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K Torii

Publications and source records attributed to K Torii.

At least 109 records · Page 6Linked to original sources

Effect of water restriction on the development of hypothalamic lesions in weanling rodents given MSG. I. Drinking behaviour and physiological parameters in mice (Mus musculus).

Deprivation of water overnight (ON: 19.00-09.00 h) induced approx. 20% haemoconcentration in weanling ICR strain mice and resulted in avid consumption of fluid offered for 30 min subsequently, with delayed restoration of serum osmolality and sodium to normal levels in those offered 8% w/v monosodium L-glutamate monohydrate (MSG) aqueous solution. Neuronal necrosis of the arcuate nucleus of the hypothalamus was found in 12/180 dehydrated mice deprived ON and subsequently consuming 3.0 g or more MSG/kg body weight offered hypertonic MSG solution as the sole source of drinking water. The lesions were less severe than in mice given MSG s.c. or by forced intubation. Mice deprived ON and subsequently consuming MSG solution with water in a free choice experiment, and those deprived during daytime (DT: 07.00-21.00 h) and subsequently consuming MSG solution, with or without water, developed fewer and less severe lesions than did mice deprived ON and subsequently consuming MSG solution solely. The provision of other nutrients (e.g. glucose, arginine) reduced glutamate-induced hypothalamic lesions and elevation of plasma L-glutamate. The findings are in accord with earlier observations that hypothalamic lesions do not result even in this most susceptible species from the 'voluntary' consumption of MSG by physiologically normal animals. No lesions were produced even in mice deprived of food and water ON and subsequently consuming up to 7.3 g MSG/kg body weight in diet and in soup.

Animals↗

Effect of water restriction on the development of hypothalamic lesions in weanling rodents given MSG. II. Drinking behaviour and physiological parameters in rats (Rattus norvegicus) and golden hamsters (Mesocricetus auratus).

No hypothalamic lesions were found in weanling Sprague-Dawley (SD) rats or in golden hamsters deprived of water and/or food overnight (ON 19.00-09.00 h) and offered monosodium L-glutamate monohydrate (MSG) in up to 10% solution for 30 min subsequently. ON restriction of water resulted in haemoconcentration, with elevation of haematocrit, plasma protein, electrolytes and osmolality in SD rats. Water-restricted rats avidly consumed large volumes of concentrated MSG solution and showed further evidence of haemoconcentration, with delayed restoration of plasma sodium and with high plasma glutamate, but did not develop lesions at up to 5.4 g MSG/kg b.w. Hamsters deprived of water ON consumed smaller volumes of MSG in aqueous solution than did SD rats, and in them no hypothalamic lesions were observed. That SD rats and golden hamsters, which are susceptible to hypothalamic lesions from the parenteral administration of high doses of MSG, did not develop lesions following the voluntary intake of MSG in aqueous solution, even under conditions of severe thirst, is further evidence of the safety of MSG as a food ingredient.

Animals↗

Pyroglutamate kinetics and neurotoxicity studies in mice.

Plasma and brain kinetics of L-glutamic (GA) and L-pyroglutamic (PY) acids were studied after oral administration of monosodium glutamate (MSG) or pyroglutamate to adult mice. Oral MSG (0.5 g/kg) increased plasma GA and PY levels 4.5 and 1.8 times, respectively. A small increase in brain PY (1.3 times the basal level) but not in brain GA, was observed. Oral administration of pyroglutamate (0.5 g/kg) increased plasma PY levels 56 times in adult mice and 69 times in infant mice. No lesions in the arcuate nucleus of the hypothalamus were observed when pyroglutamate was administered orally to infant mice at doses of 2 and 4 g/kg.

Animals↗

Drinking behavior and the development of hypothalamic lesions from aspartame ingestion in water-restricted weanling mice.

Wealing mice that had been deprived overnight of water, or of water and diet, were offered a solution containing L-aspartyl-L-phenylalanine-methylester (APM) or monosodium L-aspartate monohydrate (MSA) as the sole source of drinking water, and/or a diet containing large amounts of APM and/or MSA for 30 min, and were killed subsequently. Only those animals exposed to concentrated (6.64% W/V) MSA solutions developed neuronal lesions in the hypothalamic arcuate nuclei. Those offered MSA in the diet only, or APM either in the diet and/or in solution, failed to develop such lesions. Apparently water-restricted weanling mice lose their ability to regulate subsequent drinking behavior, and consume hyperosmolar MSA or APM solutions whose osmolarity or sweetness would be aversive to humans. Such animals are unsuitable for the safety evaluation of APM.

Animals↗

Biochemical studies of taste sensation. IX. Enhancement of L-[3H]glutamate binding to bovine taste papillae by 5'-ribonucleotides.

