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1.
Br J Nutr ; 126(12): 1843-1851, 2021 12 28.
Article in English | MEDLINE | ID: mdl-33632354

ABSTRACT

Differences in individual eating habits may be influenced by genetic factors, in addition to cultural, social or environmental factors. Previous studies suggested that genetic variants within sweet taste receptor genes family were associated with sweet taste perception and the intake of sweet foods. The aim of this study was to conduct a genome-wide association study (GWAS) to find genetic variations that affect confection consumption in a Japanese population. We analysed GWAS data on confection consumption using 14 073 participants from the Japan Multi-Institutional Collaborative Cohort study. We used a semi-quantitative FFQ to estimate food intake that was validated previously. Association of the imputed variants with confection consumption was performed by linear regression analysis with adjustments for age, sex, total energy intake and principal component analysis components 1-3. Furthermore, the analysis was repeated adjusting for alcohol intake (g/d) in addition to the above-described variables. We found 418 SNP located in 12q24 that were associated with confection consumption. SNP with the ten lowest P-values were located on nine genes including at the BRAP, ACAD10 and aldehyde dehydrogenase 2 regions on 12q24.12-13. After adjustment for alcohol intake, no variant was associated with confections intake with genome-wide significance. In conclusion, we found a significant number of SNP located on 12q24 genes that were associated with confections intake before adjustment for alcohol intake. However, all of them lost statistical significance after adjustment for alcohol intake.


Subject(s)
Alcohol Drinking , Candy , Eating , Genome-Wide Association Study , Polymorphism, Single Nucleotide , Acyl-CoA Dehydrogenase/genetics , Alcohol Drinking/genetics , Cohort Studies , Eating/genetics , Humans , Japan/epidemiology
2.
Eur J Clin Nutr ; 75(3): 480-488, 2021 03.
Article in English | MEDLINE | ID: mdl-32895509

ABSTRACT

BACKGROUND/OBJECTIVE: Although benefits of fish consumption for health are well known, a significant percentage of individuals dislike eating fish. Fish consumption may be influenced by genetic factors in addition to environmental factors. We conducted a genome-wide association study (GWAS) to find genetic variations that affect fish consumption in a Japanese population. METHODS: We performed a two-stage GWAS on fish consumption using 13,739 discovery samples from the Japan Multi-Institutional Collaborative Cohort study, and 2845 replication samples from the other population. We used a semi-quantitative food frequency questionnaire to estimate food intake. Association of the imputed variants with fish consumption was analyzed by separate linear regression models per variant, with adjustments for age, sex, energy intake, principal component analysis components 1-10, and alcohol intake (g/day). We also performed conditional analysis. RESULTS: We found 27 single nucleotide polymorphisms (SNPs) located in 12q24 and 14q32.12 that were associated with fish consumption. The 19 SNPs were located at 11 genes including six lead SNPs at the BRAP, ACAD10, ALDH2, NAA25, and HECTD4 regions on 12q24.12-13, and CCDC197 region on 14q32.12. In replication samples, all five SNPs located on chromosome 12 were replicated successfully, but the one on chromosome 14 was not. Conditional analyses revealed that the five lead variants in chromosome 12 were in fact the same signal. CONCLUSION: We found that new SNPs in the 12q24 locus were related to fish intake in two Japanese populations. The associations between SNPs on chromosome 12 and fish intake were strongly confounded by drinking status.


Subject(s)
Genome-Wide Association Study , Polymorphism, Single Nucleotide , Acyl-CoA Dehydrogenase , Alcohol Drinking/genetics , Aldehyde Dehydrogenase, Mitochondrial/genetics , Cohort Studies , Genetic Predisposition to Disease , Humans , Japan
3.
Biomed Rep ; 10(3): 202-210, 2019 Mar.
Article in English | MEDLINE | ID: mdl-30906550

