scholarly journals Hurler's, Hunter's and Morquio's syndromes. A biochemical study in the light of current views of the underlying defects

1971 ◽  
Vol 123 (5) ◽  
pp. 883-894 ◽  
Author(s):  
M. F. Dean ◽  
Helen Muir ◽  
R. J. F. Ewins
Keyword(s):  
Molecular Weight ◽  
Chondroitin Sulphate ◽  
Biochemical Study ◽  
Heparan Sulphate ◽  
Total Output ◽  
Dermatan Sulphate ◽  
Keratan Sulphate ◽  
Hurler’S Syndrome ◽  
Morquio's Syndrome ◽  
Hunter's Syndrome

Glycosaminoglycans were isolated from the urine of three patients with Hurler's, Hunter's and Morquio's syndromes and also from the liver and spleen of the case of Hurler's syndrome by a procedure avoiding further degradation. A method of determining the proportions of dermatan sulphate, heparan sulphate and chondroitin sulphate in each preparation is described. The relative proportions of these glycosaminoglycans in the urine and organs of the case of Hurler's syndrome were very similar. Glycosaminoglycans from the organs were of much lower molecular weight than normal, consisting of single chains of molecular weight about 5000 together with multiples of up to four such chains attached to peptide moieties. The linkage region normally attaching glycosaminoglycan chains to protein in whole protein–polysaccharides of connective tissue was degraded progressively towards serine. The total output and relative proportions of abnormal glycosaminoglycans in the urine were compared in two brothers with Hunter's syndrome examined on two occasions 4 years apart. At comparable ages they excreted about the same amount, and the relative proportions of each glycosaminoglycan remained essentially constant. The composition and chromatographic behaviour of the glycosaminoglycan in the urine from the case of Morquio's syndrome indicated that it consisted of material containing about one-third keratan sulphate and two-thirds chondroitin sulphate as part of the same molecule, as in proteoglycans of cartilage. The total output of glycosaminoglycans, although higher than normal, was considerably less than in other types of Mucopolysaccharidoses.

scholarly journals The nature of the non-ultrafilterable glycosaminoglycans of normal human urine

1971 ◽  
Vol 122 (3) ◽  
pp. 373-384 ◽  
Author(s):  
E. Wessler
Keyword(s):  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Dermatan Sulphate ◽  
Keratan Sulphate ◽  
Molar Ratios ◽  
Sodium Barbital ◽  
Normal Human ◽  
Normal Men ◽  
Barbital Buffer ◽  
Acidic Glycosaminoglycans

1. The non-ultrafilterable acidic glycosaminoglycans from pooled urine of normal men, aged about 20, were isolated and characterized. The isolation procedure included digestion with sialidase and pronase, and fractionation by stepwise elution from an ECTEOLA-cellulose column. The glycosaminoglycans in each fraction were separated from each other by preparative electrophoresis in sodium barbital buffer and in barium acetate. 2. Approximate relative amounts of the different glycosaminoglycans were: chondroitin sulphate 60%, chondroitin 2%, hyaluronic acid 4%, dermatan sulphate 1%, heparan sulphate 15% and keratan sulphate 18%. Chondroitin sulphate–dermatan sulphate hybrids seemed to occur in trace amounts. 3. Chondroitin sulphate, heparan sulphate and keratan sulphate were heterogeneous with respect to degree of sulphation. Two distinct groups of chondroitin sulphate fractions were found, with sulphate/hexosamine molar ratios of about 0.5 and 1 respectively. The sulphate/hexosamine molar ratios in the heparan sulphate fractions varied from 0.5 to 0.9; the N-sulphate/hexosamine ratio was about 0.5 in all fractions. The sulphate/hexosamine molar ratios in the keratan sulphate fractions varied from 0.2 to 0.7.

Dermatan sulphate promotes neuronal differentiation in mouse and human stem cells

2020 ◽  
Author(s):  
Chika Ogura ◽  
Kazumi Hirano ◽  
Shuji Mizumoto ◽  
Shuhei Yamada ◽  
Shoko Nishihara
Keyword(s):  
Stem Cells ◽  
Neurite Outgrowth ◽  
Neuronal Differentiation ◽  
Neural Progenitor Cells ◽  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Embryonic Stem ◽  
Hydroxyl Group ◽  
Human Stem Cells ◽  
Dermatan Sulphate

