Biomedical subjects

Makoto Hattori

Publications and source records attributed to Makoto Hattori.

At least 19 recordsLinked to original sources

PubMed2007

Distinctly different sensitivity in the induction and reversal of anergy of Th1 and Th2 cells.

T cell anergy is one of the mechanisms of immunological tolerance. We examined in this study the distinct responses of Th1 and Th2 cells to in vitro anergic stimulation using Th1 and Th2 cells from two strains of T cell receptor transgenic mice. Proliferation of the Th2 cells was difficult to suppress by anergic stimulation, while that of Th1 cells was significantly inhibited even by weak stimulation. However, IL-4 production by Th2 cells was definitely reduced by anergic stimulation, although the inhibition level of IL-4 was lower than that of IFN-gamma production by Th1 cells. We also examined the reversal of anergy in both subsets. While both the anergized Th1 and Th2 cells responded to IL-2 stimulation, only the anergy of the Th2 cells could be reversed. This result indicates that progression of the cell cycle was not sufficient for anergy reversal in Th1 cells. Our findings indicate that the induction and reversal of T cell anergy might be affected by the distinct signaling features of Th1 and Th2 cells.

Animals↗

PubMed2006

Regulatory effect of amino acids on the pasting behavior of potato starch is attributable to its binding to the starch chain.

The binding of an amino acid, glycine (Gly), alanine (Ala), epsilon-aminocaproic acid (-AC), monosodium glutamate (GluNa), or lysine (Lys), to starch was examined by a biomolecular interaction analyzer (IAsys). A starch sample (ATS) hydrolyzed to an extent of 1% hydrolysis rate with 15% sulfuric acid was used as a model starch for the binding examination. The reducing end of ATS was oxidized by the Somogyi reagent, and the conversion of the reducing end to the carboxyl group of ATS was confirmed by a carboxylic acid fluorescence labeling reagent. The oxidized ATS was immobilized to the amino group of a sensor cuvette by using water-soluble carbodiimide and N-hydroxysuccinimide through an amide bond. The IAsys examination showed that Gly, Ala, and epsilon-AC scarcely bound to the immobilized starch chains but that GluNa and Lys favorably bound with their increasing concentrations. The relative binding index (RBI) of each amino acid was defined by the ratio of the slope of the linear regression equation between the binding response and the concentration for each amino acid to that for Gly. Because the relationships between the RBI and the pasting characteristics (pasting temperature, peak viscosity, breakdown, and swelling index) could each be expressed by a linear regression equation with a high correlation coefficient, it is concluded that the regulation of the pasting behavior of starch with an amino acid is caused by binding of the amino acid to the starch chains.

Amino Acids↗

PubMed2006

Oral administration of alginic acid oligosaccharide suppresses IgE production and inhibits the induction of oral tolerance.

We have found that alginic acid oligosaccharide (ALGO) enhanced Th1 by promoting IL-12 production, suggesting that ALGO can be applied as an anti-allergic food. In this study we examined both positive and negative functions of ALGO. First we investigated the anti-allergic activity of ALGO, as a positive function, when orally administered. IgE production was significantly inhibited in mice fed ALGO as compared to control mice. This result indicates that ALGO had anti-allergic activity even when orally administered. On the other hand, we also found a negative function of ALGO. Oral co-administration of a protein antigen and ALGO inhibited the induction of oral tolerance to the protein. These data indicate the potential of ALGO as an anti-allergic food material and the necessity of further examination to determine a safe method application.

Administration, Oral↗

PubMed2006

Reduced immunogenicity of beta-lactoglobulin by conjugating with chitosan.

Bovine beta-lactoglobulin (beta-LG) was conjugated with chitosan (CHS) by means of a water-soluble carbodiimide to reduce the immunogenicity of beta-LG. Each beta-LG-CHS conjugate was purified by ion-exchange chromatography and hydrophobic chromatography. The conjugation between beta-LG and CHS was confirmed by SDS-PAGE, the isoelectric point of the conjugate being higher than that of beta-LG. Two types of the beta-LG-CHS conjugate were obtained with molar ratios of beta-LG to CHS of 1:1 (F1) and 1:2 (F2). Structural analyses by fluorescence measurement, ELISA with monoclonal antibodies and retinol-binding activity indicated that the conjugates had almost maintained the native structure of beta-LG. The antigenicity of the beta-LG-CHS conjugates was similar to that of beta-LG in C3H/He mice. Reduction of the immunogenicity of beta-LG was achieved by conjugation with CHS. In particular, F2 showed very low immunogenicity. B cell epitopes of beta-LG and the conjugates recognized in C3H/He mice were determined with 15-mer multi-pin peptide; the linear epitope profiles of the conjugates were found to be similar to those of beta-LG, while the antibody response to each epitope was dramatically reduced. Conjugation of beta-LG with chitosan was effective for reducing the immunogenicity of beta-LG.

