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

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 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.

Influence of testosterone on chondroitin sulphate proteoglycan in the rat prostate

1996 ◽  
Vol 74 (5) ◽  
pp. 645-651 ◽  
Author(s):  
Doris E. Terry ◽  
Albert F. Clark
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Testosterone Propionate ◽  
Chondroitin Sulphate ◽  
Fluorescein Isothiocyanate ◽  
Ventral Lobe ◽  
Adult Rat ◽  
Sulphate Proteoglycan ◽  
Chondroitin Sulphate Proteoglycan ◽  
Rat Prostate

There are recognized interactions between prostatic stromal and epithelial cells. These interactions may be influenced by the composition of the extracellular matrix, which is composed of proteins such as collagen, laminin, fibronectin, and proteoglycans (PGs) such as chondroitin sulphate proteoglycan (CSPG). In our continuing studies on prostate biology, we examined the three lobes of the normal adult rat prostate, i.e., ventral, dorsal, and lateral, for CSPG by indirect immunofluorescence, using an immunospecific monoclonal antibody (CS-56) for the chondroitin sulphate (CS) moiety of the PG. Staining of the prostate sections with the CS-56 antibody followed by labelling with IgG fluorescein isothiocyanate conjugate indicated strong fluorescent signals associated with the ventral lobe basement membrane. The signal was stronger and more continuous in the distal acini than in the proximal acini. The staining of the dorsal and lateral lobes was less intense than that of the ventral lobe. Following castration of the rats, the basement membrane staining became discontinuous. Androgen replacement by administration of testosterone propionate (TP) reversed the effects of castration. Quantification of the total CS content showed decreases of about 60% in the ventral and lateral lobes after castration. TP administration for 14 days increased the total CS content several fold above the values for castrated rats in all the lobes. The results demonstrated that CS content was significantly higher for TP-treated animals, suggesting mat the expression of prostate CSPG is regulated by androgens. This approach should be useful in the study of the extracellular matrix in prostate biology.Key words: androgen, basement membrane, extracellular matrix, glycosaminoglycan, prostate.

scholarly journals Synthesis of glycosaminoglycans by human embryonic lung fibroblasts. Different distribution of heparan sulphate, chondroitin sulphate and dermatan sulphate in various fractions of the cell culture

1977 ◽  
Vol 167 (2) ◽  
pp. 383-392 ◽  
Author(s):  
Ingrid Sjöberg ◽  
Lars-Åke Fransson
Keyword(s):  
Glucuronic Acid ◽  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Periodate Oxidation ◽  
Exchange Chromatography ◽  
Lung Fibroblasts ◽  
Relative Distribution ◽  
Dermatan Sulphate ◽  
Human Embryonic Lung ◽  
Iduronic Acid

Foetal human lung fibroblasts, grown in monolayer, were allowed to incorporate 35SO42− for various periods of time. 35S-labelled macromolecular anionic products were isolated from the medium, a trypsin digest of the cells in monolayer and the cell residue. The various radioactive polysaccharides were identified as heparan sulphate and a galactosaminoglycan population (chondroitin sulphate and dermatan sulphate) by ion-exchange chromatography and by differential degradations with HNO2 and chondroitinase ABC. Most of the heparan sulphate was found in the trypsin digest, whereas the galactosaminoglycan components were largely confined to the medium. Electrophoretic studies on the various 35S-labelled galactosaminoglycans suggested the presence of a separate chondroitin sulphate component (i.e. a glucuronic acid-rich galactosaminoglycan). The 35S-labelled galactosaminoglycans were subjected to periodate oxidation of l-iduronic acid residues followed by scission in alkali. A periodate-resistant polymer fraction was obtained, which could be degraded to disaccharides by chondroitinase AC. However, most of the 35S-labelled galactosaminoglycans were extensively degraded by periodate oxidation–alkaline elimination. The oligosaccharides obtained were essentially resistant to chondroitinase AC, indicating that the iduronic acid-rich galactosaminoglycans (i.e. dermatan sulphate) were composed largely of repeating units containing sulphated or non-sulphated l-iduronic acid residues. The l-iduronic acid residues present in dermatan sulphate derived from the medium and the trypsin digest contained twice as much ester sulphate as did material associated with the cells. The content of d-glucuronic acid was low and similar in all three fractions. The relative distribution of glycosaminoglycans among the various fractions obtained from cultured lung fibroblasts was distinctly different from that of skin fibroblasts [Malmström, Carlstedt, Åberg & Fransson (1975) Biochem. J.151, 477–489]. Moreover, subtle differences in co-polymeric structure of dermatan sulphate isolated from the two cell types could be detected.

scholarly journals Influence of collagen lattice on the metabolism of small proteoglycan II by cultured fibroblasts

