ADSORPTION OF FIBRONECTIN, ALBUMIN AND FIBROBLAST GROWTH FACTOR-BASICONTO POLYELECTROLYTE COMPLEX (PEC), WHICH CONTROLS HUMAN PERIODONTAL-LIGAMENT FIBROBLAST (HPLF) PROLIFERATION AND DIFFERENTIATION
T. Hamano et al., ADSORPTION OF FIBRONECTIN, ALBUMIN AND FIBROBLAST GROWTH FACTOR-BASICONTO POLYELECTROLYTE COMPLEX (PEC), WHICH CONTROLS HUMAN PERIODONTAL-LIGAMENT FIBROBLAST (HPLF) PROLIFERATION AND DIFFERENTIATION, Journal of macromolecular science. Pure and applied chemistry, A35(10), 1998, pp. 1681-1693
Cells in vivo are surrounded by many types of extracellular matrices (
e.g., collagen, proteoglycans, and adhesion proteins), vitamins, growt
h factors, and hormones which control cell functions. Poly-electrolyte
complex (PEC), composed of polysaccharides, has a structure similar t
o that of glycosaminoglycans. In order to assess the importance of the
adsorption of fibronectin (hFN), albumin (Alb), and fibroblast growth
factor-basic (FGF-b) onto PECs in effecting cell proliferation, the h
FN and Alb adsorbed onto the surface had a charge balance which decrea
sed with the increasing negative charge on CS100-SCHNx (SPECs). Howeve
r, in the case of using CCHN70 as a polyanion, the amount of their ads
orption was at minimum when the charge balance = 0. Moreover, Alb adso
rption onto PECs increased with an increase in the degree of substitut
ion of anionic functional groups of polyanion. On the other hand, the
amount of FGF-b adsorption onto CPEC70 (CS100-CCHN70) was higher than
that onto SPECs, although cell proliferation was more pronounced on SP
ECs than on CPEC70. As has been reported previously [1], cell morpholo
gies showed an aggregate on CPEC70 and a spreading on SPECs. Therefore
, the high amount of FGF-b adsorption onto CPEC70 might be attributabl
e to induce cell aggregation and differentiation.