Animals↗

PubMed2006

Effect of sorbed water on the thermal stability of soybean protein.

A soybean protein isolate (SPI), and its beta-conglycinin and glycinin componets were obtained from defatted soybean flour by applying dissolution and precipitation based on the difference in their solubility depending on each isoelectric point. The purity evaluated by SDS-PAGE of the beta-conglycinin and glycinin preparations was about 84% and 80%, respectively, resulting in a clear difference in the pH dependence on solubility. A BET plot derived from the water sorption isotherm at 25 degrees C showed that the amount of the monolayer adsorption of these preparations was about 6-9%, the value for the beta-conglycinin preparation being about 1.5 times higher than that for the glycinin preparation. The beta-conglycinin and glycinin preparations were respectively denatured at around 75 degrees C and 86 degrees C in the presence of excess water, whereas the denaturation temperature of both preparations was markedly increased by decreasing sorbed water content below 40%, corresponding well with the unfrozen water content.

Adsorption↗

PubMed2006

Oral administration of IL-12 abrogates the induction but not the maintenance of oral tolerance.

BACKGROUND: IL-12 is a Th1-inducing cytokine and known to be induced by some food factors. This function of such foods is expected to be applied for antiallergic materials. However, the influence of IL-12 on the immune responses has not been fully investigated. Oral tolerance is an immunologically unresponsive state induced by orally administered food antigens. Although a failure in the induction of oral tolerance would result in food allergy, the mechanisms for the induction and abrogation of oral tolerance have not been clarified. IL-12 induced by food factors may also affect the induction of oral tolerance. In this study we examined the effect of the oral administration of IL-12 on the induction and maintenance of oral tolerance. METHODS: BALB/c mice were fed beta-lactoglobulin with or without IL-12. After immunizing them with the antigen, the serum antibody titer of these mice was measured to evaluate the induction of oral tolerance. RESULTS: The induction of oral tolerance was prevented in the mice that had been simultaneously fed the antigen and IL-12. On the other hand IL-12 did not abrogate the already established oral tolerance when it was administered after feeding the antigen. We also found that oral tolerance could be induced normally in mice that had failed to induce such tolerance by simultaneous feeding of IL-12 and the antigen. CONCLUSIONS: The results indicate that IL-12 induced in the intestine by some food factors is involved in the regulation of oral tolerance.

Administration, Oral↗

PubMed2006

Development of a multi-Fourier-transform interferometer: fundamentals.

We describe the development of an instrument that uses a Martin-Puplett-type Fourier-transform spectrometer to apply an aperture synthesis technique to millimeter and submillimeter waves. We call this instrument a multi-Fourier-transform interferometer (MuFT). The MuFT performs wideband imaging, spectroscopy, and polarimetry, at millimeter and submillimeter wavelengths. We describe the fundamentals of the MuFT and give an example of one potential implementation. A full description of the observables with a MuFT is provided. A physical explanation of the observability of complex visibility by the MuFT is given. Fundamental restrictions on observations with the MuFT, e.g., limits on spectral and spatial resolution and on fields of view, are discussed. The advantages of the MuFT are summarized.

Journal Article↗

PubMed2006

Mulberry latex rich in antidiabetic sugar-mimic alkaloids forces dieting on caterpillars.

Since ancient times, mulberry leaves (Morus spp.) have been used to rear the silkworm Bombyx mori. Because the silkworm grows well on mulberry leaves, the toxicities and defensive activities of these leaves against herbivorous insects have been overlooked. Here we show that mulberry leaves are highly toxic to caterpillars other than the silkworm B. mori, because of the ingredients of the latex, a milky sap exuded from mulberry leaf veins. The toxicity of mulberry leaves was lost when the latex was eliminated from the leaves, and artificial diets containing latex showed toxicity. Mulberry latex contained very high concentrations of alkaloidal sugar-mimic glycosidase inhibitors reported to have antidiabetic activities, such as 1,4-dideoxy-1,4-imino-D-arabinitol, 1-deoxynojirimycin, and 1,4-dideoxy-1,4-imino-D-ribitol. The overall concentrations of these inhibitors in latex reached 1.5-2.5% (8-18% dry weight) in several mulberry varieties, which were approximately 100 times the concentrations previously reported from whole mulberry leaves. These sugar-mimic alkaloids were toxic to caterpillars but not to the silkworm B. mori, indicating that the silkworm can circumvent the mulberry tree's defense. Our results suggest that latex ingredients play key roles in defense of this tree and of other plants against insect herbivory, and they imply that plant latexes are treasuries of bioactive substances useful as medicines and pesticides.

