A protective effect of milk fat globule EGF factor VIII (MFG-E8) on the spontaneous fusion of milk fat globules in breast milk

2015 ◽  
Vol 158 (1) ◽  
pp. 25-35 ◽  
Author(s):  
T. Yasueda ◽  
K. Oshima ◽  
H. Nakatani ◽  
K. Tabuchi ◽  
D. Nadano ◽  
...  
Keyword(s):  
Breast Milk ◽  
Protective Effect ◽  
Factor Viii ◽  
Milk Fat ◽  
Fat Globules ◽  
Milk Fat Globules ◽  
Milk Fat Globule ◽  
Fat Globule

scholarly journals Milk Fat Globule Membrane Proteome and Micronutrients in the Milk Lipid Fraction: Insights into Milk Bioactive Compounds

Dairy ◽  
2021 ◽  
Vol 2 (2) ◽  
pp. 202-217
Author(s):  
Michele Manoni ◽  
Donata Cattaneo ◽  
Sharon Mazzoleni ◽  
Carlotta Giromini ◽  
Antonella Baldi ◽  
...  
Keyword(s):  
Milk Fat ◽  
Lipid Fraction ◽  
Value Added ◽  
Milk Lipid ◽  
Milk Fat Globule Membrane ◽  
Fat Globules ◽  
Milk Fat Globules ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Value Added Products

Milk lipids are composed of milk fat globules (MFGs) surrounded by the milk fat globule membrane (MFGM). MFGM protects MFGs from coalescence and enzymatic degradation. The milk lipid fraction is a “natural solvent” for macronutrients such as phospholipids, proteins and cholesterol, and micronutrients such as minerals and vitamins. The research focused largely on the polar lipids of MFGM, given their wide bioactive properties. In this review we discussed (i) the composition of MFGM proteome and its variations among species and phases of lactation and (ii) the micronutrient content of human and cow’s milk lipid fraction. The major MFGM proteins are shared among species, but the molecular function and protein expression of MFGM proteins vary among species and phases of lactation. The main minerals in the milk lipid fraction are iron, zinc, copper and calcium, whereas the major vitamins are vitamin A, β-carotene, riboflavin and α-tocopherol. The update and the combination of this knowledge could lead to the exploitation of the MFGM proteome and the milk lipid fraction at nutritional, biological or technological levels. An example is the design of innovative and value-added products, such as MFGM-supplemented infant formulas.

scholarly journals Comparative Proteomics of Milk Fat Globule Membrane (MFGM) Proteome across Species and Lactation Stages and the Potentials of MFGM Fractions in Infant Formula Preparation

Foods ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1251 ◽  
Author(s):  
Michele Manoni ◽  
Chiara Di Lorenzo ◽  
Matteo Ottoboni ◽  
Marco Tretola ◽  
Luciano Pinotti
Keyword(s):  
Milk Fat ◽  
Human Breast Milk ◽  
Primary Role ◽  
Water Emulsion ◽  
Milk Fat Globule Membrane ◽  
Fat Globules ◽  
Lipid Fractions ◽  
Milk Fat Globules ◽  
Milk Fat Globule ◽  
Fat Globule

Milk is a lipid-in-water emulsion with a primary role in the nutrition of newborns. Milk fat globules (MFGs) are a mixture of proteins and lipids with nutraceutical properties related to the milk fat globule membrane (MFGM), which protects them, thus preventing their coalescence. Human and bovine MFGM proteomes have been extensively characterized in terms of their formation, maturation, and composition. Here, we review the most recent comparative proteomic analyses of MFGM proteome, above all from humans and bovines, but also from other species. The major MFGM proteins are found in all the MFGM proteomes of the different species, although there are variations in protein expression levels and molecular functions across species and lactation stages. Given the similarities between the human and bovine MFGM and the bioactive properties of MFGM components, several attempts have been made to supplement infant formulas (IFs), mainly with polar lipid fractions of bovine MFGM and to a lesser extent with protein fractions. The aim is thus to narrow the gap between human breast milk and cow-based IFs. Despite the few attempts made to date, supplementation with MFGM proteins seems promising as MFGM lipid supplementation. A deeper understanding of MFGM proteomes should lead to better results.

Glycoprotein Filament Removal From Human Milk Fat Globules by Heat Treatment

PEDIATRICS ◽  
1988 ◽  
Vol 81 (1) ◽  
pp. 141-146
Author(s):  
Wolfgang Buchheim ◽  
Ulrich Welsch ◽  
Gail E. Huston ◽  
Stuart Patton
Keyword(s):  
Milk Fat ◽  
Electrophoretic Analysis ◽  
Fat Absorption ◽  
Fat Globules ◽  
Heated Milk ◽  
Milk Fat Globules ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Human Milk Fat ◽  
Additional Explanation

Freeze-etch electron microscopy was applied to milk fat globules to observe surface details. A remarkable array of filaments, approximately 0.5 µm in length, was seen on human, but not bovine, globules. Heating human globules removed the filaments that were identified as high molecular weight glycoproteins by freezeetch and gel electrophoretic analysis of the heating medium. Extraction of these globule glycoproteins was slight at 60°C for one minute but substantial and tending to plateau at 80°C for one minute. Such heat-induced alterations of the milk fat globule surface provide an alternative or additional explanation to milk lipase inactivation as the cause of reduced milk fat absorption from heated milk by the preterm infant.

Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains

2009 ◽  
Vol 390 (1) ◽  
Author(s):  
Fernando Sánchez-Juanes ◽  
Josefa M. Alonso ◽  
Lorena Zancada ◽  
Pablo Hueso
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Milk Fat ◽  
Fatty Acid Content ◽  
Fat Globules ◽  
Whole Milk ◽  
Milk Fat Globules ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Milk Fat Globule Membranes

AbstractSeveral components of milk fat globule membranes (MFGMs) have been reported to display beneficial health properties and some of them have been implicated in the defense of newborns against pathogens. These observations prompted us to determine the glycosphingolipid content of MFGMs and their interaction with pathogens. A comparative study with whole milk components was also carried out. Milk fat globules and MFGMs were isolated from milk. Gangliosides and neutral glycosphingolipids were obtained from MFGMs and whole milk and their fatty acid contents were determined by gas chromatography-mass spectrometry (GC-MS). MFGMs and whole milk showed similar ganglioside and neutral glycosphingolipid contents, with whole milk having more GM3 and glucosylceramide and less GD3,O-acetyl GD3,O-acetyl GT3, and lactosylceramide. The fatty acid content of gangliosides from both sources showed a similar composition. However, the neutral glycosphingolipid fatty acid content seemed to be quite different. Whole milk had fewer very-long-chain fatty acids (18.1% vs. 46.4% in MFGMs) and more medium-chain and unsaturated C18:1 and C18:2 fatty acids. Milk fat globules, MFGMs, lactosylceramide, and gangliosides GM3 and GD3 were observed to bind enterotoxigenicEscherichia colistrains. Furthermore, bacterial hemagglutination was inhibited by MFGMs and glycosphingolipids.

scholarly journals The endoplasmic reticulum and casein-containing vesicles contribute to milk fat globule membrane

2016 ◽  
Vol 27 (19) ◽  
pp. 2946-2964 ◽  
Author(s):  
Edith Honvo-Houéto ◽  
Céline Henry ◽  
Sophie Chat ◽  
Sarah Layani ◽  
Sandrine Truchet
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Milk Fat ◽  
Milk Secretion ◽  
Milk Fat Globule Membrane ◽  
Fat Globules ◽  
Milk Fat Globules ◽  
Milk Fat Globule ◽  
Fat Globule ◽  
Milk Fat Globule Membranes

During lactation, mammary epithelial cells secrete huge amounts of milk from their apical side. The current view is that caseins are secreted by exocytosis, whereas milk fat globules are released by budding, enwrapped by the plasma membrane. Owing to the number and large size of milk fat globules, the membrane surface needed for their release might exceed that of the apical plasma membrane. A large-scale proteomics analysis of both cytoplasmic lipid droplets and secreted milk fat globule membranes was used to decipher the cellular origins of the milk fat globule membrane. Surprisingly, differential analysis of protein profiles of these two organelles strongly suggest that, in addition to the plasma membrane, the endoplasmic reticulum and the secretory vesicles contribute to the milk fat globule membrane. Analysis of membrane-associated and raft microdomain proteins reinforces this possibility and also points to a role for lipid rafts in milk product secretion. Our results provide evidence for a significant contribution of the endoplasmic reticulum to the milk fat globule membrane and a role for SNAREs in membrane dynamics during milk secretion. These novel aspects point to a more complex model for milk secretion than currently envisioned.

Origin of Milk Fat Globules and the Nature of the Milk Fat Globule Membrane

1983 ◽  
pp. 83-118 ◽  
Author(s):  
T. W. Keenan ◽  
Daniel P. Dylewski ◽  
Terry A. Woodford ◽  
Rosemary H. Ford
Keyword(s):  
Milk Fat ◽  
Milk Fat Globule Membrane ◽  
Fat Globules ◽  
Milk Fat Globules ◽  
Milk Fat Globule ◽  
Fat Globule

Thermal effects on IgM-milk fat globule-mediated agglutination

2018 ◽  
Vol 86 (1) ◽  
pp. 108-113 ◽  
Author(s):  
Steffen F. Hansen ◽  
Lotte B. Larsen ◽  
Lars Wiking
Keyword(s):  
Milk Fat ◽  
Storage Temperature ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Immunoglobulin M ◽  
Laser Scanning Microscopy ◽  
Fat Globules ◽  
Milk Fat Globules ◽  
Milk Fat Globule ◽  
Fat Globule

AbstractThe process of agglutination causes firm cream layers in bovine milk, and a functioning agglutination mechanism is paramount to the quality of non-homogenized milks. The phenomenon is not well-described, but it is believed to occur due to interactions between immunoglobulins (Ig) and milk fat globules. For the first time, this paper demonstrates how the process of agglutination can be visualized using confocal laser scanning microscopy, rhodamine red and a fluoresceinisothiocynat-conjugated immunoglobulin M antibody. The method was used to illustrate the effect on agglutination of storage temperature and pasteurization temperature. Storage at 5 °C resulted in clearly visible agglutination which, however, was markedly reduced at 15 °C. Increasing storage temperature to 20 or 37 °C cancelled any detectable interaction between IgM and milk fat globules, whereby the occurrence of cold agglutination was documented. Increasing 20 s pasteurization temperatures from 69 °C to 71 °C and further to 73 °C lead to progressively higher inactivation of IgM and, hence, reduction of agglutination. Furthermore, 2-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that changes in storage temperature caused a redistribution of Ig-related proteins in milk fat globule membrane isolates. Poly-immunoglobulin G receptor was present in milk fat globule preparations stored at cold (4 °C) conditions, but absent at storage at higher temperature (25 °C). The findings provide valuable knowledge to dairy producers of non-homogenized milk in deciding the right pasteurization temperature to retain the crucial agglutination mechanism.

Sign in / Sign up

Export Citation Format

Share Document