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PubMed1994

Appearance and fate of a beta-galactanase, alpha, beta-galactosidases, heparan sulfate and chondroitin sulfate degrading enzymes during embryonic development of the mollusc Pomacea sp.

The characterization and properties of a beta-galactanase and alpha- and beta-galactosidases as well as heparan sulfate and chondroitin sulfate degrading enzymes which appear during the 15 days of the embryonic development of the mollusc Pomacea sp. is reported. The beta-galactanase, which appears around day 7 of development, was separated from alpha- and beta-galactosidase which emerge at day 1 and 4 after oviposition, respectively. The galactanase seems to be responsible for the degradation of an acidic beta-galactan (which is also synthesized by the eggs around day 5) to galactose and di- and tri-galactosides. Heparan sulfate appears around day 10 of development together with a heparan sulfate endoglucuronidase responsible for the degradation of its N-acetylated region. An alpha-N-acetylglucosaminidase and a beta-glucuronidase which act upon the N-acetylated fragments formed from heparan sulfate emerge around day 4 of development. Chondroitin sulfate and a chondroitin sulfate sulfatase emerge around day 9 of development whereas a beta-N-acetylgalactosaminidase and the beta beta-galactan, heparan and chondroitin sulfate, respectively. The possible role of these elements in the migration of mesenchymal cells, in the processes of cell-cell recognition and control of cell growth is discussed.

Acetylglucosaminidase↗
PubMed1994

Chondroitinase ABC-resistant sulfated trisaccharides isolated from digests of chondroitin/dermatan sulfate chains.

Four kinds of sulfated trisaccharides resistant to chondroitinase ABC were isolated after chondroitinase B or ABC treatment of dermatan sulfate or various chondroitin sulfate isomers, respectively. Their composition was determined by chemical analysis and fast atom bombardment-mass spectrometry. Their structures were characterized by chondroitinase ACII digestion in conjunction with HPLC, and 500-MHz one- and two-dimensional 1H NMR spectroscopy. All the four trisaccharides have in common the core saccharide sequence, alpha-L-delta 4,5HexpA-(1-->3)-beta-D-GalpNAc-(1-->4)-D-GlcpA. A monosulfated component isolated from shark scapular cartilage chondroitin sulfate C or bovine aorta dermatan sulfate was elucidated as alpha-L-delta 4,5HexpA-(1-->3)-beta-D-GalpNAc6SO3(-)-(1-->4)-D-GlcpA or alpha-L-delta 4,5HexpA-(1-->3)-beta-D-GalpNAc4SO3(-)-(1-->4)-D-GlcpA , respectively. A disulfated component obtained from shark scapular cartilage chondroitin sulfate C or squid cartilage chondroitin sulfate E was identified as alpha-L-delta 4,5HexpA2SO3(-)-(1-->3)-beta-D-GalpNAc6SO3(-)-(1-->4)-D-G lcpA or alpha-L-delta 4,5HexpA-(1-->3)-beta-D-GalpNAc4SO3(-)6SO3(-)-(1-->4)- D-GlcpA, respectively. These trisaccharides are derived from the reducing termini of the parent polysaccharides. Some of the trisaccharides could be derived from the reducing termini exposed by the peeling reaction during the alkaline treatment while some others may represent the cleavage sites exposed by tissue endo-beta-D-glucuronidase(s), indicating the presence of such enzyme(s) which may release chondroitin/dermatan sulfate fragments from proteoglycans.

Animals↗
PubMed2000

Patients with head and neck tumors excrete a chondroitin sulfate with a low degree of sulfation: a new tool for diagnosis and follow-up of cancer therapy.

The chondroitin sulfate excreted in the urine of 10 patients with cancer of the head and neck and 27 healthy subjects was analyzed. The disaccharide products formed from chondroitin sulfate excreted by these 10 patients by action of chondroitinase ABC show a significant (P < 0.0001) relative increase of nonsulfated disaccharide (35.6% +/- 5.7%) when compared with the nonsulfated disaccharide (10.0% +/- 0.9%) present in the chondroitin sulfate of 27 healthy subjects. In 6 patients the structure of the excreted compound was analyzed up to 4 months after surgery. After removal of the cancer, the percent amounts of the nonsulfated disaccharide tend to approach the values found for the chondroitin sulfate of healthy subjects. A significant (P < 0.0001) change in the ratio of urinary chondroitin sulfate and heparan sulfate and a decrease in the electrophoretic migration of chondroitin sulfate were also observed. All of the patients with head and neck cancer analyzed so far have shown this structural anomaly of urinary chondroitin sulfate. This assay may be useful in the diagnosis and follow-up of cancer therapy.

Adult↗
PubMed2000

Overexpression of different isoforms of glucosaminyl N-deacetylase/N-sulfotransferase results in distinct heparan sulfate N-sulfation patterns.