1-Deoxynojirimycin↗

PubMed2006

Interfacial behavior of fatty-acylated sericin prepared by lipase-catalyzed solid-phase synthesis.

Fatty-acylated sericin {1:0.7 molar ratio of sericin (Mr 18,700) to oleic acid} was prepared by lipase-catalyzed solid-phase synthesis in n-hexane containing oleic acid to endow sericin with interfacial properties. Acylation with oleic acid was confirmed by 1H-NMR. The fatty-acylated sericin exhibited superior emulsifying activity index and emulsion stability in the presence of 0-0.5 M NaCl, in a temperature range of 30-80 degrees C and pH range of 2-7, as compared with the control sericin. The fatty-acylated sericin (1:0.4 molar ratio) prepared by using low-molecular-weight sericin (Mr 5,000) also exhibited superior emulsifying properties. The affinity of the fatty-acylated sericin to a hydrophobic surface as evaluated by a biomolecular interaction analyzer was about twice as much as that of the control sericin. The fatty-acylated sericin showed retarded water vaporization, similar to the control sericin, indicating good retention of moistness, and was adsorbed four times as much to defatted wool with little desorption as compared with the control sericin.

Acylation↗

PubMed2006

Contribution of the net charge to the regulatory effects of amino acids and epsilon-poly(L-lysine) on the gelatinization behavior of potato starch granules.

The effects of lysine (Lys), monosodium glutamate (GluNa), glycine, alanine and epsilon-poly(L-lysine) (PL) with different degrees of polymerization on the gelatinization behavior of potato starch granules were investigated by DSC, viscosity and swelling measurements, microscopic observation, and measurement of the retained amino acid amount to clarify the contribution of the net charge to their regulatory effects on the gelatinization behavior. The amino acids and PL each contributed to an increase in the gelatinization temperature, and a decrease in the peak viscosity and swelling. These effects strongly depended on the absolute value of their net charge. The disappearance of a negative or positive net charge by adjusting the pH value weakened the contribution. The swelling index and size of the potato starch granules changed according to replacement of the swelling medium. The amino acids and PL were easily retained by the swollen potato starch granules according to replacement of the outer solution of the starch granules.

Amino Acids↗

PubMed2006

Improved physical and biochemical features of a collagen membrane by conjugating with soluble egg shell membrane protein.

Soluble egg shell membrane protein (SEP) prepared from the egg shell membrane by performic acid oxidation and pepsin digestion was applied to prepare a membrane conjugated with pepsin-solubilized collagen (PSC) by cross-linking with water-soluble carbodiimide. SEP enabled a conjugated membrane to be constructed with a well-developed network structure having thicker collagen fibrils and higher stability than the PSC membrane alone, as indicated by reduced solubility and collagenase-digestion, increased denaturation temperature, and superior flexibility. The SEP-PSC membrane (SEP:PSC of 1:1, w/w) had lower sweatiness than the PSC membrane. Fibroblasts and keratinocytes adhered to the SEP-PSC-coated wells (SEP:PSC of 1:10, w/w) as a fundamental model of an artificial skin similar to that to the PSC-coated wells due to similar expression level of several cell-adhesion proteins. An SEP-PSC coating accelerated the cell growth of fibroblasts, whereas the cell growth of keratinocytes did not change, or decreased slightly due to more rapid differentiation indicated by a more substantial expression of differentiation marker proteins than a PSC-coating without SEP.

Animals↗

PubMed2005

Interaction of porphyran with a hydrophobic surface and stabilization of liposomes.