Abstract Dermatan sulphate (DS), a glycosaminoglycan, is present in the extracellular matrix and on the cell surface. Previously, we showed that heparan sulphate plays a key role in the maintenance of the undifferentiated state in mouse embryonic stem cells (mESCs) and in the regulation of their differentiation. Chondroitin sulphate has also been to be important for pluripotency and differentiation of mESCs. Keratan sulphate is a marker of human pluripotent stem cells. To date, however, the function of DS in mESCs has not been clarified. Dermatan 4 sulfotransferase 1, which transfers sulphate to the C-4 hydroxyl group of N-acetylgalactosamine of DS, contributes to neuronal differentiation of mouse neural progenitor cells. Therefore, we anticipated that neuronal differentiation would be induced in mESCs in culture by the addition of DS. To test this expectation, we investigated neuronal differentiation in mESCs and human neural stem cells (hNSCs) cultures containing DS. In mESCs, DS promoted neuronal differentiation by activation of extracellular signal-regulated kinase 1/2 and also accelerated neurite outgrowth. In hNSCs, DS promoted neuronal differentiation and neuronal migration, but not neurite outgrowth. Thus, DS promotes neuronal differentiation in both mouse and human stem cells, suggesting that it offers a novel method for efficiently inducing neuronal differentiation.

Heparin and dermatan sulphate induced capacitation of frozen-thawed bull spermatozoa measured by merocyanine-540

Zygote ◽  
2007 ◽  
Vol 15 (3) ◽  
pp. 225-232 ◽  
Author(s):  
A.-S. Bergqvist ◽  
J. Ballester ◽  
A. Johannisson ◽  
N. Lundeheim ◽  
H. Rodríguez-Martínez
Keyword(s):  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Negative Control ◽  
Dermatan Sulphate ◽  
Flow Cytometric ◽  
Merocyanine 540 ◽  
Incubation Duration ◽  
Flow Cytometric Study ◽  
Oviductal Fluid

SummaryGlycosaminoglycans (GAGs) are present in the oviduct in which the major part of sperm capacitation occurs. In this study we have tested how capacitation of frozen-thawed bull spermatozoa is effected by exposure to different GAGs detectable or possibly present in oviductal fluid; i.e. heparin, hyaluronan, heparan sulphate, dermatan sulphate and chondroitin sulphate. Following exposure of different duration, the spermatozoa were stained with either Chlortetracycline (CTC) or merocyanine-540 and evaluated with epifluorescent light microscopy or flow cytometry, respectively. Heparin elicited a significant increase in the number of alive, capacitated spermatozoa, either expressed as higher merocyanine-540 fluorescence (p < 0.0001) or as B-pattern (p = 0.0021) in the CTC assay, during 4 h of incubation. When comparing the different GAG treatments one by one to the negative control in the flow cytometric study, only heparin and dermatan sulphate were significant (p < 0.0001) higher than the control at 0–30 min of incubation. Duration of incubation did not affect the proportion of capacitated spermatozoa when measured as merocyanine-540 fluorescence or CTC B-pattern, but the length of the incubation did affect the number of dead (Yo-PRO 1 positive) spermatozoa (p < 0.0001). Exposure to zona pellucida proteins significantly increased the proportion of acrosome reacted spermatozoa (p = 0.016). Both heparin and dermatan sulphate induce capacitation of frozen-thawed bull spermatozoa in vitro.

scholarly journals Sulphated glycosaminoglycans in regenerating rat liver

1980 ◽  
Vol 188 (3) ◽  
pp. 769-773 ◽  
Author(s):  
M Edward ◽  
W F Long ◽  
H H Watson ◽  
F B Williamson
Keyword(s):  
Molecular Mechanisms ◽  
Temporal Trend ◽  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Fold Increase ◽  
Sham Operation ◽  
Dermatan Sulphate ◽  
Weight Percentage ◽  
Biphasic Pattern ◽  
Sulphated Glycosaminoglycans

The total weight percentage glycosaminoglycan content of rat liber was found to increase by 50% in the first 30 h after partial hepatectomy. The content returned to near normal by the third day, but then increased again to a second maximum at 5-6 days, only to gradually decline to normal by the ninth day, when regeneration was nearly complete. This biphasic pattern was most marked in the chondroitin sulphate A/C component, with a 6-fold increase by the sixth day. Dermatan sulphate showed the same temporal trend, whereas heparan sulphate remained relatively unaltered. No such changes were detected in the livers of rats subjected to sham operation. The possible molecular mechanisms underlying the apparent link between cellular glycosaminoglycan content and proliferative tendency are discussed.

scholarly journals Properties, bioactive potential and extraction processes of glycosaminoglycans: an overview

2021 ◽  
Vol 51 (7) ◽  
Author(s):  
Evellin Balbinot-Alfaro ◽  
Meritaine da Rocha ◽  
Alexandre da Trindade Alfaro ◽  
Vilásia Guimarães Martins
Keyword(s):  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Extraction Process ◽  
Therapeutic Agents ◽  
Biological Processes ◽  
Dermatan Sulphate ◽  
Extraction Processes ◽  
Therapeutic Properties ◽  
Bioactive Potential ◽  
General Aspects