ABSTRACT

Few studies have investigated the association between dietary intake and blood concentrations of water-soluble vitamins in patients with ulcerative colitis (UC). In the present study, vitamin concentrations were measured in the blood and urinary excretion of 23 outpatients with UC and compared against a control group of 20 healthy participants. A weighed food record procedure was used to ensure controlled macronutrient and vitamin intakes of the UC cohort. Individuals in the control group were given a semi-purified diet for 8 days prior to assessment. Multiple linear regression analysis was used to identify important differences in vitamin concentrations, independent of sex, age and other confounding variables. The blood concentrations of vitamins B2, C, niacin and folate were markedly lower in the patients with UC than those in the control group, and the renal clearance of vitamins B1, B6, B12 and folate was notably higher in the UC cohort. It was concluded that vitamins B2, C, niacin and folate were at significantly lower concentrations in patients with UC following adjustment for coexisting factors. The lower levels of niacin may be partially due to impaired reabsorption. Chronic inflammation, common in patients with UC, with may contribute to the lower levels of other vitamins by rendering amino acid and carbohydrate metabolism into a hypermetabolic state. As the role of vitamins in metabolic activity is constant and pervasive, nutritional management including the application of water-soluble vitamins appears important for patients suffering from UC.

4.
Nutr Metab Insights ; 9: 85-92, 2016.
Article in English | MEDLINE | ID: mdl-27812289

ABSTRACT

We examined the concentrations of water-soluble vitamins in blood and urinary excretion of 22 patients with type 2 diabetes mellitus (type 2DM) and 20 healthy control participants. Macronutrient and vitamin intakes of type 2DM subjects were measured using a weighed food record method. Control participants consumed a semipurified diet for eight days. Multiple linear regression models were used to determine whether significant differences existed in vitamin concentrations in blood independent of age, sex, and other confounding factors. Concentrations of vitamins B2, B6, C, niacin, and folate in blood were significantly lower in type 2DM subjects than in controls, independent of confounding factors. Renal clearances of vitamins B6, C, niacin, and folate were significantly higher in type 2DM subjects than in controls. In conclusion, concentrations of vitamins B2, B6, C, niacin, and folate in blood were significantly lower in type 2DM subjects than in controls, independent of confounding factors; based on the evidence of increased urinary clearance of these vitamins, the lower levels were likely due to impaired reabsorption processes.

5.
J Agric Food Chem ; 56(19): 9200-5, 2008 Oct 08.
Article in English | MEDLINE | ID: mdl-18788814

ABSTRACT

The water extract of guar meal ( Cyamopsis tetragonolobus) was examined for its foamability. Compared with egg white, the extract showed an extraordinary foam stability: no drainage after 3 h of standing in contrast to 65% drainage for egg white at the same protein concentration. The acid-precipitated protein from the extract was responsible for the high foamability and designated guar foaming albumin (GFA). The foaming activity of GFA was 20 times higher than that of egg white. GFA consisted of two subunits with molecular masses of 6 and 11 kDa linked to each other through disulfide bonds. The cleavage of disulfide bonds in GFA affected the foamability only slightly. GFA remarkably decreased the surface tension of water at low protein concentrations. Immunoblotting analysis demonstrated that GFA did not react to the antisera from allergic patients against plant food. These results suggest that GFA serves as an effective food additive in developing protein-stabilized foam.


Subject(s)
Cyamopsis/chemistry , Plant Extracts/chemistry , Plant Proteins/chemistry , Chemical Phenomena , Chemical Precipitation , Food Additives , Hydrogen-Ion Concentration , Ovalbumin/chemistry
6.
Cells Tissues Organs ; 183(1): 41-52, 2006.
Article in English | MEDLINE | ID: mdl-16974094

