Stimulation by bovine lactoferrin of nerve growth factor synthesis/secretion in mouse L-M cells.
Cultured mouse fibroblasts synthesize and secrete nerve growth factor (NGF). To learn the mechanism of action of an iron-binding protein, lactoferrin (Lf), on cultured animal cells, we have examined the effects of bovine Lf (bLf) on NGF synthesis/secretion in mouse L-M cells, a line derived from L929 fibroblast cells. Both apo- and holo-bLf induced an increase in NGF content in the cell-conditioned medium (CM) with similar effectiveness. Neither apo- nor holo- bovine transferrin (bTf) was effective, indicating that the observed induction of NGF production cannot be attributed to stimulation of iron transport. A basic peptide fragment of bLf (residues 17-41) isolated from a pepsin hydrolyzate of bLf was found to be effective for stimulation of NGF synthesis/secretion in L-M cells. This observation demonstrates that the basic nature of Lf is important for its interaction with fibroblast cells.
Shinoda
I
I
Nutritional Science Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.
Fukuwatari
Y
Y
Shimamura
S
S
Tomita
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D017077:Culture Media, Conditioned; D007739:L Cells; D007781:Lactoferrin / Q000737:chemistry / Q000494:pharmacology*; D051379:Mice; D008969:Molecular Sequence Data; D009414:Nerve Growth Factors / Q000096:biosynthesis* / Q000378:metabolism; D010446:Peptide Fragments / Q000494:pharmacology; D014168:Transferrin / Q000494:pharmacology
D017077:Culture Media, Conditioned; D009414:Nerve Growth Factors; D010446:Peptide Fragments; D014168:Transferrin; D007781:Lactoferrin