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- 1. 魚油と海洋由来オメガ3脂肪酸 fish oil and marine omega 3 fatty acids
- 2. 食物アレルゲンの分子機能 molecular features of food allergens
- 3. Biomarkers of cardiac injury other than troponin
- 4. 非甲状腺疾患における甲状腺機能 thyroid function in nonthyroidal illness
- 5. インスリン様成長因子Iの生理学 physiology of insulin like growth factor 1
- Effect of limited enzymatic hydrolysis on linoleic acid binding properties of β-lactoglobulin.
- Sponton OE, Perez AA, Carrara C, Santiago LG.Author information Grupo de Biocoloides, Instituto de Tecnología de Alimentos, Universidad Nacional del Litoral, 1 de Mayo 3250 (3000), Santa Fe, Argentina.Abstractβ-Lactoglobulin (BLG) is a member of lipocalin family, proteins with ability to bind small hydrophobic ligands, such as retinol, vitamins and fatty acids. Moreover, BLG is susceptible to protease action producing a wide range of polypeptides depending on the hydrolysis degree (HD). In the present work, the effect of limited enzymatic hydrolysis on fatty acid binding properties of BLG was studied. Linoleic acid (LA) was used as a model fatty acid. Limited enzymatic hydrolysis was performed using α-chymotrypsin immobilised on agarose microparticles. BLG hydrolysates were produced at HD: 1%, 3% and 5%. In order to determine the influence of HD on BLG molecular weight SDS-PAGE was used. BLG structural modification and LA binding properties were monitored by means of fluorescence spectroscopic techniques. The increase in HD produced: (i) a BLG degradation and a molecular weight distribution of BLG hydrolysates and (ii) an increased exposition of buried hydrophobic residues, however it was observed a decrease in surface hydrophobicity possibly due to a deterioration of hydrophobic protein domains. It was observed that enzymatic hydrolysis treatment produced a decrease in BLG ability for binding LA. It was concluded that limited enzymatic hydrolysis could deteriorate the specific site on BLG structure necessary for binding LA.
- Food chemistry.Food Chem.2014 Mar 1;146:577-82. doi: 10.1016/j.foodchem.2013.09.089. Epub 2013 Sep 25.
- β-Lactoglobulin (BLG) is a member of lipocalin family, proteins with ability to bind small hydrophobic ligands, such as retinol, vitamins and fatty acids. Moreover, BLG is susceptible to protease action producing a wide range of polypeptides depending on the hydrolysis degree (HD). In the present w
- PMID 24176383
- Loss of NDG-4 extends lifespan and stress resistance in Caenorhabditis elegans.
- Brejning J, Nørgaard S, Schøler L, Morthorst TH, Jakobsen H, Lithgow GJ, Jensen LT, Olsen A.Author information Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, Aarhus, 8000-DK, Denmark.AbstractNDG-4 is a predicted transmembrane acyltransferase protein that acts in the distribution of lipophilic factors. Consequently, ndg-4 mutants lay eggs with a pale appearance due to lack of yolk, and they are resistant to sterility caused by dietary supplementation with the long-chain omega-6 polyunsaturated fatty acid dihommogamma-linolenic acid (DGLA). Two other proteins, NRF-5 and NRF-6, a homolog of a mammalian secreted lipid binding protein and a NDG-4 homolog, respectively, have previously been shown to function in the same lipid transport pathway. Here, we report that mutation of the NDG-4 protein results in increased organismal stress resistance and lifespan. When NDG-4 function and insulin/IGF-1 signaling are reduced simultaneously, maximum lifespan is increased almost fivefold. Thus, longevity conferred by mutation of ndg-4 is partially overlapping with insulin signaling. The nuclear hormone receptor NHR-80 (HNF4 homolog) is required for longevity in germline less animals. We find that NHR-80 is also required for longevity of ndg-4 mutants. Moreover, we find that nrf-5 and nrf-6 mutants also have extended lifespan and increased stress resistance, suggesting that altered lipid transport and metabolism play key roles in determining lifespan.
- Aging cell.Aging Cell.2014 Feb;13(1):156-64. doi: 10.1111/acel.12165. Epub 2013 Nov 28.
- NDG-4 is a predicted transmembrane acyltransferase protein that acts in the distribution of lipophilic factors. Consequently, ndg-4 mutants lay eggs with a pale appearance due to lack of yolk, and they are resistant to sterility caused by dietary supplementation with the long-chain omega-6 polyunsat
- PMID 24286221
- Role of mammalian sirtuin 1 (SIRT1) in lipids metabolism and cell proliferation of goose primary hepatocytes.
- Han C, Wan H, Ma S, Liu D, He F, Wang J, Pan Z, Liu H, Li L, He H, Xu H, Wei S, Xu F.Author information Institute of Animal Breeding & Genetic, Sichuan Agricultural University, Chengdu, Sichuan 611130, PR China. Electronic address: firstname.lastname@example.org.AbstractOur result showed in the fatty liver formation induced-by overfeeding goose, it was accompanied by an activation of mammalian target of rapamycin (mTOR) pathway and cell proliferation. Recent studies have suggested a crucial role for mammalian sirtuin 1 (SIRT1) in regulating lipid metabolism and cell proliferation, so we hypothesize that resveratrol -activated and nicotinamide -inhibited SIRT1 acts goose hepatocellular lipid metabolism and cell proliferation by mTOR signal pathway. Here we show that both resveratrol and nicotinamide could evidently affect the DNA synthesis rate, the lipids accumulation, the mRNA level and protein content of genes involved in the lipids metabolism, mTOR signal pathway, and the cell cycle progression of goose primary hepatocytes. Moreover, rapamycin decreased the effect of nicotinamide on lipids accumulation and cell proliferation. These findings suggest that SIRT1 functions as a regulator for mTOR signaling and plays an essential role in the regulation of hepatocyte lipid metabolism and cell proliferation.
- Molecular and cellular endocrinology.Mol Cell Endocrinol.2014 Jan 25;382(1):282-91. doi: 10.1016/j.mce.2013.10.012. Epub 2013 Oct 19.
- Our result showed in the fatty liver formation induced-by overfeeding goose, it was accompanied by an activation of mammalian target of rapamycin (mTOR) pathway and cell proliferation. Recent studies have suggested a crucial role for mammalian sirtuin 1 (SIRT1) in regulating lipid metabolism and cel
- PMID 24145124
- 夢はバラ色 戦略的創造研究推進事業(ERATO) : 村田脂質活性構造プロジェクト
- 村田 道雄,佐藤 文憲
- 生産と技術 65(3), 110-113, 2013
- NAID 40019765799
- 前川 素子,島本 知英
- 生化學 84(10), 862-866, 2012-10-25
- NAID 10031122395
- 高度不飽和脂肪酸および脂肪酸結合タンパク質の神経新生に対する役割 (特集 生物機能における脂質の重要性)
- 大隅 典子
- オレオサイエンス 11(10), 359-363, 2011-10
- NAID 40019008946
- 1. Curr Opin Clin Nutr Metab Care. 2014 Mar;17(2):124-9. doi: 10.1097/MCO.0000000000000031. Fatty acid binding proteins: tissue-specific functions in health and disease. Thumser AE(1), Moore JB, Plant NJ. Author ...
- 1. Clin Chim Acta. 2005 Feb;352(1-2):15-35. Fatty acid-binding proteins as plasma markers of tissue injury. Pelsers MM(1), Hermens WT, Glatz JF. Author information: (1)Department of Molecular Genetics ...