ABSTRACT

The extracellular matrix surrounding avian oocytes, referred to as the perivitelline membrane (PL), exhibits a three-dimensional network of fibrils between granulosa cells and the oocyte. We previously reported that one of its components, ZPC, is synthesized in granulosa cells that are specifically incorporated into the PL; this incorporation might be mediated by a specific interaction with ZPB1, another PL constituent, which is synthesized in the liver. In order to extend our previous findings, we established an expression system for quail ZPB1 using a mammalian cell line, and several ZPB1 mutants lacking the zona pellucida (ZP) domain or the glutamine-rich repeat region were produced. Western blot analysis of the immunoprecipitated materials with anti-ZPC antiserum indicated that ZPB1 was coimmunoprecipitated with the antiserum in the presence of ZPC. Ligand blotting also revealed the specific binding of ZPC and ZPB1 and indicated that the binding of these two components might be mediated via an ionic interaction. An analysis using recombinant ZPB1 demonstrated that the ZPB1 lacking the ZP domain did not bind to ZPC, whereas the mutant missing the glutamine-rich repeat region retained its capacity for binding. Furthermore, although the ZPB1 lacking the N-terminal half of the ZP domain was able to bind to ZPC, the deletion of the C-terminal half completely abolished ZPB1 binding to ZPC. These results suggested that the C-terminal half of the ZP domain of ZPB1 contains a binding site for ZPC, and that it appears to be involved in insoluble PL fibril formation in the quail ovary.


Subject(s)
Avian Proteins/metabolism , Coturnix/metabolism , Egg Proteins/metabolism , Granulosa Cells/metabolism , Membrane Glycoproteins/metabolism , Zona Pellucida/metabolism , Animals , Avian Proteins/chemistry , Avian Proteins/genetics , Binding Sites , Blotting, Western , CHO Cells , Cells, Cultured , Coturnix/genetics , Cricetinae , Cricetulus , Egg Proteins/chemistry , Egg Proteins/genetics , Electrophoresis, Polyacrylamide Gel , Female , Granulosa Cells/cytology , Hydrogen-Ion Concentration , Immunoprecipitation , Membrane Glycoproteins/chemistry , Membrane Glycoproteins/genetics , Molecular Weight , Osmolar Concentration , Plasmids/genetics , Protein Binding , Transfection
7.
Neurosci Res ; 56(2): 224-8, 2006 Oct.
Article in English | MEDLINE | ID: mdl-16899318

ABSTRACT

Magnetic resonance (MR) imaging using super-paramagnetic iron oxides (SPIOs) is a powerful tool to monitor transplanted cells in living animals. Since, however, SPIOs are negative contrast agents, positive agents have been explored. In this study, we examined the feasibility of FITC-labeled poly-L-lysine-CF3 (PLK-CF3) using glial cells. FITC-labeled PLK-CF3 was easily internalized by neuroblastoma cells and glia as adding it into culture medium. No toxicity was seen at the concentration of less than 80 microg/ml. MR images positively detected labeled cells transplanted in the brain of living mouse. The results indicate that FITC-labeled PLK-CF3 is a useful positive contrast agent for MR tracking.


Subject(s)
Cell Transplantation/methods , Magnetic Resonance Imaging , Neuroglia/transplantation , Polylysine/metabolism , Animals , Cells, Cultured , Contrast Media , Ferrosoferric Oxide/metabolism , Male , Mice , Mice, Inbred ICR , Neuroglia/physiology , Rats
8.
Biosci Biotechnol Biochem ; 70(1): 144-51, 2006 Jan.
Article in English | MEDLINE | ID: mdl-16428832

ABSTRACT

We have recently established the monoclonal antibodies (mAbs) specific to the major food allergen, ovomucoid, as mAb 7D, recognizing the carbohydrate moiety of ovomucoid, and mAb 6H, the peptide moiety (Biosci. Biothechnol. Biochem., 68, 2490-2497, (2004)). Using these mAbs, we found commercially available ovalbumin preparations contaminated with a considerable amount of ovomucoid together with other glycoproteins. To examine the contaminants, egg white was subjected to cation-exchange chromatography. An unidentified protein was found in egg white that reacted with mAb 7D but not with mAb 6H, having a molecular size of about 52 kDa and a blocked N-terminus. Two internal amino acid sequences of the fragments obtained after a lysyl endopeptidase and a hydroxylamine treatment revealed the protein to be ovalbumin Y (ovalbumin-related gene Y protein). We conclude that ovalbumin Y is a unique chimeric glycoprotein having an amino acid sequence similar to that of ovalbumin, but having a carbohydrate moiety similar to that of ovomucoid.


