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Biomedical subjects

M Endo

Publications and source records attributed to M Endo.

At least 1,063 records · Page 59Linked to original sources
PubMed1980

The two survival cases of alpha-pattern coma caused by large amounts of hypnotica and neuroleptica.

The EEGs of two men (42 and 63 years old) in coma who took large amounts of hypnotica and neuroleptica for intended suicides were occupied by an alpha pattern, and the patients were diagnosed as alpha-pattern coma. The prominent pattern in their EEGs changed from an alpha pattern to a theta pattern, and subsequently into an alpha pattern of low amplitude. The patients recovered without any residual neurological symptoms. It has been confirmed by our two cases, as well as by other reported cases, that the outcome of the alpha-pattern coma caused by drug poisoning is favorable. It is concluded that a longitudinal EEG recording should be performed as early as possible when the patient is in a comatose state.

Adult↗
PubMed1980

Mucocutaneous lymph node syndrome. Successful aortocoronary bypass homograft in a four-year-old boy.

Mucocutaneous lymph node syndrome has been reported in more than 7,000 cases in Japan and other countries, and 1 to 2 percent of the patients died suddenly. This syndrome accompanied by coronary arterial aneurysm and thrombosis has been noted in postmortem examinations. The usual age is 1 to 1.5 years, and surgical subjects also include babies and infants. We report the findings in a four-year-old boy with this syndrome who was subjected to successful aortocoronary bypass grafting using his mother's fresh vein for homografting.

Child↗
PubMed1980

Heterogeneity of human urinary glycosaminoglycans.

Crude urinary glycosaminoglycans (GAG) obtained from normal adult men were fractionated by ethanol-fractionation, followed by Dowex 1 column chromatography. The resulting acidic subfractions were qualitatively analyzed for monosaccharide composition and examined by electrophoresis on cellulose acetate membrane and paper chromatography before and after mucopolysaccharidase digestions. Some of the major subfractions were also examined by gel filtration and infrared spectral analysis. The result showed that urinary GAG were extremely heterogeneous in the molecular size, negative charge and the chemical composition. Hyaluronic acid, heparan sulfate, chondroitin sulfates A and C, chondroitin, dermatan sulfate and keratan sulfate were found in wide distribution in these acidic subfractions. Of these GAG, chondroitin sulfate isomers were distributed into almost all acidic subfractions, indicating to be the most heterogeneous.

Adult↗
PubMed1980

Fractionation with ethanol of human urinary glycosaminoglycans.

Crude glycosaminoglycans (GAG) separated from normal human urine by cetylpyridinium chloride-precipitation were fractionated with ethanol. The resulting fractions were then examined by electrophoresis on cellulose acetate membranes before and after enzymatic digestions and nitrous acid treatment. Analytical data for these fractions and the electrophoretograms suggested that ethanol-fractionation was useful to separate roughly chondroitin sulfate A, C-type GAG and heparan sulfate in human urine.

Chondroitin Sulfates↗
PubMed1980

Glycoconjugates (glycosaminoglycans and glycoproteins) and glycogen in the human cervix uteri.

Glycoconjugates and glycogen obtained from the cervix uteri of nonpregnant women of proliferative phase and secretory phase, and from the postpartum cervix uteri were determined by electrophoresis on cellulose acetate membrane and chemical analysis before and after enzymatic digestion and nitrous acid treatment. Although the contents of neutral glycopeptide fraction in these tissues were similar, the glycogen content in the postpartum tissue greatly decreased. The contents in terms of hexosamine of hyaluronic acid, chondroitin sulfate, heparan sulfate and acidic glycopeptides in the postpartum tissue greatly increased in comparison with those in the nonpregnant tissues, whereas that of dermatan sulfate slightly decreased. In addition, dermatan sulfate in the postpartum tissue contained a small portion of non-sulfate disaccharide units, which was not detected in the nonpregnant tissues. The results indicate that significant changes in the contents of glycoconjugates and glycogen of human cervix uteri occur in ripening. The roles of these substances in the cervical ripening are discussed.

