scholarly journals Characterization of an apically derived epithelial membrane glycoprotein from bovine milk, which is expressed in capillary endothelia in diverse tissues.

1985 ◽  
Vol 100 (2) ◽  
pp. 397-408 ◽  
Author(s):  
D E Greenwalt ◽  
I H Mather
Keyword(s):  
Endothelial Cells ◽  
Epithelial Cells ◽  
Milk Fat ◽  
Bovine Milk ◽  
Mammary Tissue ◽  
Specific Marker ◽  
Total Carbohydrate ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

A glycoprotein (PAS IV) of apparent Mr 76,000 was purified from bovine milk-fat-globule membrane and partially characterized. PAS IV contained mannose, galactose, and sialic acid as principal sugars (approximately 5.3% total carbohydrate [wt/wt]) and existed in milk in at least four isoelectric variants. The glycoprotein appeared to be an integral membrane protein by several criteria. PAS IV was recovered in the detergent phase of Triton X-114 extracts of milk-fat-globule membrane at room temperature. When bound to membrane, PAS IV was resistant to digestion by a number of proteinases, although after solubilization with non-ionic detergents, the protein was readily degraded. Amino acid analysis of the purified protein revealed a high percentage of amino acids with nonpolar residues. The location of PAS IV was determined in bovine tissues by using immunofluorescence techniques. In mammary tissue, PAS IV was located on both the apical surfaces of secretory epithelial cells and endothelial cells of capillaries. This glycoprotein was also detected in endothelial cells of heart, liver, spleen, pancreas, salivary gland, and small intestine. In addition to mammary epithelial cells, PAS IV was also located in certain other epithelial cells, most notably the bronchiolar epithelial cells of lung. The potential usefulness of this protein as a specific marker of capillary endothelial cells in certain tissues is discussed.

scholarly journals Specific antibodies to PAS IV, a glycoprotein of bovine milk-fat-globule membrane, bind to a similar protein in cardiac endothelial cells and epithelial cells of lung bronchioles

1985 ◽  
Vol 228 (1) ◽  
pp. 233-240 ◽  
Author(s):  
D E Greenwalt ◽  
V G Johnson ◽  
I H Mather
Keyword(s):  
Endothelial Cells ◽  
Epithelial Cells ◽  
Milk Fat ◽  
Periodic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bovine Milk ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

We recently described the tissue distribution of PAS IV (periodic acid/Schiff-positive Band IV), a hydrophobic glycoprotein isolated from bovine milk-fat-globule membrane [Greenwalt & Mather (1985) J. Cell Biol. 100, 397-408]. By using immunofluorescence techniques, PAS IV was detected in mammary epithelial cells, the bronchiolar epithelium of lung, and the capillary endothelium of several tissues, including heart, salivary gland, pancreas, spleen and intestine. In the present paper we describe the specificity of the antibodies used for these studies. Two monoclonal antibodies, E-1 and E-3, were shown by solid-phase immunoassay and immunoaffinity chromatography to be specific for PAS IV (of Mr 76000) in milk-fat-globule membrane and recognize a glycoprotein of slightly higher Mr (85000) in heart. Affinity-purified rabbit antibodies to PAS IV were also shown to recognize components of Mr 76000 and 85000 in fat-globule membrane and heart respectively, by using immunoblotting procedures after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Additionally, an immunoreactive protein in lung of Mr 85000 was detected. Despite these differences in molecular size, the fat-globule membrane and heart forms of PAS IV were shown to be very similar by peptide-mapping techniques. The possible significance of the expression of similar forms of PAS IV in both epithelial and capillary endothelial cells is briefly discussed.

scholarly journals Bovine milk-fat-globule membrane contains an enzymically inactive form of acetyl-CoA carboxylase

1989 ◽  
Vol 257 (3) ◽  
pp. 925-927 ◽  
Author(s):  
B J Shriver ◽  
J B Allred ◽  
C R Roman-Lopez
Keyword(s):  
Milk Fat ◽  
Bovine Milk ◽  
Mammary Tissue ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Milk Fat Globule Membrane ◽  
Inactive Form ◽  
Mitochondrial Fractions ◽  
Milk Fat Globule ◽  
Fat Globule

Enzymically inactive acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] was found as a component of bovine milk-fat-globule membrane (MFGM). Acetyl-CoA carboxylase was present in MFGM at a higher concentration than in cytosolic or mitochondrial fractions of bovine mammary tissue, which makes it unlikely that its presence was due to simple contamination by these subcellular constituents.

