Search PubMed⌕ Search

Biomedical subjects

M Majima

Publications and source records attributed to M Majima.

At least 127 records · Page 7Linked to original sources

Loss of the activity of human coagulation factor XII by a chymotrypsin-like protease activated in rat mast cells during degranulation with compound 48/80.

Mediator release from mast cells is an initial step in the immediate-type hypersensitivity. Thus, the interaction of neutral proteases released from mast cells with plasma kallikrein-kinin system was investigated. Two proteases, chymotrypsin-like (CHY) and trypsin-like (TRY) proteases, were activated in purified rat mast cells after degranulation with compound 48/80. Three fourths of the CHY activity remained in the cell residue, and the activity was inhibited by chymostatin, whereas most of the TRY activity was released in the medium and was inhibited by leupeptin. The incubation of rat or human plasma with degranulated mast cell (DMC) suspension did not cause the activation of plasma prekallikrein, but did cause a loss in the activity of coagulation factor XII, as ascertained by the lack of activation of prekallikrein in either the DMC-treated plasma by glass powder or in the incubation of DMC-treated human plasma with factor XII deficient plasma activated by kaolin. The prekallikrein and high-molecular-weight kininogen levels were sufficient for activation of factor XII.

Animals↗

[Pathological characteristics of the thyroid gland in patients with triiodothyronine-predominant Graves' disease].

Pathology of the thyroid gland tissue was characterized in patients with Triiodothyronine (T3)-predominant Graves' disease who had normal levels of serum T4 but increased levels of serum T3 during antithyroid drug therapy. In order to compare this group of patients with an usual type of Graves' patients, age, sex, dietary intake of iodide, duration of antithyroid therapy and the dose of thionamide drugs were matched between the two groups of patients. Thyroid tissue was obtained from subtotal thyroidectomy. In examining the histology of the thyroid gland, integration eye piece plate II with regularly arranged 100 lattice points was set on eye lens of a microscope. The number of crossing points which were projected on each 4 histological elements was counted in randomly selected 10 fields of vision in each patient's thyroid. Assuming that the every histological element is arranged in a random manner, errors of each visual field by this method would be less than 12%. In consequence, the significant difference was demonstrated in the weight of subtotally resected thyroid and the ratio of each histological element except interstitial tissue occupied in the total thyroid tissue between T3-predominant Graves' disease and control Graves' disease. The volume composition of the epithelial cells and vacuoles in patients with T3-predominant Graves' disease was significantly greater than that of patients with control Graves' disease (24.7 +/- 10.6 vs 14.4 +/- 6.5%, 5.9 +/- 3.9 vs 2.0 +/- 1.0%, Mean +/- SD, respectively, p less than 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)

Graves Disease↗

Demonstration of chondroitin sulfates degrading endo-beta-glucuronidase activity in rabbit liver.

Reduced chondroitin sulfate was incubated with rabbit liver extracts followed by reduction once more with sodium [3H]borohydride, and then passed through a Sephadex G-100 column. Chondroitin sulfate obtained from the incubation medium at pH 4 was only slightly depolymerized and was highly radioactive. Paper chromatographic analyses showed that glucuronic acid residues became exposed at the reducing terminal of chondroitin sulfate after incubation with the liver extracts. These results suggest that endo-beta-glucuronidase activity which degrades chondroitin sulfate is present in the rabbit liver.

Animals↗

Serum ferritin as a marker of thyroid hormone action on peripheral tissues.

Serum ferritin measurements were evaluated as a marker of thyroid hormone action on peripheral tissues. Mean serum ferritin concentrations were not significantly different in euthyroid, thyrotoxic, and hypothyroid subjects due to a wide spread in ferritin levels among individuals. Intraindividual changes in serum ferritin, however, occurred with changing thyroid function. All 18 patients with thyrotoxic Graves' disease had a decrease in serum ferritin levels when they became euthyroid during antithyroid drug therapy. Furthermore, a significant intraindividual correlation between serum levels of ferritin and T4 or T3 was found in 2 patients with thyrotoxic Graves' disease in whom levels were measured serially throughout the course of therapy. Similarly, serum ferritin levels increased in all 12 hypothyroid patients with Hashimoto's disease when euthyroidism was achieved with L-T4 therapy. Administration of 75 micrograms T3 daily for 1 week to 11 euthyroid subjects resulted in a 23-243% (mean +/- SD, 117 +/- 70%) increase in serum ferritin above basal values. In contrast, in 3 patients with thyroid hormone resistance, the same treatment produced rises in serum ferritin concentrations of only 2%, 5%, and 15%. Our data suggest that alterations in thyroid status in a given individual produce changes in serum ferritin levels. Measurement of this protein before and after T3 therapy may prove useful in the diagnosis of thyroid hormone resistance.

Adult↗

Urinary glycosaminoglycans bearing glucuronic acid or iduronic acid residue at the reducing terminals.