ABSTRACT: Glycosaminoglycans (GAGs) are long-chain polysaccharides that are divided into sulphates and non-sulphates, these being chondroitin sulphate, heparan sulphate, dermatan sulphate, heparin sulphate and the only non-sulphate in the group is hyaluronic acid. GAGs are obtained from animal tissue and by an expensive low-yield extraction process; however, they are highly commercially valued polysaccharides and exploited in the biomedical market. Their disaccharidic composition, chain length and sulfation pattern present great variability depending on the species and extraction factors. GAGs possess immunomodulatory, antioxidant, antiviral, anti-inflammatory, neuroprotective, antiproliferative and anticoagulant properties, functioning as therapeutic agents modulating an array of biological processes. This report presents the general aspects of each GAG, source and extraction process, in addition to the characteristics that give them the most varied therapeutic properties and pharmacological applications.

scholarly journals The presence of a cartilage-like proteoglycan in the adult human meniscus

1981 ◽  
Vol 197 (1) ◽  
pp. 77-83 ◽  
Author(s):  
P J Roughley ◽  
D McNicol ◽  
V Santer ◽  
J Buckwalter
Keyword(s):  
Hyaluronic Acid ◽  
Chondroitin Sulphate ◽  
Gradient Centrifugation ◽  
Large Subunit ◽  
Dermatan Sulphate ◽  
Keratan Sulphate ◽  
Adult Human ◽  
Cscl Density Gradient ◽  
Cartilage Proteoglycans ◽  
Aggregate Structures

Proteoglycans were extracted from the adult human meniscus under dissociative conditions and purified by CsCl-density-gradient centrifugation. The preparations of highest density contained proteoglycan that possessed the ability to interact with hyaluronic acid, was of large subunit size and was composed of chondroitin sulphate, keratan sulphate and sialic acid-containing oligosaccharides. This ‘cartilage-like’ proteoglycan also exhibited subunit and aggregate structures analogous to those of hyaline-cartilage proteoglycans when examined by electron microscopy. However, the composition of this proteoglycan was more comparable with proteoglycans from immature cartilage than from age-matched cartilage. The preparations from lower density, which were enriched in dermatan sulphate, contained smaller proteoglycan that was not able to interact with hyaluronic acid. This non-aggregating proteoglycan may be structurally distinct from the ‘cartilage-like’ proteoglycan, which does not contain dermatan sulphate.

scholarly journals Coupling of glycosaminoglycans to agarose beads (Sepharose 4B)

1971 ◽  
Vol 124 (4) ◽  
pp. 677-683 ◽  
Author(s):  
P.-H. Iverius
Keyword(s):  
Cyanogen Bromide ◽  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Direct Analysis ◽  
Dermatan Sulphate ◽  
Peptide Residue ◽  
Agarose Beads ◽  
Freeze Dried ◽  
Coupling Procedure ◽  
Sepharose 4B

1. Heparin, heparan sulphate, chondroitin sulphate and dermatan sulphate were covalently attached to beads of agarose activated by cyanogen bromide. The bond is probably mediated by the amino group of a serine or peptide residue at the reducing end of the polysaccharide chain. 2. The uptake of glycosaminoglycan during the coupling procedure is about 0.9mg/ml of wet gel. However, direct analysis of washed and freeze-dried gels reveals that only about one-third of this amount is firmly attached to the gel. 3. The use of the gels for polysaccharidase analyses is exemplified by a hyaluronidase assay. Further applications, e.g. interaction studies and preparative purposes, are discussed.

scholarly journals Detection of secondary structure in glycosaminoglycans via the1H n.m.r. signal of the acetamido NH group

1982 ◽  
Vol 207 (1) ◽  
pp. 139-144 ◽  
Author(s):  
J E Scott ◽  
F Heatley
Keyword(s):  
Secondary Structure ◽  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Periodate Oxidation ◽  
Close Approach ◽  
Dimethyl Sulphoxide ◽  
Space Filling ◽  
Keratan Sulphate ◽  
Inorganic Cations ◽  
Acid Glycosaminoglycans

