Polydispersity of glycosaminoglycans in normal human urine.

Endo, Masahiko; Namiki, Osamu; Yosizawa, Zensaku

doi:10.1620/tjem.131.327

Cited by 14 publications

(7 citation statements)

References 20 publications

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“…The results of a comprehensive study on urinary GAG showed the presence of hyaluronic acid, chondroitin sulfates and chondroitin, dermatan sulfate and dermatan, heparan sulfate and keratan sulfate in normal human urine (Endo et al 1980b, c). Moreover, the presence of various degree of the depolymerization products of each GAG and of wide range of the desulfated products of each sulfated GAG was suggested (Endo et al 1980c). These observations suggest that it is hard to investigate the detailed nature of each urinary GAG of a patient or a normal individual.…”

Section: Discussionmentioning

confidence: 99%

A method of screening test for excretion pattern of urinary glycosaminoglycans and its application to normal human urine.

Nagatsuka

Sato

Ototani

et al. 1980

Tohoku J. Exp. Med.

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Section: Discussionmentioning

confidence: 99%

A method of screening test for excretion pattern of urinary glycosaminoglycans and its application to normal human urine.

Nagatsuka

Sato

Ototani

et al. 1980

Tohoku J. Exp. Med.

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“…Although the GAG compositions of the urinary GAG fractions from orthopedic patients (Nagatsuka et al 1981;Sato et al 1982) and normal individuals (Varadi et al 1967;Endo et al 1980) have been reported, the present study provided more o f urinary crude GAG fractions separated from precise information on the urinary GAG than those reported previously. Especially, precise information was obtained on the TCA-insoluble peptide-bound GAG in the urinary GAG fraction from orthopedic patients.…”

Section: Resultsmentioning

confidence: 71%

Enzymatic determination of urinary glycosaminoglycans from orthopedic patients.

Satake

Ototani

Isemura

et al. 1983

Tohoku J. Exp. Med.

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Crude glycosaminoglycan (GAG) fraction was directly precipitated with cetylpyridinium chloride without prior dialysis of urine of orthopedic patients. The crude GAG fraction was then fractionated with trichloroacetic acid (TCA). The TCA-insoluble peptide-bound GAG fraction thus obtained was treated with alkali to eliminate the peptide moiety for enzymatic analysis. The GAG compositions of this fraction and the TCA-soluble fraction were determined by digestion with mucopolysaccharidases (chondroitinase AC, chondroitinase B, chondroitinase C, heparitinase and Streptomyces hyaluronidase). When the amount of the crude GAG fraction was small, no significant amount of the TCA-insoluble peptide-bound GAG fraction was obtained. The GAG composition of this case was also determined by the same procedures after direct alkali-treatment of the crude GAG fraction. The data indicated that the proportion of the TCA-insoluble peptide-bound GAG fraction was very small. The alkali-treated TCA-insoluble peptide-bound GAG fraction contained a larger proportion of heparan sulfate than the TCA-soluble GAG fraction. It was clearly demonstrated that the patients with Werner's syndrome and mucopolysaccharidosis I-S (Scheie) excreted large amounts of hyaluronic acid and dermatan sulfate respectively, into urines. It was indicated in most cases that major urinary GAG were chondroitin 4-sulfate, chondroitin 6-sulfate plus chondroitin and heparan sulfate, while minor ones were dermatan sulfate and hyaluronic acid. In addition, the data suggested a wide range of the degree of desulfation of urinary GAG, and the presence of significant amounts of keratan sulfate plus acidic glycopeptides in the urinary GAG fractions. The present data provided more precise information on urinary GAG from orthopedic patients than those reported previously. glycosaminoglycan; urinary glycosaminoglycans; mucopolysaccharidases; orthopedic patientSince the presence of mucosubstances (glycosaminoglycans and glycoproteins) in human urine was first recognized by Morner (1895), numerous investigations have

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“…The urinary GAG fraction was separated from the cetylpyridinium chloride complex of the non-dialyzable fraction from 10 liters of the pooled urine of healthy adults (Endo et al 1980b). This GAG fraction was dissolved in 0.5 M acetic acid containing 5% calcium acetate and then the fraction precipitated within the range from 40% to 50% of ethanol was collected.…”

Section: Isolation Of Urinary C/ Smentioning

confidence: 99%

“…It was found that the ChS was one of the typical low sulfated ChS which are normally excreted into the urine (Varadi et al 1967;Endo et al 1980b). However, the data obtained showed also that the ChS contained a small ammount of glucosamine-containing substance.…”

Section: Characterization Of Urinary Chsmentioning

confidence: 99%

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Reducing terminals of urinary chondroitin sulfate.

Matsue

Takagaki

Honda

et al. 1985

Tohoku J. Exp. Med.

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Human urinary chondroitin sulfate isolated from the cetylpyridinium chloridecomplex of the non-dialyzable fraction of the pooled urine was subjected to ethanol fractionation, successive enzymic digestion with neuraminidase and mucopolysaccharidases, and anion exchange chromatography. The gas liquid chromatographic analyses of the acetyl and butaneboronic acid ester derivatives of the reduced terminal sugar units after treatment with sodium borohydride plus hydrolysis revealed that 42° of the urinary chondroitin sulfate was bound to peptide through xylose. The reducing terminal sugar units of the peptide-free form consisted of 34.6% of xylose, 22.4% of galactose, 16.4% of glucose of unknown origin and 26.6% of glucuronic acid. These observations showed that the xyloside, galactoside and glucuronide linkages at non-terminal sites of carbohydrate chains of chondroitin sulfate were cleaved in tissues. It was thus suggested that the endo-types of /3-xylosidase, $-galactosidase and $-glucuronidase, which act on proteochondroitin sulfate are present in tissues. reducing terminal ; urinary chondroitin sulfate ; galactose ; glucuronic acid ; xylose Human urinary chondroitin sulfate (ChS), depolymerized and desulfated to various extents, has been regarded as the final degradation products in the catabolism of tissue proteochondroitin sulfate (Wasteson and Wessler 1971; Endo et al. 1980 b). Therefore, identification of the reducing terminal sugar unit of urinary ChS provides a clue to the elucidation of the mechanism of catabolism of tissue proteochondroitin sulfate. Endo et al. (1980c) and Maj ima et al. (1984a, b) indicated that a fraction of urinary glycosaminoglycans (GAGS) has a glucuronic acid residue at the reducing terminal by using the Milner-Avigad reaction (1967) and the isotope labeling method. Then, Endo et al. (1980c) stated that xylose residue might be present at Received January 24, 1985; accepted for publication March 28, 1985. All sugars mentioned in this paper are of D configuration except for gulonic acid, gulonolactone, iduronic acid, idonolactone and fucose which are of z configuration.

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Polydispersity of glycosaminoglycans in normal human urine.

Cited by 14 publications

References 20 publications

A method of screening test for excretion pattern of urinary glycosaminoglycans and its application to normal human urine.

A method of screening test for excretion pattern of urinary glycosaminoglycans and its application to normal human urine.

Enzymatic determination of urinary glycosaminoglycans from orthopedic patients.

Reducing terminals of urinary chondroitin sulfate.

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