• Title/Summary/Keyword: Fat globule membrane protein

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Composition, Structure, and Bioactive Components in Milk Fat Globule Membrane

  • Ahn, Yu-Jin;Ganesan, Palanivel;Kwak, Hae-Soo
    • Food Science of Animal Resources
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    • v.31 no.1
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    • pp.1-8
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    • 2011
  • A unique biophysical membrane which surrounds the milk fat globules is called the milk fat globule membrane (MFGM). Various researches were studied about origin, composition, structure and bioactive components of MFGM. Bioactive protein components of MFGM play an important beneficiary function such as defense mechanism in new born. Among the bioactive lipid components from MFGM phospholipids showed health enhancing functions. The phospholipids also help in the production of certain dairy product from deterioration. MFGM phospholipids also showed antioxidant activity in some dairy products such as butter and ghee produced from milk of buffalo. Based on the beneficial effects, researchers developed MFGM as functional ingredients in various food products. This current review focuses on health enhancing function of MFGM and its components in various dairy products.

Composition of Lipids Associated with Dense Coat-enriched Fractions of Bovine Milk Fat Globule Membrane (우유 지방구막의 고밀도 표피에 결합된 지질의 조성)

  • Kwak, Hae-Soo;Chung, Choong-Il;Lee, Jae-Young
    • Korean Journal of Food Science and Technology
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    • v.21 no.5
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    • pp.726-734
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    • 1989
  • To analyze the components of dense coat fractions associated with fat globule membrane, The membrane was treated with various concentrations of Triton X-100, a non-ionic detergent, and the composition of lipids associated to the detergent insoluble material was analyzed. The amount of protein, phospholipid, cholesterol and ganglioside in milk fat globule membrane was reduced consistently with increasing concentrations of Triton X-100. Butyrophilin (band 12), xanthine oxidase (band 3) and band 16 as constituents of insoluble coat materials was revealed after electrophorisis on SDS-polyacrylamide gels. Phosphatidyl ethanolamine, phosphatidyl choline, phosphatidyl serine, phosphatidyl inositol and sphingomyelin were identified as the major phospholipids of the coat materials without selective concentration relative to the original membranes. Percentages of total phospholipid were not changed by any of the treatments. Fatty acids of total lipid were myristate, palmitate, stearate (major saturated acids), oleate and linoleate (major unsaturated acids). Cholesterol contents on a protein basis were slightly reduced with increasing concentrations of Triton X-100. Cholesterol adhered to protein more tightly than other constituents The contents of gangliosides was proportionally refuted with increasing concentration of Triton X-100.

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Biochemical Studies on the Sugar Chain Structure of Glycoproteins with the Same Protein Core of Bovine Milk Fat Globule Membrane (공통의 1차 구조를 가진 우유 지방구막 구성단백질의 당쇄 구조에 관한 생화학적 연구)

  • Seok, Jin-Seok
    • Journal of Dairy Science and Biotechnology
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    • v.21 no.2
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    • pp.138-147
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    • 2003
  • We here analyzed and proposed the structures of the N-linked sugar chains of PAS-7 from bovine milk fat globule membrane. The N-linked sugar chains were liberated from PAS-7 by hydrazinolysis and, after modifying the reducing ends with 2-aminopyridine (PA), were separated into one neutral (7N,55%) and two acidic (7M mono-, 43%; 7D, di-, 2%) sugar chain roups. The latter were converted into neutral groups (7MN and 7DN) by sialidase digestion. The structure of each of these PA-neutral sugar chains was determined by sugar analysis, sequential exoglycosidase digestion, partial acetolysis, and 1H-NMR spectroscopy. The results show that the 10 sugar chains were of the biantennary complex type with and without fucose. The structure of 7N2A one of the major sugar chains, was proposed as; [structure: see text] A structural comparison between PAS-6 and -7 indicated that although they shared the same protein core, their sugar moiety was markedly different, involving the existence of a different pathway during the post-transcriptional modification.

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Cloning and Expression of Lactadherin Gene from Korean Women (한국 여성의 Lactadherin 유전자 Cloning과 발현 연구)

  • Yom, Heng-Cherl
    • Development and Reproduction
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    • v.11 no.3
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    • pp.253-261
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    • 2007
  • Lactadherin is a glycoprotein of human milk fat globule membrane that binds to mucin and butyrophilin forming the protein complex. Especially, mucin and lactadherin in human milk efficiently protect infants with poor immune functions right after birth from infections by microorganisms and play important roles for their early survival, growth and development. Lactadherin inhibits the propagation and growth of rotavirus that is a global pathogen causing infants' diarrhea. Recently this protein was known to promote neovascularization and its deficiency related to develop Alzheimer's disease. In this study, the basic biochemical and physiological aspects of lactadherin were investigated. Messenger RNAs were isolated from mammary tissues from Korean women patients to clone a 1.2 kb cDNA and sequenced its DNA to determine its amino acid sequences. The cDNA was cloned to express its 43 kD protein in E. coli, which was confirmed by Western blot. The recombinant protein was purified and injected to 2 rabbits to raise antibodies against it. The semi-purified milk fat globule membrane proteins from Korean women was analyzed by Western blot using the rabbit antibody to give 70, 55, 46, 30 kD bands. Also several polymorphism and SNPs of lactadherin gene from Korean women were observed compared with those of Caucasian women.

