Growth Factor Delivery
Published on: August 22, 2016
Structural features in carrageenan that interact with a heparin-binding hematopoietic growth factor and modulate its
Aiye Liang1, Xiaomian Zhou, Qiuyan Wang
1Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023, China.
Abstract:
The effects of carrageenans' structural features on its interaction with granulocyte colony-stimulating factor (G-CSF) and on the growth and differentiation of a G-CSF dependent leukemia cell line (NFS-60) were studied. lambda, iota, and kappa carrageenans, with decreasing contents of sulfation, bound to G-CSF with binding constants of (6.2+/-0.6) x 10(5)M(-1), (7.4+/-0.5) x 10(5)M(-1) and (6.0+/-0.4) x 10(5)M(-1), and with 27.7+/-0.2, 17.4+/-0.1 and 8.4+/-0.1 binding sites, respectively. However, kappa carrageenan oligosaccharide had no affinity for G-CSF. The three carrageenans significantly inhibited G-CSF-induced growth of NFS-60 cells. The high sulfate content lambda carrageenan could also induce the maturation of the cells, but relatively low sulfate content iota and kappa carrageenans could not. The results suggested that G-CSF-carrageenan bindings were dependent on carrageenans' sulfate contents and chain lengths, which could also affect the growth and differentiation of NFS-60 cells.
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