Functional interactions of heparan sulfate (HS) with selected proteins depend on distinct saccharide sequences which are generated during biosynthesis of the polysaccharide. Glucosaminyl N-deacetylase/N-sulfotransferases (NDSTs) catalyze both the N-deacetylation and N-sulfation reactions that initiate the modification of the (GlcNAc-GlcA)(n) polysaccharide backbone. The N-acetyl/N-sulfate exchange is restricted to certain regions of the polysaccharide chains, and only these can be further modified by glucuronyl C5-epimerization and O-sulfation at various positions. To investigate whether NDST isoforms influenced differently the structure of HS, murine NDST-1 was overexpressed in human kidney 293 cells, and the structure of the HS produced was compared to HS from NDST-2 overexpressing cells [Cheung, W. F., Eriksson, I., Kusche-Gullberg M., Lindahl, U., and Kjellén, L. (1996) Biochemistry 35, 5250-5256]. The level of N-sulfation increased from 40% in control cells to 60% and 80%, respectively, in NDST-1 and NDST-2 transfected cells. Interestingly, the increase in N-sulfation was accompanied by an increased chain length, while no effect on IdoA content or O-sulfation was seen. The most extended N-sulfated domains were found in HS synthesized by NDST-2 transfected cells. Since both the N-deacetylase and the N-sulfotransferase activities were lower in these cells than in the NDST-1 overexpressing cells, we conclude that, in addition to the level of enzyme expression, the NDST isoform also is important in determining the N-sulfation pattern in HS.

Acetylation↗
PubMed2002

Selenate-resistant mutants of Arabidopsis thaliana identify Sultr1;2, a sulfate transporter required for efficient transport of sulfate into roots.

To investigate how plants acquire and assimilate sulfur from their environment, we isolated and characterized two mutants of Arabidopsis thaliana deficient in sulfate transport. The mutants are resistant to selenate, a toxic analogue of sulfate. They are allelic to each other and to the previously isolated sel1 (selenate-resistant) mutants, and have been designated sel1-8 and sel1-9. Root elongation in these mutants is less sensitive to selenate than in wild-type plants. Sulfate uptake into the roots is impaired in the mutants under both sulfur-sufficient and sulfur-deficient conditions, but transport of sulfate to the shoot is not affected. The sel1 mutants contain lesions in the sulfate transporter gene Sultr1;2 located on the lower arm of chromosome 1. The sel1-1, sel1-3 and sel1-8 mutants contain point mutations in the coding sequences of Sultr1;2, while the sel1-9 mutant has a T-DNA insertion in the Sultr1;2 promoter. The Sultr1;2 cDNA derived from wild-type plants is able to complement Saccharomyces cerevisiae mutants defective in sulfate transport, but the Sultr1;2 cDNA from sel1-8 is not. The Sultr1;2 gene is expressed mainly in roots, and accumulation of transcripts increases during sulfate deprivation. Examination of transgenic plants containing the Sultr1;2 promoter fused to the GUS-reporter gene indicates that Sultr1;2 is expressed mainly in the root cortex, the root tip and lateral roots. Weaker expression of the reporter gene was observed in hydathodes, guard cells and auxiliary buds of leaves, and in anthers and the basal parts of flowers. The results indicate that Sultr1;2 is primarily involved in importing sulfate from the environment into the root.

Alleles↗
PubMed1999

Molecular cloning and characterization of a human uronyl 2-sulfotransferase that sulfates iduronyl and glucuronyl residues in dermatan/chondroitin sulfate.

A partial-length human cDNA with a predicted amino acid sequence homologous to a previously described heparan sulfate iduronyl 2-sulfotransferase (Kobayashi, M., Habuchi, H., Yoneda, M., Habuchi, O., and Kimata, K. (1997) J. Biol. Chem. 272, 13980-13985) was obtained by searching the expressed sequence-tagged data bank. Northern blot analysis was performed using this homologous cDNA as a probe, which demonstrated ubiquitous expression of messages of 5.1 and 2.0 kilobases in a number of human tissues and in several human cancer cell lines. Since the human lymphoma Raji cell line had the highest level of expression, it was used to isolate a full-length cDNA clone. The full-length cDNA was found to contain an open reading frame that predicted a type II transmembrane protein composed of 406 amino acid residues. The cDNA in a baculovirus expression vector was expressed in Sf9 insect cells, and cell extracts were then incubated together with 3'-phosphoadenosine 5'-phospho[35S]sulfate and potential glycosaminoglycan acceptors. This demonstrated substantial sulfotransferase activity with dermatan sulfate, a small degree of activity with chondroitin sulfate, but no sulfotransferase activity with desulfated N-resulfated heparin. Analysis of [35S]sulfate-labeled disaccharide products of chondroitin ABC, chondroitin AC, and chondroitin B lyase treatment demonstrated that the enzyme only transferred sulfate to the 2-position of uronyl residues, which were preponderantly iduronyl residues in dermatan sulfate, but some lesser transfer to glucuronyl residues of chondroitin sulfate.