1990 ◽  
Vol 269 (1) ◽  
pp. 149-155 ◽  
Author(s):  
H Greve ◽  
P Blumberg ◽  
G Schmidt ◽  
W Schlumberger ◽  
J Rauterberg ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Chondroitin Sulphate ◽  
Heparan Sulphate ◽  
Type I ◽  
Collagen Gels ◽  
Dermatan Sulphate ◽  
Cultured Fibroblasts ◽  
Monolayer Cultures ◽  
Collagen Lattice ◽  
Small Proteoglycan

Small dermatan sulphate proteoglycan II from cultured human skin fibroblasts interacts with type I collagen in vitro and in vivo. When fibroblasts are maintained in a type I collagen lattice the proteoglycan remains exclusively within the lattice, and its association with fibrils can be demonstrated immunocytochemically. On the basis of [35S]sulphate incorporation, small proteoglycan II comprises about 80% of total proteoglycans secreted by cells in monolayer culture. In a collagen lattice, fibroblasts down-regulate its synthesis to the level of large chondroitin sulphate/dermatan sulphate and of heparan sulphate proteoglycans, the synthesis of which remains unaffected. Compared with the product from monolayer cultures, small proteoglycan II from collagen gels contained a longer polysaccharide chain which is characterized by a larger proportion of disulphated and a smaller proportion of monosulphated glucuronic acid-containing disaccharides. The half-life varied between 60 and 110 h. It is suggested that the compositional differences between the proteoglycan from monolayer cultures and from cells in a collagen lattice are related to the slower intracellular trafficking of the proteoglycan under the latter culture conditions.

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.

scholarly journals Comparative study on glycosaminoglycans synthesized in peripheral and peritoneal polymorphonuclear leucocytes from guinea pigs

1984 ◽  
Vol 217 (1) ◽  
pp. 199-207 ◽  
Author(s):  
Y Ohhashi ◽  
F Hasumi ◽  
Y Mori
Keyword(s):  
Cell Surface ◽  
Guinea Pigs ◽  
Lysosomal Enzymes ◽  
Culture Medium ◽  
Chondroitin Sulphate ◽  
Alkali Treatment ◽  
Heparan Sulphate ◽  
Polymorphonuclear Leucocytes ◽  
Dermatan Sulphate ◽  
Cell Cell

Glycosaminoglycans synthesized in polymorphonuclear (PMN) leucocytes isolated from blood (peripheral PMN leucocytes) and in those induced intraperitoneally by the injection of caseinate (peritoneal PMN leucocytes) were compared. Both peripheral and peritoneal PMN leucocytes were incubated in medium containing [35S]sulphate and [3H]glucosamine. Each sample obtained after incubation was separated into cell, cell-surface and medium fractions by trypsin digestion and centrifugation. The glycosaminoglycans secreted from peripheral and peritoneal PMN leucocytes were decreased in size by alkali treatment, indicating that they existed in the form of proteoglycans. Descending paper chromatography of the unsaturated disaccharides obtained by the digestion of glycosaminoglycans with chondroitinase AC and chondroitinase ABC identified the labelled glycosaminoglycans of both the cell and the medium fractions in peripheral PMN leucocytes as 55-58% chondroitin 4-sulphate, 16-19% chondroitin 6-sulphate, 16-19% dermatan sulphate and 6-8% heparan sulphate. Oversulphated chondroitin sulphate and oversulphated dermatan sulphate were found only in the medium fraction. In peritoneal PMN leucocytes there is a difference in the composition of glycosaminoglycans between the cell and the medium fractions; the cell fraction was composed of 60% chondroitin 4-sulphate, 5.5% chondroitin 6-sulphate, 16.8% dermatan sulphate and 13.9% heparan sulphate, whereas the medium fraction consisted of 24.5% chondroitin 4-sulphate, 28.2% chondroitin 6-sulphate, 33.7% dermatan sulphate and 10% heparan sulphate. Oversulphated chondroitin sulphate and oversulphated dermatan sulphate were found in the cell, cell-surface and medium fractions. On the basis of enzymic assays with chondro-4-sulphatase and chondro-6-sulphatase, the positions of sulphation in the disulphated disaccharides were identified as 4- and 6-positions of N-acetylgalactosamine. Most of the 35S-labelled glycosaminoglycans synthesized in peripheral PMN leucocytes were retained within cells, whereas those in peritoneal PMN leucocytes were secreted into the culture medium. Moreover, the amount of glycosaminoglycans in peritoneal PMN leucocytes was significantly less than that in peripheral PMN leucocytes. Assay of lysosomal enzymes showed that these activities in peritoneal PMN leucocytes were 2-fold higher than those in peripheral PMN leucocytes.

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