Two simple methods for dissolving salts of acid glycosaminoglycans with inorganic cations (e.g. Li+ and Na+) in dry dimethyl sulphoxide are described. Complete n.m.r. spectra of, e.g., Na+ and Li+ salts of chondroitin sulphate and keratan sulphate were obtained on these solutions. In [2H6]dimethyl sulphoxide the NH resonance of 2-acetamido-2-deoxy hexosides is in the range 7.2-8.0 delta, but is downfield (8.3-9.3 delta) when the NH is H-bonded to -CO2-. Heparan sulphate shows two NH resonances, of which one (at 8.3 delta) is probably indicative of H-bonding. Space-filling models show that a very close approach of NH to -CO2- across the alpha-glucosaminidic bond is possible, and a solution configuration for heparan sulphate is proposed. The n.m.r. results are entirely compatible with interpretations of periodate-oxidation kinetics, based on H-bonded secondary structures present in hyaluronate and chondroitin sulphates, but not in dermatan (or keratan) sulphate.

scholarly journals The glycosaminoglycans of human tracheobronchial cartilage

1970 ◽  
Vol 120 (4) ◽  
pp. 777-785 ◽  
Author(s):  
R. M. Mason ◽  
F. S. Wusteman
Keyword(s):  
Molecular Weight ◽  
Potassium Hydroxide ◽  
Chondroitin Sulphate ◽  
Cetylpyridinium Chloride ◽  
Exchange Chromatography ◽  
Chemical Heterogeneity ◽  
Keratan Sulphate ◽  
Sulphate Content ◽  
Age Dependent ◽  
Dowex 1

1. The glycosaminoglycans of human tracheobronchial cartilages from subjects of various ages were liberated by proteolysis of the tissue and purified by ion-exchange chromatography. Purified glycosaminoglycans were fractionated on Dowex 1 resin and cetylpyridinium chloride was used to separate chondroitin sulphates and keratan sulphates occurring in the same fraction. 2. The total chondroitin sulphate content of the cartilages decreased linearly with increasing age. Age-dependent changes in the chemical heterogeneity of chondroitin sulphate were observed, a low-sulphated compound making up 25% of the total glycosaminoglycan at birth but rapidly diminishing in content during the first 6 months of life. Of the total chondroitin sulphate the 6-isomer became rather more prominent than the 4-isomer with increasing age. 3. The total keratan sulphate content of the cartilages increased from trace amounts only at birth to a plateau value by the beginning of the fifth decade. Of the total keratan sulphate approx. 70% was due to a high-molecular-weight compound with a sulphate/hexosamine ratio of 1.5–1.8: 1.0. The degree of sulphation varied between compounds isolated from different individuals. The remaining 30% of the keratan sulphate appeared to be intimately associated with chondroitin 6-sulphate and could only be separated from it after treatment with 0.45m-potassium hydroxide. The hybrid glycosaminoglycans were of lower molecular weight and had a lower sulphate/hexosamine ratio than the major keratan sulphate compound.

Glycosaminoglycans in the three lobes of the rat prostate following castration and testosterone treatment

1996 ◽  
Vol 74 (5) ◽  
pp. 653-658 ◽  
Author(s):  
Doris E. Terry ◽  
Albert F. Clark
Keyword(s):  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Lateral Lobe ◽  
Enzymatic Digestion ◽  
Ventral Lobe ◽  
Dorsal Lobe ◽  
Dermatan Sulphate ◽  
Sham Control ◽  
Time Intervals ◽  
Rat Prostate

Androgen dependence of glycosaminoglycans (GAGs) in the prostate was studied using tissue from intact (sham control), castrated, and androgen-treated castrated rats. GAGs from the ventral, dorsal, and lateral lobes of the prostate were isolated and characterized by cellulose electrophoresis using appropriate GAG standards and enzymatic digestion or nitrous acid hydrolysis. Androgen deprivation was initiated by castration and rats were sacrificed at various time intervals after 7 days castration. After castration, the total GAG content decreased in the three prostate lobes. At day 7 after castration, the total hyaluronic acid (HA) content decreased by 74% (ventral lobe) and 34% (lateral lobe) compared with the sham control. No effect was observed for HA content in the dorsal lobe. Castration decreased the total heparan sulphate (HS), dermatan sulphate (DS), and chondroitin sulphate (CS) contents in the three prostate lobes at 0 days of treatment, except for the CS content in the dorsal and lateral lobes. Androgen replacement increased the total GAG contents in the three prostate lobes. At 14 days of testosterone propionate treatment, there were 9-, 6.8-, 4.1- and 3.7-fold increases in HA, HS, DS, and CS, respectively, in the ventral lobe. These increases were more rapid and profound in the ventral than in the dorsal and lateral lobes. These findings indicate that all GAGs are regulated by androgen and there may be lobe-specific differences in their regulation. This could be a function of the heterogenous populations of cells in each lobe.Key words: castration, glycosaminoglycan, prostate, testosterone

Sign in / Sign up

Export Citation Format

Share Document