Amino Acid Sequence↗
PubMed1989

Plasma anticoagulant mechanisms of heparin, heparan sulfate, and dermatan sulfate.

The relationship between two anticoagulant actions of glycosaminoglycans (GAGs), namely the catalysis of thrombin inhibition (assessed by thrombin-antithrombin-III and thrombin-heparin-cofactor-II formation) and the inhibition of prothrombin activation, was explored by comparing the effects of heparin, heparan sulfate, and dermatan sulfate on the two reactions in plasma. Heparan sulfate and dermatan sulfate were also resulfated in vitro to yield products with sulfate/carboxylate ratios similar to those of heparin. Their effects on thrombin inhibition and the activation of prothrombin were also determined. The catalytic efficiency of the five GAGs on thrombin inhibition and their inhibitory effects on prothrombin activation decreased in the following order: heparin; resulfated dermatan sulfate; resulfated heparan sulfate; heparan sulfate = dermatan sulfate. These results suggest that the catalytic efficiency of a glycosaminoglycan on thrombin inhibition translates to its inhibitory effect on prothrombin activation, since catalysis of thrombin inhibition results in the inhibition of the thrombin-dependent positive feedback reactions of coagulation which facilitate prothrombinase formation.

Antithrombin III↗
PubMed1983

Absorption of sulfate from orally administered magnesium sulfate in man.

The purpose of this investigation was to determine the suitability of orally administered magnesium sulfate as a source of inorganic sulfate for counteracting the systemic depletion of sulfate caused by large doses of acetaminophen and certain other drugs that are metabolized to sulfate conjugates. Oral administration of 13.9 g magnesium sulfate U.S.P., in 4 equal hourly increments, to seven healthy men resulted in the urinary excretion (corrected for baseline excretion rate) of an amount of inorganic sulfate equivalent to 30.2 +/- 17.2 percent (mean +/- SD) of the dose during the first 24 hours. Excretion during the subsequent 48 hours was negligible. Six of the subjects experienced loose stools or diarrhea. Compared to sodium sulfate, magnesium sulfate appears to be absorbed less completely and more erratically, and to produce more adverse effects.

Administration, Oral↗
PubMed1985

Sulfation of chondroitin oligosaccharides in vitro. Analysis of sulfation ratios.

Microsomal preparations from cultured chick embryo chondrocytes were incubated with 3'-phosphoadenosine 5'-phosphosulfate and oligosaccharides prepared from chondroitin. Rates of 4- and 6-sulfation were measured at pH 6 and 8 in the presence of MnCl2 and Brij 58. Ratios of the overall 6-sulfation to 4-sulfation rates ranged from 40-200 at pH 8 and from 6-35 at pH 6, depending upon the composition of the assay mixture. When saturating concentrations of 3'-phosphoadenosine 5'-phosphosulfate and the oligosaccharide acceptors were used, the resulting products were mixtures of monosulfated oligosaccharides. The compositions of the mixtures formed from oligosaccharides with degrees of polymerization from 4-12 at pH 6 and 8 were analyzed. Sulfate substituents were found at all N-acetyl-D-galactosamine (GalNAc) residues in the acceptors but were not evenly distributed along the oligosaccharide chains. For oligosaccharides with nonreducing terminal D-glucuronic acid (GlcUA) residues, sulfation at the nonreducing terminal GlcUA----GalNAc occurred exclusively at the C6 of the GalNAc residue. However, for oligosaccharides with nonreducing terminal GalNAc residues the rate of 6-sulfation of the nonreducing terminal GalNAc was markedly reduced and was similar to the rate of 4-sulfation at the same position. The rates of sulfation at the reducing ends of the oligosaccharides were relatively high for the shorter oligosaccharide acceptors but decreased with increasing length of the acceptor, suggesting that the sulfotransferases recognized primarily the GalNAc residues in the nonreducing terminal regions.

Animals↗
PubMed1984

Isolation and structural studies of heparan sulfates and chondroitin sulfates from three species of molluscs.

The isolation and some structural features of heparan sulfates and chondroitin sulfates from three species of molluscs (Pomacea sp., Tagelus gibbus, and Anomalocardia brasiliana) are reported. It is shown that heparan sulfates with structural similarities to the ones found in mammals are present in the three molluscs analyzed. All the heparan sulfates were degraded by heparitinases I and II to four distinct unsaturated disaccharides with the same properties as the ones present in heparan sulfates of mammalian origin. This suggests that these four disaccharide units are maintained through the evolution. Furthermore, the proportion of these units varied in the heparan sulfates according to the species of origin. The chondroitin sulfates, on the other hand, exhibit different structural features according to the species of origin. For instance, by the action of chondroitinase AC, 4- and nonsulfated disaccharides are produced from Pomacea chondroitin, whereas 4- and 6-sulfated disaccharides are formed from Tagelus and Anomalocardia. The possible role of these compounds in cell recognition and/or adhesiveness is discussed in view of the present findings.