Cell Division↗
PubMed1980

Polydispersity of glycosaminoglycans in normal human urine.

To elucidate precise nature of urinary glycosaminoglycans (GAG) GAG in the acidic subfractions obtained in a previous paper (Endo et al. 1980) were quantitated by digestion with mucopolysaccharidases, nitrous acid treatment and by quantitative cellulose acetate membrane (Separax) electrophoresis. Hyaluronic acid, chondroitin sulfates and chondroitin, dermatan sulfate and dermatan, heparan sulfate, keratan sulfate, and acidic glycopeptide were found in wide distribution in these subfractions. The results suggested the presence of various degree of the depolymerization products of each GAG and of wide range of the desulfation products of each sulfated GAG. Distribution map of each GAG in the subfractions showed more detailed polydispersity of GAG in normal human urine than that reported previously.

Adult↗
PubMed1980

Chemical nature of human urinary glycosaminoglycans.

To elucidate precise chemical nature of urinary glycosaminoglycans (GAG), GAG in the seven major acidic subfractions in a previous paper (Endo et al. 1980a) were analyzed for the chemical compositions and studied on the linkage between carbohydrate and peptide. All the subfractions examined contained galactosamine, hexuronic acid as the major constituent sugars, and xylose, galactose, L-fucose as the minor ones. Some of the subfractions contained additional glucosamine. Sulfate was also found in all the subfractions as their major constituent. The contents of total amino acids ranged from 1.20 to 17.9%. Serine, threonine, aspartic acid, glutamic acid, glycine, alanine and leucine were found as major amino acids. Pronase digestion did not significantly change their molecular size. The presence of O-xylosyl-serine linkage between carbohydrate chains and peptide moieties ws verified byan alkali treatment. Nevertheless, the presence of small portions of galactose and xylose residues at the reducing ends of the carbohydrate chains suggested a possibility of exertion of endo-beta-galactosidase and endo-beta-xylosidase activities for the linkage regions.

Amino Acids↗
PubMed1980

Urinary keratan sulfate of Morquio's disease.

To elucidate precise chemical nature of urinary keratan sulfate (KS) of Morquio's disease, crude glycosaminoglycans (GAG) were separated from 24-hr urines of 3 patients with Morquio's disease and from pooled urine of a healthy boy, using cetylpyridinium chloride. KS fractions were then separated from the crude GAG after removal of other GAG and acidic glycopeptide by successive digestion with testicular hyaluronidase and chondroitinase ABC, and by nitrous acid treatment, followed by Dowex 1 column chromatography. The distribution of KS in several fractions (1.5 M Fr-5.0 M Fr) obtained by Dowex 1 column chromatography suggested polydispersity of urinary KS. The relative amounts (micrograms/24-hr urine/kg body weight) of the KS fractions excreted into Morquio's urine were 52-63 times as much as that excreted into normal urine. The KS fractions contained galactose, glucosamine and sulfate as the major constituents, together with fairly amounts of galactosamine and sialic acid, and small amounts of mannose, L-fucose and glucose. The KS fractions resembled sulfated glycopeptide with respect to the sugar composition. The contents of sulfate and sialic acid in each KS fraction from Morquio's urine were higher than those in the corresponding one from normal urine, whereas opposite was the case for the ratio of glucosamine to galactosamine. The sulfate contents in the KS fractions from Morquio's urine indicated that the patient excreted over-sulfated KS into urine. The chemical compositions of the KS fractions from Morquio's urine suggest that the sulfatase specific for 6-sulfate linked to sugars with the galactose configuration may act in a early step of the catabolism of oversulfated KS in the normal tissues.

Adolescent↗
PubMed1980

Reducing terminals and molecular weights of glycosaminoglycans in normal human urine.