The urinary glycosaminoglycan was reduced with NaB[3H]4, and was separated into three fractions according to molecular size by column chromatography on Sephadex G-200. The hexuronic acid residues at the reducing terminals of each fraction were quantified by the method of preferential quantitation of hexuronic acid at the reducing terminals. This method consisted of hydrolysis with trifluoroacetic acid and nitrous acid, lactonization, and paper chromatographic analysis. Both radioactive gulonolactone and idonolactone were detected in the fractions with a lower molecular size, but not in those with a higher molecular size. These observations demonstrated that the glucuronide and iduronide linkages at other-than-terminal sites of carbohydrate chains were cleaved by the processes of depolymerization of glycosaminoglycans in tissues. Therefore, it is highly likely that endo-beta-glucuronidase(s) and endo-alpha-iduronidase(s) which belong to the glycosidase of endo type such as hyaluronidase are involved in the catabolic degradation of glycosaminoglycans in tissues.

Carbohydrate Sequence↗

Improved analytical method for the hexuronic acids at the reducing terminals of glycosaminoglycans.

When endo-uronidases act on glycosaminoglycans, the reaction products have hexuronic acid residues at the reducing terminals. An analytical method for hexuronic acids at the reducing terminals was devised for hyaluronate oligosaccharides having hexuronic acid residues at the reducing terminals. The procedure is as follows: Hexuronic acid residues at the reducing terminals of hyaluronate oligosaccharides were tritiated with reduction using NaB[3H]4 and the products were hydrolyzed with trifluoroacetic acid and nitrous acid. As a result, the tritiated and reduced hexuronic acid residues, that is aldonic acids, were liberated from the reducing terminals. After passing them through anion and cation ion-exchange resins, the aldonic acids were lactonized. The lactones were developed on paper chromatography, and their radioactivities determined on the paper. The method is also useful for discrimination between glucuronic acid and iduronic acid at the reducing terminals of glycosaminoglycans.

Chromatography, Paper↗

The application of the Milner-Avigad method for the quantitative determination of endouronidase activities.

The Milner-Avigad method (Milner, Y. and Avigad, G. (1967) Carbohydr. Res. 4, 359-361) has been shown to have high specificity for measuring the reducing powers of free hexuronic acids; its applicability in the quantitative determination of endouronidase activity was the purpose of this investigation. Among the constituent monosaccharides of glycosaminoglycans, hexuronic acids showed high color yield by this method, while xylose, galactose and N-acetylhexosamine recorded negligible color yield. Among the monosaccharide residues at the reducing terminals of oligosaccharides, only hexuronic acids exhibited color yield. However, the color yield was less than that of free hexuronic acids. Gel filtration chromatography of reaction products revealed that the cleavage of the oligosaccharide chains and the resultant exposure of new reducing terminals were not caused by the reaction procedures involved in this method. These data indicate that the Milner-Avigad method is useful for determining the presence of hexuronic acid residues preferentially at reducing terminals of glycosaminoglycan moieties. Thus, it supported the conclusion that the Milner-Avigad method is applicable for the quantitative determination of endouronidase activity using glycosaminoglycan as a substrate.

Animals↗

Some properties of synthetic fucopyranosylserines and -threonines.

alpha Fuc-Ser, alpha Fuc-Thr, beta Fuc-Ser, and beta Fuc-Thr were synthesized stereoselectively in good yields, and their properties were investigated. beta-Fucosylserine (and -threonine) was synthesized by Koenigs-Knorr reaction of per-O-acetylfucopyranosyl bromide with N-carbobenzoxy-L-serine (and -threonine) benzyl ester using mercuric cyanide, followed by hydrogenolysis and deacetylation. alpha-Fucosylserine (and -threonine) was synthesized by the halide-ion catalyzed reaction of per-O-benzylfucopyranosyl bromide with the serine (and threonine) derivative described above, followed by hydrogenolysis. These substances each gave a single peak on an amino acid analyzer. The anomeric configurations of these compounds were determined by 1H-NMR spectroscopy, optical rotation measurement and enzymatic degradations of these compounds. On acid hydrolysis, alpha Fuc-Ser and alpha Fuc-Thr were more rapidly hydrolyzed than the corresponding beta-series compounds. Under mild alkaline conditions in the presence of sodium borohydride, per-protected beta Fuc-Thr released about 50% of fucose but free beta Fuc-Thr did not However, free alpha Fuc-Thr and beta Fuc-Thr were cleaved to give acetylated fucose during acetylation with acetic anhydride-pyridine. alpha-L-Fucosidases, which were purified from abalone and rabbit livers by affinity chromatography, acted very well on alpha Fuc-Ser and alpha Fuc-Thr, but not on the beta-series compounds.

Fucose↗

Enzymic determination of urinary free L-fucose.

Conditions necessary for the precise measurement of free L-fucose in urine by an enzymic method using L-fucose dehydrogenase have been studied. The normal urinary levels of L-fucose were 16.4 /+- 9.1 micrograms/ml in children (22.2 /+- 6.5 micrograms/mg of creatinine) and 17.7 /+- 8.5 micrograms/ml in adults (16.6 /+- 5.7 micrograms/mg of creatinine). There was a close correlation between the concentration of free L-fucose and that of creatinine. A close correlation was also found between the concentration of free L-fucose and alpha-L-fucosidase activity. Thus, it was suggested that the free L-fucose in urine reflected the metabolism of L-fucose or L-fucose-containing glycoconjugates. In a preliminary screening test, several urine samples which showed high concentrations of free L-fucose, namely cases of "fucosuria" were found.

Adult↗