Subject(s)
Avian Proteins/chemistry , Avian Proteins/metabolism , Carbohydrates/chemistry , Ovalbumin/chemistry , Ovomucin/chemistry , Ovomucin/metabolism , Amino Acid Sequence , Animals , Antibodies, Monoclonal/immunology , Chickens , Chromatography, Ion Exchange , Conserved Sequence , Enzyme-Linked Immunosorbent Assay , Hydroxylamine , Molecular Sequence Data , Molecular Weight , Ovomucin/immunology , Sequence Alignment
9.
Int J Syst Evol Microbiol ; 53(Pt 1): 253-258, 2003 Jan.
Article in English | MEDLINE | ID: mdl-12656181

ABSTRACT

A strain (KREDT) that formed endospores and produced the pigment prodigiosin was isolated from activated sludge. The presence of spores in cells of strain KREDT was evident upon electron microscopy examination, heat treatment and the detection of dipicolinic acid in the cells. Biochemical characteristics, and 16S rDNA sequence and DNA-DNA homology data identified strain KREDT as Serratia marcescens. The major respiratory quinone of strain KREDT was found to be ubiquinone Q-8. The formation of endospores by Gram-negative bacteria has not been observed previously, and has never been reported in any species of Serratia. Here, it is shown that strain KREDT (JCM 11315T = CIP 107489T) represents a novel subspecies of S. marcescens, for which the name Serratia marcescens subsp. sakuensis is proposed.


Subject(s)
Serratia marcescens/classification , Serratia marcescens/isolation & purification , Sewage/microbiology , DNA, Bacterial/genetics , DNA, Ribosomal/genetics , Drug Resistance, Bacterial , Fatty Acids/analysis , Hot Temperature , Japan , Microscopy, Electron , Molecular Sequence Data , Phylogeny , Pigments, Biological/analysis , Quinones/analysis , RNA, Bacterial/genetics , RNA, Ribosomal, 16S/genetics , Serratia marcescens/genetics , Serratia marcescens/physiology , Spores, Bacterial/isolation & purification
10.
Eur J Biochem ; 269(8): 2223-31, 2002 Apr.
Article in English | MEDLINE | ID: mdl-11985601

ABSTRACT

In avian species, an egg envelope homologous to the mammalian zona pellucida is called the perivitelline membrane. We have previously reported that one of its components, a glycoprotein homologous to mammalian ZPC, is synthesized in the granulosa cells of the quail ovary. In the present study, we investigated the proteolytic cleavage of the newly synthesized ZPC and the secretion of ZPC from the granulosa cells. Western blot analysis of the cell lysates demonstrated that the 43-kDa protein is the precursor of mature ZPC (proZPC), and is converted to the 35-kDa protein before secretion. The accumulation of proZPC in the presence of brefeldin A, and conversion of proZPC to ZPC in the presence of monensin, indicate the possibility that the proteolytic processing of ZPC occurs in the Golgi apparatus. An analysis of amino-acid sequence identified that the C terminus of mature ZPC protein is Phe360, and the N-terminal amino-acid sequence of the proZPC-derived fragment was determined as Asp363. These results suggest that newly synthesized ZPC is cleaved at the consensus furin cleavage site, and the resulting two basic residues at the C terminus are subsequently trimmed off to generate mature ZPC prior to secretion.


Subject(s)
Coturnix/physiology , Egg Proteins/metabolism , Granulosa Cells/metabolism , Membrane Glycoproteins/metabolism , Protein Processing, Post-Translational , Receptors, Cell Surface , Animals , Brefeldin A/pharmacology , Female , Granulosa Cells/physiology , Molecular Sequence Data , Monensin/pharmacology , Protein Synthesis Inhibitors/pharmacology , Zona Pellucida Glycoproteins
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