The interaction of the taste substance monosodium L-glutamate with taste receptors has been investigated. Binding of L-[3H]glutamate was measured to preparations of bovine circumvallate (taste) papillae (type I preparation) and to control tongue epithelial preparations (type II preparation) devoid of taste receptors. Binding is operationally defined using a membrane filtration assay. Substantially greater binding occurred to the type I preparation than to the type II preparation, and the binding to the type I preparation showed evidence of saturation. The apparent Kd of L-glutamate was estimated to be in the range of 20--30 mM. The unique taste effect of L-glutamate was considered to depend importantly on its demonstrated synergism in combination with certain 5'-ribonucleotides. A several-fold enhancement of binding of L-[3H]glutamate occurred in the presence of certain 5'-ribonucleotides. 5'-GMP, 5'-IMP and 5'-UMP each increased the binding of L-[3H]glutamate, while 5'-XMP, 5'-AMP and 5'-CMP did not. None of these nucleotides affected the lower level of binding to the type II preparation. Neither the free bases, adenine and guanine, their nucleosides nor their di- or triphosphonucleotides were effective in increasing L-[3H]glutamate binding to the type I preparation. The nucleotide specificity of the glutamate binding enhancement therefore shows a marked similarity with the nucleotide specificity in evoking the synergistic taste effect in humans.

Animals↗

Studies on the binding of adenylyl-3', 5'-cytidine to ribonuclease.

The interaction of adenylyl-3',5'-cytidine (ApC) with ribonuclease-A (RNAase-A) was studied by steady-state kinetics and ultraviolet difference spectroscopy. X-ray difference Fourier synthesis at 4 A resolution was also used to study the binding of ApC to RNAase-S. Unlike well-studied compounds like uridylyl-3',5'-adenosine, ApC binds in an unique way: (1) the cytidine moiety is bound to the B1 and R1 sites, (2) the adenosine moiety protrudes to the solution and is not fixed spatially and (3) the phosphate group is bound to the non-specific site (the "Po site") previously postulated (Sawada, F. and Irie, M. (1969) J. Biochem. (Tokyo) 66, 415--418) as the binding site for the 5'-phosphate of uridine 2',5'-diphosphate or uridine 3',5'-diphosphate. This conclusion is consistent with that derived for adenylyl-3',5' -4-thiouridine based on CD difference spectroscopy (White, M.D., Keren-Zur, M. and Lapidot, Y. (1977) Nucleic Acid Res. 4, 843--851). The "Po site" is most likely the epsilon-amino group of Lys 66.

Adenine Nucleotides↗

Relationship between polyamine contents and protease activity in the rat submaxillary gland.

The effect of polyamines on the protease activity in the submaxillary gland of castrated rats has been investigated in vivo. The protease activity, which is increased by testosterone, is also increased to a lesser degree by the subcutaneous administration of spermidine. The administration of putrescine was less effective than that of spermidine. The increase of polyamine contents in the submaxillary gland of the castrated rats administered either testosterone or spermidine was nearly parallel to the increase of the enzymatic activity. The administration of methylglyoxal bis(guanylhydrazone), a potent inhibitor of spermidine synthesis, with testosterone inhibited slightly the increase of the protease activity by testosterone, while the administration of the inhibitor with spermidine had essentially no effect on the increase of the enzymatic activity by spermidine. The administration of testosteorne also caused a slight increase of S-adenosyl-L-menthionine decarboxylase activity. These results suggest that spermidine synthesis may be necessary for the stimulation by testosterone of protease synthesis in the rat submaxillary gland.

Adenosylmethionine Decarboxylase↗

Crystal structure of monoclinic ribonuclease-S at 4 A resolution. The mode of binding of 4-thiouridylic acid and a fragment of folic acid, p-aminobenzoylglutamic acid.

A four-A electron density map was calculated for the monoclinic crystal of ribonuclease-S (RNase-S) based on two heavy-atom derivatives. Close geometrical similarity was found between the two crystallographically independent RNase-S molecules (called molecules ZA and ZB) in this crystal and that (called molecule Y) in the trigonal crystal. Using the rotational and translational parameters relating these three molecules, it was established that the crystallographic two-fold symmetry between the two molecules ZA in the monoclinic crystal was exactly identical to that between the two molecules Y in the trigonal crystal, suggesting the tendency of RNase-S molecules to associate in this way although the interaction is weak. The 4-A difference Fourier maps calculated for the monoclinic crystal established the following conclusions. (1) 4-Thiouridine-2'(3')-monophosphates binds to the B1 and R1 sites like other pyrimidine nucleoside-2'(3')-monophosphates as expected from previous spectrophotometric studies, but not to the B2 site even at the concentration of 20 mM. An attempt to visualize the photoproduct generated by irradiation of near-ultraviolet light in this complex failed. (2) p-Aminobenzoylglutamic acid, a fragment of folic acid, seems to bind to RNase-S with its benzene ring close to the B2 site and the alpha-carboxylate group close to the p1 site. The model is compatible with most of the chemical results obtained by Sawada et al. ((1977) Biochim. Biophys. Acta 479, 188-197).

4-Aminobenzoic Acid↗