Comparison of Proliferative Effect of Human Lactoferrin and Its Proteolytic Peptide on Normal and Transformed Epithelial Cells

Abstract

Human lactoferrin (hLF) is an iron-binding glycoprotein with a variety of functions. hLF undergoes proteolytic cleavage to smaller peptides in the stomach following ingestion. In the present study, we evaluated the effects of hLF and its proteolytic product, human lactoferrin peptide (hLFP), on the proliferation of two epithelial cells, HEK293 normal cells and KATO III gastric carcinoma cells, using an MTT assay and expression of proliferative nuclear cell antigen (PCNA), a notable proliferation marker. When the two epithelial cells were stimulated with hLF and hLFP in the presence of fetal bovine serum (FBS), hLFP stimulated proliferation of both cell types at lower concentrations than hLF by two orders of magnitude. The cancer cells exhibited proliferative responses to both hLF and hLFP at lower concentrations by 23 orders of magnitude than the normal cells. Either hLF or hLFP alone did not support appreciable proliferation of these cell lines in the absence or low concentrations of FBS. Bovine serum albumin or its proteolytic product failed to promote cellular proliferation even in the presence of 10 % FBS, indicating the specificity of the proliferative activity of hLF and hLFP. These data highlight feasibility of hLF and its peptide for adjuvants for tissue culture medium.