title: The bovine lactoferrin region responsible for promoting the collagen gel contractile activity of human fibroblasts.
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.
authors.affiliation: Functional Biomolecule Laboratory, National Institute of Livestock and Grassland Science, 2 Ikenodai, Tsukuba, Ibaraki 305-0901, Japan. takay@affrc.go.jp
authors.forename: Yoshiharu
authors.initials: Y
authors.lastname: Takayama
authors.forename: Koko
authors.initials: K
authors.lastname: Mizumachi
authors.forename: Toshiaki
authors.initials: T
authors.lastname: Takezawa
mesh_terms: D000818:Animals; D002417:Cattle; D002460:Cell Line; D003094:Collagen / Q000502:physiology*; D004305:Dose-Response Relationship, Drug; D005347:Fibroblasts / Q000502:physiology*; D005782:Gels; D006801:Humans; D007781:Lactoferrin / Q000737:chemistry* / Q000494:pharmacology*; D018994:Myosin Light Chains / Q000378:metabolism; D010446:Peptide Fragments / Q000494:pharmacology; D010766:Phosphorylation
chemical_list: D005782:Gels; D018994:Myosin Light Chains; D010446:Peptide Fragments; D003094:Collagen; D007781:Lactoferrin