Production and characterization of monoclonal antibodies directed against bovine milk fat globule membrane (MFGM)

1994 ◽  
Vol 1199 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Naohito Aoki ◽  
Hidenori Kuroda ◽  
Miho Urabe ◽  
Yoshimi Taniguchi ◽  
Takahiro Adachi ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Milk Fat ◽  
Bovine Milk ◽  
Milk Fat Globule Membrane ◽  
Milk Fat Globule ◽  
Fat Globule

Chemical changes in bovine milk fat globule membrane caused by heat treatment and homogenization of whole milk

2002 ◽  
Vol 69 (4) ◽  
pp. 555-567 ◽  
Author(s):  
SUNG JE LEE ◽  
JOHN W. SHERBON
Keyword(s):  
Heat Treatment ◽  
Membrane Proteins ◽  
Milk Fat ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Chemical Changes ◽  
Milk Fat Globule Membrane ◽  
Whole Milk ◽  
Milk Fat Globule ◽  
Fat Globule

The effects of heat treatment and homogenization of whole milk on chemical changes in the milk fat globule membrane (MFGM) were investigated. Heating at 80 °C for 3–18 min caused an incorporation of whey proteins, especially β-lactoglobulin (β-lg), into MFGM, thus increasing the protein content of the membrane and decreasing the lipid. SDS-PAGE showed that membrane glycoproteins, such as PAS-6 and PAS-7, had disappeared or were weakly stained in the gel due to heating of the milk. Heating also decreased free sulphydryl (SH) groups in the MFGM and increased disulphide (SS) groups, suggesting that incorporation of β-lg might be due to association with membrane proteins via disulphide bonds. In contrast, homogenization caused an adsorption of caseins to the MFGM but no binding of whey proteins to the MFGM without heating. Binding of caseins and whey proteins and loss of membrane proteins were not significantly different between milk samples that were homogenized before and after heating. Viscosity of whole milk was increased when milk was treated with both homogenization and heating.

scholarly journals Safety and Tolerance Evaluation of Milk Fat Globule Membrane-Enriched Infant Formulas: A Randomized Controlled Multicenter Non-Inferiority Trial in Healthy Term Infants

2014 ◽  
Vol 8 ◽  
pp. CMPed.S16962 ◽  
Author(s):  
Claude Billeaud ◽  
Giuseppe Puccio ◽  
Elie Saliba ◽  
Bernard Guillois ◽  
Carole Vaysse ◽  
...  
Keyword(s):  
Weight Gain ◽  
Milk Fat ◽  
Bovine Milk ◽  
Control Group ◽  
Infant Formulas ◽  
Term Infants ◽  
Milk Fat Globule Membrane ◽  
Standard Formula ◽  
Milk Fat Globule ◽  
Fat Globule

Objective This multicenter non-inferiority study evaluated the safety of infant formulas enriched with bovine milk fat globule membrane (MFGM) fractions. Methods Healthy, full-term infants ( n = 119) age ≤14 days were randomized to standard infant formula (control), standard formula enriched with a lipid-rich MFGM fraction (MFGM-L), or standard formula enriched with a protein-rich MFGM fraction (MFGM-P). Primary outcome was mean weight gain per day from enrollment to age 4 months (non-inferiority margin: –3.0 g/day). Secondary (length, head circumference, tolerability, morbidity, adverse events) and exploratory (phospholipids, metabolic markers, immune markers) outcomes were also evaluated. Results Weight gain was non-inferior in the MFGM-L and MFGM-P groups compared with the control group. Among secondary and exploratory outcomes, few between-group differences were observed. Formula tolerance rates were high (>94%) in all groups. Adverse event and morbidity rates were similar across groups except for a higher rate of eczema in the MFGM-P group (13.9% vs control [3.5%], MFGM-L [1.4%]). Conclusion Both MFGM-enriched formulas met the primary safety endpoint of non-inferiority in weight gain and were generally well tolerated, although a higher rate of eczema was observed in the MFGM-P group.

Sign in / Sign up

Export Citation Format

Share Document