Effects of lactoferrin on collagen gel contractile activity and myosin light chain phosphorylation in human fibroblasts

FEBS Letters

Mizumachi, Koko¹  Takayama, Yoshiharu¹ 

[1] National Institute of Livestock and Grassland Science, 2 Ikenodai, Kukizaki, Inashiki, Ibaraki 305-0901, Japan

关键词: Lactoferrin;    Cell migration;    Collagen gel contraction;    Myosin light chain phosphorylation;    bLf;    bovine lactoferrin;    hLf;    human lactoferrin;    FBS;    fetal bovine serum;    DMEM;    Dulbecco's minimal essential medium;    Rock;    Rho kinase;    MLC;    myosin light chain;    MLCK;    myosin light chain kinase;    LPA;    lysophosphatidic acid;    TGF-β;    transforming growth factor;    PDGF;    platelet-derived growth factor;    ERK;    extracellular-regulated kinase;    MAPK;    mitogen-activated protein kinase;    PTK;    protein tyrosine kinase;   

DOI  :  10.1016/S0014-5793(01)03041-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

When fibroblasts are plated on a type I collagen gel they reduce the size of the gel and the extent of collagen gel contraction reflects the motile activity of the fibroblasts. We found that both bovine and human lactoferrin (Lf) enhanced the collagen gel contractile activity of WI-38 human fibroblasts. Rho inhibitor (exoenzyme C3), Rho kinase inhibitor (Y-27632), myosin light chain kinase inhibitor (ML-7), MEK inhibitor (PD98059) and Src family tyrosine kinase inhibitor inhibited the Lf-enhanced collagen gel contraction. Treatment of fibroblasts with Lf induced the phosphorylation of myosin light chain (MLC) within 30 min. Lf-enhanced MLC phosphorylation was inhibited by Y-27632 and ML-7. These results suggest that Lf promotes the motility of fibroblasts by regulating MLC phosphorylation.

【 授权许可】

Unknown