期刊
FEBS LETTERS
卷 508, 期 1, 页码 111-116出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(01)03041-1
关键词
lactoferrin; cell migration; collagen gel contraction; myosin light chain phosphorylation
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. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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