Three porphyran preparations with high emulsifying ability and varying molecular mass, 3,6-anhydrogalactose content, and sulfate content without any protenaceous component were prepared from dried nori processed from Porphyra yezoensis, a red alga. Each of these preparations was applied to demonstrate adsorption or binding to the surface of oil droplets. The decrease in porphyran concentration of the aqueous phase of O/W emulsions prepared with porphyran and with toluidine blue (TB)-porphyran complex formed by adding TB to the O/W emulsions indicated ready adsorption to the surface of oil droplets. The decrease in zeta-potential of the O/W emulsions suggested that the sulfate groups of the adsorbed porphyran were oriented toward the external aqueous phase. A biomolecular interaction analysis exhibited rapid binding of porphyran to C16-alkane, probably through 3,6-anhydrogalactose. Porphyran-coated liposomes were tolerant to digestion with phospholipase D. The increased molecular weight of the porphyran preparations had an increased effect on these characteristics. The results of this study demonstrate that the emulsifying ability of porphyran is derived from the adequate adsorption to the surface of oil droplets and that porphyran could be effectively applied to stabilize liposomes.

Adsorption↗

PubMed2005

Laccase-type phenoloxidase in salivary glands and watery saliva of the green rice leafhopper, Nephotettix cincticeps.

The activity and composition of leafhopper saliva are important in interactions with the host rice plant, and it may play a physiological role in detoxifying toxic plant substances or ingesting sap. We have characterized diphenoloxidase in the salivary glands of Nephotettix cincticeps, its activity as a laccase, and its presence in the watery saliva with the objective of understanding its function in feeding on rice plants. Nonreducing SDS-PAGE of salivary gland homogenates with staining by the typical laccase substrate 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), hydroquinone or syringaldazine revealed a band at a molecular mass of approximately 85 kDa at pH 5. A band also appeared at a molecular mass of approximately 200 kDa when the gels were treated with dopamine, L-3,4-dihydroxyphenylalanine (DOPA) or catechol at pH 7. The ABTS-oxidizing activity of the homogenates was drastically inhibited by N-hydroxyglycine, a specific inhibitor of laccase. However, the dopamine-oxidizing activity was not inhibited by N-hydroxyglycine, while it was inhibited by phenylthiourea (PTU). Thus, the salivary glands of N. cincticeps contain two types of phenoloxidases: a laccase (85 kDa) and a phenoloxidase (200 kDa). Laccase activity was detected in a holidic sucrose diet that was fed on for 16 h by two females, but only a trace of catechol oxidase activity was observed, suggesting that the laccase-type phenoloxidase was the predominant phenoloxidase secreted in watery saliva. The laccase exhibited an optimum pH of 4.75-5 in McIlvaine buffer and had a PI of 4.8. Enzyme activity was histochemically localized in V cells of the posterior lobe of the salivary glands. It remained at the same level throughout the adult stage from 2 days after eclosion. A possible function of N. cincticeps salivary laccase may be rapid oxidization of potentially toxic monolignols to nontoxic polymers during feeding on the rice plant. This is the first report proving that laccase occurs in the salivary glands of Hemiptera species and is secreted in the watery saliva.

Animals↗

PubMed2005

Complete refolding of bovine beta-lactoglobulin requires disulfide bond formation under strict conditions.

beta-Lactoglobulin (beta-LG) denatured with 6 M guanidine hydrochloride (GdnHCl) containing a reducing agent and subsequently dialysed against phosphate-buffered saline (PBS) resulted in incomplete refolding of this protein despite the fact that the biological activity for retinol-binding was recovered to almost the same degree as that of the native molecule [Hattori, M., Ametani, A., Katakura, Y., Shimizu, M., Kaminogawa, S. J., Biol. Chem. 268 (1993) 22414-22419]. The enzyme probe method, evaluation of hydrophilicity values, in-gel mobility on SDS-PAGE, and evaluation of disulfide bonds with the Ellman method showed exposure of the hydrophobic region(s) and incorrect disulfide bond formation in such dialyzed beta-LG molecules. We reveal in this present work that complete refolding could be attained by diluting denatured beta-LG with PBS containing a reducing agent, before slow reoxidation of the sulfhydryl groups upon dialysis for gradient removal of the reducing agent in 6 steps. Complete renaturation was confirmed by analyzing the retinol-binding activity, CD spectra, intrinsic fluorescence, binding ability of monoclonal antibodies (mAbs), and SDS-PAGE. Step-by-step disulfide bond formation was considered to be critical for the complete refolding of denatured beta-LG. Our method can contribute to establish a procedure for complete refolding of useful recombinant proteins in vitro without such biological aids as chaperones.

Animals↗

PubMed2005

Reduced T cell response to beta-lactoglobulin by conjugation with acidic oligosaccharides.

