Post-weaning increases in the milk-fat globule EGF-factor VIII on fat globules in mouse milk and in the uptake of the fat globules by HC11 mammary epithelial cells

Nakatani, Hajime; Yasueda, Takehiko; Oshima, Kenzi; Okajima, Tetsuya; Nadano, Daita; Flint, David; Matsuda, Tsukasa

doi:10.1093/jb/mvs116

Cited by 7 publications

(4 citation statements)

References 32 publications

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“…Milk fat globules are phagocytosed in fact by HC11 mouse mammary epithelial cells in vitro , and milk fat globules recovered from involuting mammary glands are taken up by HC11 cells more effectively than those from lactating mammary glands [ 15 ]. Interestingly, MFG-E8 is present on some, but not all, milk fat globules in breast milk at lactation stages, whereas most of MFGs are MFG-E8 positive at early involution stages [ 15 , 16 ].…”

Section: Mammary Gland Development and Involutionmentioning

confidence: 99%

MFG-E8: Origin, Structure, Expression, Functions and Regulation

Oshima

Yasueda

Nishio

et al. 2014

MFG-E8 and Inflammation

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Milk Fat Globule-Epidermal Growth Factor-Factor 8 (MFG-E8) with bivalent binding activity to integrin receptors and acidic phospholipids is a secretary glycoprotein exhibiting versatile functions in cell physiology affecting health and diseases. Recent progress in genomics and structural biology studies, in addition to long time accumulation of classical biochemical studies, has been showing its unique molecular structure advantageous to the link between cells and their target cells as well as molecular complexes and its critical roles in regulating infl ammation and immunity. MFG-E8 is expressed and secreted by a variety of cells and tissues, especially professional and non-professional phagocytes such as macrophages, immature dendritic cells and the epithelial cells of mammary glands and epididymis. Although MFG-E8 expression has been shown to be up-regulated by a lactogenic hormone, prolactin (PRL), and neuronal chemokine, fractalkine, molecular mechanisms involved in MFG-E8 expression in health and disease states remain largely unknown. The secreted MFG-E8 specifi cally recognizes the acidic phospholipids and opsonized the targets to be cleared by phagocytosis mainly in paracrine and occasionally in endocrine manners. In addition to the enhancing role in phagocytosis, MFG-E8 binds to its target cells expressing MFG-E8 receptors and acts as a ligand, which modulates infl ammatory responses. Moreover, MFG-E8 alone shows ligand activity to intestinal epithelial cells locally exposing the acidic phospholipids and vascular endothelial cells expressing the integrins.

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Section: Mammary Gland Development and Involutionmentioning

confidence: 99%

MFG-E8: Origin, Structure, Expression, Functions and Regulation

Oshima

Yasueda

Nishio

et al. 2014

MFG-E8 and Inflammation

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“…Milk fat globules (MFGs) are membrane-bound structures varying in size between 0.2 μm and 15 μm that derive from the endoplasmic reticulum of mammary gland epithelial cells [ 32 , 33 ]. Human and mouse milk fat globules have average diameters between 4–5 and 4–7 μm, respectively [ 34 , 35 ]. Milk fat globules and milk cells are both present in the cell pellet of milk and are sometimes collectively referred to as membrane enclosed structures, visible by brightfield imaging ( Fig 2A ) [ 11 ].…”

Section: Resultsmentioning

confidence: 99%

Characterization and comparison of human and mouse milk cells

Doerfler,

Yerneni,

Newby

et al. 2024

PLoS ONE

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Recent data has characterized human milk cells with unprecedented detail and provided insight into cell populations. While such analysis of freshly expressed human milk has been possible, studies of cell functionality within the infant have been limited to animal models. One commonly used animal model for milk research is the mouse; however, limited data are available describing the composition of mouse milk. In particular, the maternal cells of mouse milk have not been previously characterized in detail, in part due to the difficulty in collecting sufficient volumes of mouse milk. In this study, we have established a method to collect high volumes of mouse milk, isolate cells, and compare the cell counts and types to human milk. Surprisingly, we found that mouse milk cell density is three orders of magnitude higher than human milk. The cell types present in the milk of mice and humans are similar, broadly consisting of mammary epithelial cells and immune cells. These results provide a basis of comparison for mouse and human milk cells and will inform the most appropriate uses of mouse models for the study of human phenomena.

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“…S2 in Supporting Information). MFG-E8 is primarily secreted as one of soluble proteins in milk serum (whey) and then gradually binds to the surfaces of the milk fat globule membranes retained in the luminal space of lactating mammary gland (Nakatani et al 2013;Yasueda et al 2015). To investigate the contribution of integrins to the transcriptional suppression of b-casein by MFG-E8, HC11 cells were cultured on the conditioned dish including the RGD motif mutant MFG-E8.…”

Section: Integrin-dependent Suppression Of B-casein Gene Expression Imentioning

confidence: 99%

“…These results indicate that MFG-E8 in ECM plays a role in suppression of gene expression in an integrin-dependent manner. MFG-E8 is primarily secreted as one of soluble proteins in milk serum (whey) and then gradually binds to the surfaces of the milk fat globule membranes retained in the luminal space of lactating mammary gland (Nakatani et al 2013;Yasueda et al 2015). To evaluate the suppressive ability of MFG-E8 secreted into the luminal space, milk serum samples prepared from the wild-type and MFG-E8-deficient mice were added to the culture media during hormone induction.…”

Section: Integrin-dependent Suppression Of B-casein Gene Expression Imentioning

confidence: 99%

Extracellular vesicle‐mediated MFG‐E8 localization in the extracellular matrix is required for its integrin‐dependent function in mouse mammary epithelial cells

et al. 2017

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Milk fat globule-EGF factor 8 (MFG-E8) is a divalent-binding secretory protein possessing an Arg-Gly-Asp (RGD) motif and a phosphatidylserine (PS)-binding motif. This protein has been shown to be involved in mammary gland development and morphogenesis. Integrin-binding activity is necessary for these MFG-E8-dependent cell processes. Although the target cells and molecules of MFG-E8 in the cellular microenvironment are important to understand its physiological function, its localization is largely unclear. Here, we found that mouse MFG-E8 localized to the basal lamina of the mammary gland during involution. In a model system of mammary COMMA-1D cells, exogenously and endogenously expressed MFG-E8 was deposited in the extracellular matrix (ECM) with membranous particles dependently on the PS-binding motifs in the discoidin domains that were essential for association ability to extracellular vesicles (EVs). These data showed the basal MFG-E8 localization mechanism in which EVs served as a scaffold. Such an immobilized MFG-E8 associating with cell substrata but not soluble one in the culture media promoted integrin-dependent suppression of β-casein expression. These results suggest that MFG-E8 requires EVs to transduce cellular signals from the basolateral side of the adhesion cells by accumulating in ECM.

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Post-weaning increases in the milk-fat globule EGF-factor VIII on fat globules in mouse milk and in the uptake of the fat globules by HC11 mammary epithelial cells

Cited by 7 publications

References 32 publications

MFG-E8: Origin, Structure, Expression, Functions and Regulation

MFG-E8: Origin, Structure, Expression, Functions and Regulation

Characterization and comparison of human and mouse milk cells

Extracellular vesicle‐mediated MFG‐E8 localization in the extracellular matrix is required for its integrin‐dependent function in mouse mammary epithelial cells

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