To elucidate the reducing terminals and the molecular weights of urinary glycosaminoglycans (GAG), the reducing power of the GAG in the acidic subfractions obtained in a previous paper (Endo et al. 1980a) was determined by the methods of Park and Johnson and of Milner and Avigard. Number-average molecular weight was calculated from the value obtained by the Park-Johnson method according to the equation of Partridge et al. The results suggested that xylose and hexuronic acid were present at the reducing terminals of the carbohydrate chains of urinary GAG, and also that 10-65% of the reducing terminals were occupied by the hexuronic acid residues. This finding strongly suggested the exertion of endoglucuronidase activity in the catabolism of the tissue GAG, specifically of chondroitin sulfate isomers. On the other hand, number-average molecular weights of urinary GAG in the subfractions ranged from 5,600 to 15,500, although most of them were within the range between 6,000 and 7,500.

Glycosaminoglycans↗
PubMed1980

Progesterone effect on the biosynthesis of glycoconjugates, specifically of sulfated glycoprotein, in the endometrium of rabbit uterus.

The endometrial scrapings obtained from the uteri of estrogen-progesterone-treated and estrogen-treated rabbits were incubated with N-acetyl-D-[1-3H]glucosamine and [35S]sulfate, and then the incubation medium (M-Fr) was separated from the tissue. The tissue was subsequently homogenized exhaustively in 0.25 M sucrose, and the insoluble residue (R-Fr) was separated. The supernatant at 8,5000 X g for 10 min of the homogenate was subjected to subcellular fractionation by discontinuous sucrose gradient ultracentrifugation, and a Golgi-rich fraction (G-Fr) was obtained. Crude glycoconjugates (glycosaminoglycans and glycoproteins) were then separated from M-Fr, R-Fr and G-Fr after pronase digestion. The amounts of the radioactivities incorporated into these glycoconjugates suggested that progesterone markedly suppressed the estrogen effect within 6 hr in R-Fr and G-Fr, whereas the suppression slightly delayed in M-Fr. The amounts of the radioactivities incorporated into acidic GC, which obtained by CPC-precipitation of the crude GC after digestion with crude heparinase, indicated that the biosynthesis of the CPC-precipitable sulfated glycoproteins was almost completely ceased by progesterone, although other glycoconjugates were still actively synthesized under the progesteronic condition.

Animals↗
PubMed1980

Terminal monosaccharides of carbohydrate chains of glycosaminoglycans in normal human urine.

To elucidate the mode of the exertion of glycosidase activities in the catabolism of the tissue glycosaminoglycans (GAG), the terminal monosaccharides of the carbohydrate chains of urinary GAG in the most prominent subfraction (40% Fr-1.25 M Fr) among the subfractions obtained in a previous paper (Endo et al. 1980a) were investigated. The results of determination of the reducing hexuronic acid and N-acetylhexosamine before and after digestion of the subfraction with beta-glucuronidase and beta-N-acetylhexosaminidase, together with previous data indicated that 0.36 and 0.37 mol of glucuronic acid and N-acetylgalactosamine, respectively, per mol of the subfraction were located at the non-reducing terminals of the carbohydrate chains. The remaining portion (0.27 mol per mol) of the non-reducing ends might be mostly occupied by the sulfated N-acetylgalactosamine residues. On the other hand, 0.25, 0.16 and 0.34 mol of glucuronic acid, N-acetylgalactosamine and xylose, respectively, per mol of the subfraction were indicated to the present at the reducing terminals of the carbohydrate chains. The remaining portion (0.25 mol per mol) of the reducing ends might be mostly occupied by the galactose residues and/or the N-acetylgalactosamine 4-sulfate residues. The present observations provided with evidence for the action of endo-beta-glucuronidase and endo-beta-N-acetylhexosaminidase on the tissue GAG, specifically on chondroitin sulfates.

Glucuronates↗