RRC ID 1198
著者 Takayama Y, Mizumachi K, Takezawa T.
タイトル The bovine lactoferrin region responsible for promoting the collagen gel contractile activity of human fibroblasts.
ジャーナル Biochem Biophys Res Commun
Abstract We have reported that bovine lactoferrin (bLf) promotes the contractile activity of collagen gels by WI-38 human fibroblasts via the phosphorylation of myosin light chain (MLC). To identify the region of bLf that is responsible for this activity, we prepared bLf fragments by limited proteolysis using trypsin and investigated the effects of each fragment on gel contractile activity. Lf consists of a single polypeptide chain containing two lobes that are independent globular structures termed the N- and C-lobes. The fragment corresponding to the C-lobe of bLf (amino acids 341-689) had a more prominent effect on collagen gel contractile activity than did that of either native bLf or its N-lobe (1-284). Further hydrolysis of the C-lobe with either pepsin or trypsin resulted in a loss of this activity. The effect of the C-lobe on collagen gel contraction by fibroblasts was dose-dependent and was associated with the elevation of MLC phosphorylation.
巻・号 299(5)
ページ 813-7
公開日 2002-12-20
DOI 10.1016/s0006-291x(02)02748-1
PII S0006291X02027481
PMID 12470651
MeSH Animals Cattle Cell Line Collagen / physiology* Dose-Response Relationship, Drug Fibroblasts / physiology* Gels Humans Lactoferrin / chemistry* Lactoferrin / pharmacology* Myosin Light Chains / metabolism Peptide Fragments / pharmacology Phosphorylation
IF 2.985
引用数 13
WOS 分野 BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
ヒト・動物細胞 WI-38