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A new health promoting function of lactoferrin – Visceral fat reduction by enteric-coated bovine lactoferrin

TOMOJI ONO1*, MICHIAKI MURAKOSHI2, HOYOKU NISHINO2

*Corresponding author
1. Lion Corporation, 100 Tajima, Odawara, Kanagawa 256-0811, Japan

2. Kyoto Prefectural University of Medicine, 465 kajii-cho, kawaramachi-hirokoji, kamigyo-ku, Kyoto, 602-8566, Japan

Abstract

Lactoferrin (LF) is an iron-binding glycoprotein found in mammalian breast milk. Its function was initially thought to be immunostimulation or protection from infection because it is present in high concentration in breast milk. The aim of this review is to discuss about a role for LF in regulating lipid metabolism, especially visceral fat reduction. In recent years, several in vivo or human epidemiological studies have demonstrated that LF may modulate lipid metabolism. However, few intervention studies were reported to indicate the positive effect of LF on lipid metabolism. As a matter of course, LF is a protein and is easily degraded by pepsin in the stomach. So we hypothesized that pepsin degraded LF diminish the modulation activity of lipid metabolism. Then we adopted enteric coated LF tablet (eLF) and proved to reduce visceral fat accumulation by RCT. As an action mechanism of eLF, we speculate that LF reach the mesenteric fat, inhibit the lipid synthesis and promote the lipolysis of adipocytes and thereby reduce visceral fat accumulation.


INTRODUCTION

The aim of this review is to discuss about a role for Lactoferrin (LF) in regulating lipid metabolism, especially visceral fat reduction. LF is a glycoprotein found in mammalian breast milk. In humans, the concentration of LF is approximately 1–3 mg/mL in breast milk and 5-7 mg/mL in colostrum. It was originally isolated from bovine milk as a red fraction in 1939 by Sørensen (1). LF belongs to the transferrin family and can contain one or two iron atoms, giving a pale pink colour to its powder and leading to the name “red protein”. The amino acid sequence of human LF was determined by Metz-Boutigue et al. in 1984 and the 3D structure was determined by Anderson et al. in 1987 (2, 3). The N- and C-terminal halves form two separate globular lobes (N-lobe and C-lobe), connected by a short alpha helix, and carrying one iron-binding site each. Commercially available LF is made from cheese whey from bovine milk. The manufacturing process was developed in the mid-1980s and infant formula containing bovine LF (bLF) was produced to improve the intestinal microbial flora (4). Currently, bLF-containing products include yoghurt, skim milk and nutr ...




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