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Preparation and Characterization of a Polar Milk Lipid-enriched Component from Whey Powder

  • Lee, Kwanhyoung;Kim, Ara;Hong, Ki-Bae;Suh, Hyung Joo;Jo, Kyungae
    • Food Science of Animal Resources
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    • v.40 no.2
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    • pp.209-220
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    • 2020
  • Milk fat globule membrane (MFGM) is a lipid carrier in mammals including humans that consists mainly of polar lipids, like phospholipids and glycolipids. In this study, a process to enrich polar lipids in commercial butter and whey powder, including polar lipids of MFGM, was developed. WPC (whey protein concentrate) 60 was selected as the most suitable raw material based on the yield, phospholipid, protein, and lactose content of the polar lipid fraction obtained by ethanol extraction of two WPC (WPC60 and WPC70) and two buttermilk (A and B). After fractionation under optimum conditions, the polar-lipid enriched fraction from WPC60 contained 38.56% phospholipids. The content of glycolipids, cerebroside, lactosylceramide, ganglioside GM3, ganglioside GD3, was 0.97%, 0.55%, 0.09%, and 0.14%, respectively. Rancimat results showed that the oxidation stability of fish oil increased with an increase in the polar-lipid fraction by more than 30 times. In addition, the secretion of IL-6 and TNF-α decreased in a concentration-dependent manner after treatment of RAW 264.7 cells with 0.1 to 100 ppm of the polar lipid fraction. In this study, polar lipid concentrates with antioxidant and anti-inflammatory activity, were prepared from milk processing by-products. The MFGM polar lipid concentrates made from by-products are not only additives for infants, but are also likely to be used as antioxidants in cooking oils and as active ingredients for functional foods.

Analysis of Sugar Chain Structure of PAS-7 Glycoprotein from Bovine Milk Fat Globule Membrane by US RAAM 2000 (OGS RAAM2000을 이용한 유지방구막 PAS-7 당단백질의 당쇄구조 해석)

  • 석진석
    • Food Science of Animal Resources
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    • v.21 no.4
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    • pp.367-373
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    • 2001
  • Glycoproteins PAS-6(50 kDa) and -7(47 kDa) from the bovine milk fat globule membrane share a common protein core but differ in their carbohydrate moiety. We have analyzed and proposed the structures of the N-linked sugar chains of PAS-7 by Oxford Glyco System(OGS) RAAM2000. The N-linked sugar chains were liberated from PAS-7 by hydrazinolysis and, after modifying the reducing ends with 2-aminobenzamide(2-AB), were separated into one neutral(7N, 55%) and two acidic(7M, mono-, 43%; 7D, di-, 2%) sugar chain groups. 7N was finally separated into 5 chains(a, b, c, d, and e), respectively. The structure of this 2AB-neutral sugar chain was determined by sugar analysis, exoglycosidase digestion with OGS glycosidase Kit and OGS RAAM2000 system. The results show that fraction e was the same of reported 7N1A, the biantennary complex type with a fucose on reducing end and two N-acetyllactosamine branch on non-reducing end. Therefore, it was proved that OGS RAAM2000 method is in conformity with conventional analysis of sugar chain structure from bovine PAS-7.

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Inductional Expression of the Human Lactadherin Gene in Mouse Mammary Epithelial Cells

  • Kwon, Mo-Sun;Koo, Bon-Chul;Kim, Teoan
    • Proceedings of the Korean Society of Embryo Transfer Conference
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    • 2002.11a
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    • pp.94-94
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    • 2002
  • Lactadherin (formerly known as BA46), a major glycoprotein of the human milk fat globule membrane, is abundant in human breast milk and breast carcinomas and may prevent symptomatic rotavirus infections. In this study, under the control of mouse whey acidic protein (WAP) promoter, the expression pattern of lactadherin (Ltd) in lactogenic hormone-dependent mouse mammary epithelial cell line HC11 were tested. pLNWLtd construct containing 2.4 kilobases of the WAP promoter and 1.5 kilobases of human lactadherin gene was stably transfered into HC11 cells using retroviral vector system. Integration and expression level of the transgene was estimated using PCR and RT-PCR, respectively. Prominent induction of Ltd gene under the WAS promoter was accomplished in the presence of insulin, hydrocortisone and prolactin, while induction with insulin alone resulted in lower expression. Our results demonstrate that the expression of the transgene is increased by synergistic effect of several lactogenic hormones, including insulin, hydrocortisone, and prolactin.

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Retrovirus Vector-Mediated Inductional Expression of the Human Lactadherin Gene in Mouse Mammary Epithelial Cells (Mouse Mammary Epithelial Cell에서 Retrovirus Vector를 이용한 Human Lactadherin 유전자의 유도적 발현)

  • 권모선;구본철;정병현;염행철;박창식;김태완
    • Korean Journal of Animal Reproduction
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    • v.27 no.1
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    • pp.15-23
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    • 2003
  • Lactadherin (formerly known as BA46), a major glycoprotein of the human milk fat globule membrane, is abundant in human breast milk and breast carcinomas and may prevent symptomatic rotavirus infections. In this study, under the control of tissue specific and hormonal inducible mouse whey acidic protein (WAP) promote., the expression pattern of lactadherin (Ltd) in lactogenic hormone-dependent mouse mammary epithelial cell line HC11 were tested. pLNWLtd construct containing 2.4 kilobases of the WAP promoter and 1.5 kilobases of human lactadherin gene was stably transfered into HC11 cells using retroviral vector system. Integration and expression level of the transgene was estimated using PCR and RT-PCR, respectively. Prominent induction of Ltd gene under the WAP promoter was accomplished in the presence of insulin, hydrocortisone and prolactin. Compared to the control (cells cultured with insulin alone), however we observed that the WAP promoter was leaky. These data indicate that luther studies are needed in finding an appropriate promoter other than WAP promoter because of its leakiness.