We have previously reported that the conjugation of beta-lactoglobulin (beta-LG) with alginic acid oligosaccharide (ALGO) and phosphoryl oligosaccharides reduced the immunogenicity of beta-LG. In addition, those conjugates showed higher thermal stability and improved emulsifying properties than those of native beta-LG. We examine in this study the effect of conjugation on the T cell response. Our results demonstrate that the T cell response was reduced when mice were immunized with the conjugates. The findings obtained from an experiment using overlapping synthetic peptides show that novel epitopes were not generated by conjugation. One of the mechanisms for the reduced T cell response to the conjugates was found to be the reduced susceptibility of the conjugates to processing enzymes for antigen presentation. We further clarify that the beta-LG-ALGO conjugate modulated the immune response to Th1 dominance. We consider that this property of the beta-LG-ALGO conjugate would be effective for preventing food allergy as well as by its reduced immunogenicity. Our observations indicate that the method used in this study could be applied to various protein allergens to achieve reduced allergenicity with multiple improvements in their properties.

Alginates↗

PubMed2005

Prevention of intestinal infection by glycomacropeptide.

The preventive effects of glycomacropeptide (GMP) against intestinal infection were investigated, and conjugates of GMP with xylooligosaccharide (XOS) and carboxymethyldextran (CMD) were prepared by the Maillard reaction to enhance the effect of GMP. The binding ability of GMP to intestinal pathogenic bacteria was evaluated by a binding assay with biotinylated bacteria. GMP showed the ability to bind to Salmonella enteritidis and enterohemorrhagic Escherichia coli O157:H7 (EHEC O157). This binding ability was decreased by a sialidase treatment and completely eliminated by periodate oxidation. These results indicate that such carbohydrate moieties as sialic acid in GMP are involved in binding to S. enteritidis and EHEC O157. The preventive effect of GMP on the adhesion of pathogenic bacteria to Caco-2 cells was also investigated. GMP showed an inhibitory effect on the adhesion of EHEC O157 in a dose-dependent manner, although it was not a potent inhibitor of the adhesion of Salmonella infection. However, in the case of Salmonella infection, GMP-XOS and GMP-CMD significantly suppressed IL-8 production which was the index of infection. Our results indicate GMP to be a promising agent for preventing intestinal infection.

Anti-Bacterial Agents↗

PubMed2004

Improvement of the functional properties of sucrose stearate by phosphorylation.

Phosphorylated sucrose stearate (SE-P) was prepared by dry-heating sucrose stearate (SE) with metaphosphoric acid. The main product was deduced to be a monophosphosucrose monostearate by chemical analysis and mass spectrometry. SE-P exhibited remarkably higher solubility and emulsifying properties than SE, especially in the acidic region and in the presence of NaCl, and SE-P bound Ca2+ at a 1:1 molar ratio (SE-P/Ca2+). SE-P markedly reduced the viscosity of potato starch paste and inhibited retrogradation, whereas SE did not reduce it so much. It is thus expected that phosphorylation would be an appropriate method for improving the functional properties of SE and that SE-P could be used as a novel emulsifier and modifier with Ca2+-binding ability for starchy foods.

Calcium↗

PubMed2004

Glycopeptide derived from hen egg ovomucin has the ability to bind enterohemorrhagic Escherichia coli O157:H7.

Ovomucin glycopeptide (OGP) was prepared by size exclusion chromatography after Pronase digestion of hen egg ovomucin, and the binding of OGP to foodborne pathogens (Bacillus cereus,Clostridium perfringens, Escherichia coli O157:H7, Listeria monocytogenes, Salmonella enteritidis, Salmonella typhimurium, and Staphylococcus aureus) was investigaed. Binding assays with biotinylated bacteria as probes in microtiter plates showed that OGP bound to only E. coli O157:H7 among these foodborne pathogens. Periodate treatment markedly reduced the binding ability, indicating that E. coli O157:H7 bound to carbohydrate moieties of OGP. Lectin blot analysis with Maackia amurensis (MAA) and Sambucus nigra (SNA), which are specific for oligosaccharides containing sialic acid, revealed their binding sites in OGP were similar to the E. coli O157:H7 binding sites that were probed with biotinylated E. coli O157:H7 after Western blotting of OGP. Sialydase treatment of OGP abolished its ability to bind E. coli O157:H7, demonstrating that sialic acid played an important role in the binding. These results suggest that OGP has E. coli O157:H7-specific binding sites that consist of sialic acid. On the basis of these properties, OGP has the potential to be an ingredient with a protective effect against E. coli O157:H7 infection and to be a novel probe for the detection of E. coli O157:H7 in the food hygiene field.

Animals↗