Animals↗
PubMed1986

Structure of proteoheparan sulfates from fibroblasts. Confluent and proliferating fibroblasts produce at least three types of proteoheparan sulfates with functionally different core proteins.

[3H]Leucine- and [35S]sulfate-labeled proteoheparan sulfates were isolated from postconfluent or proliferating cultures of human skin fibroblasts. Cell layers were solubilized by Triton X-100, and transferrin-binding macromolecules were isolated by affinity chromatography. Proteoglycans with no affinity for transferrin were purified by using ion-exchange and gel permeation chromatography. Postconfluent cells synthesize a proteoheparan sulfate of Mr 350,000 (as determined by gel permeation chromatography) which has affinity for transferrin as well as for octyl-Sepharose. Its core protein (Mr 180,000) consists of two disulfide-bonded polypeptides of Mr 90,000. This species was not detected in cultures of proliferating cells. Proliferating and confluent cells also synthesize other forms of proteoheparan sulfates (Mr 200,000-400,000) which have no affinity for transferrin. However, most of them have affinity for octyl-Sepharose. The core protein of proteoheparan sulfates made by proliferating cells has Mr 50,000. A smaller form (Mr 250,000) of this proteoglycan was solubilized by Triton X-100, whereas a larger form (Mr 400,000) remained associated with the pericellular matrix. A third type of proteoheparan sulfate (Mr 200,000) without affinity for transferrin nor octyl-Sepharose was associated with postconfluent cell layers but not with proliferating ones. Its core protein has Mr 35,000. Heparan sulfate oligosaccharides (Mr 6,000 or higher) were found in proliferating cells but not in postconfluent ones.

Cell Division↗
PubMed1988

Distribution of chondroitin 4-sulfate and chondroitin 6-sulfate in human articular and growth cartilage.

The relative concentrations of chondroitin 4- and chondroitin 6-sulfate in different normal human cartilages are reported. Articular cartilages contained higher concentrations of chondroitin 6-sulfate, whereas growth cartilages contained nearly equal amounts of chondroitin 4- and chondroitin 6-sulfate. Adult cartilages, in which the calcification process is already complete, contained only chondroitin 6-sulfate. The results suggest that chondroitin 6-sulfate is related to the integrity of the articular surfaces, whereas chondroitin 4-sulfate seems to be an important factor in the calcification process. The pathogenesis of the bone and cartilage alterations that occur in patients affected by heritable disorders of the sulfation of chondroitin sulfate are discussed in view of these findings.

Cartilage, Articular↗
PubMed1986

Dissociation of increased sulfation from sulfate replenishment and hepatoprotection in acetaminophen-poisoned mice by N-acetylcysteine stereoisomers.

N-Acetylcysteine stereoisomers were compared for their ability to alter the sulfation and hepatotoxicity of acetaminophen. The clinically used L-isomer increased urinary excretion of inorganic sulfate 2-3 fold and prevented liver injury, but failed to increase acetaminophen sulfation in mice. Conversely, the nonphysiologic D-isomer failed to increase urinary excretion of inorganic sulfate or prevent hepatotoxicity, but increased acetaminophen sulfation appreciably (by 39%). The basis of the incongruence between changes in the availability of inorganic sulfate and the sulfation of acetaminophen is not known. These data indicate that a modest increase in acetaminophen sulfation, occurring alone following N-acetylcysteine treatment, is insufficient to explain the profound efficacy of the antidote in mice, and further suggest that this holds true for other species, such as humans, that are comparatively poor in the sulfoconjugation of acetaminophen.

Acetaminophen↗
PubMed1991

A novel method for differentiating dextran sulfate from related sulfated polysaccharides.

A method is described for unequivocal identification of dextran sulfate, based on combined chemical desulfation and dextranase enzymolysis of dextran sulfate moieties to isomaltose, a specific indicator of dextran-type precursors. The method was developed using high-resolution (300 MHz) 1H NMR spectroscopy for assurance of the molecular transformations, identification, and estimation of the hydrolysis products. Overall conversion of approximately 80% of highly sulfated and moderately sulfated dextran sulfates was realized. Both 2-D 1H and 13C NMR spectra of a dextran sulfate (MW 500,000) clarified the extent of sulfation (75%) at C-4 and confirmed that sulfation at positions C-2 and C-3 was virtually complete. Estimation of the hydrolysis products (isomaltose, major; alpha-D-glucose, minor) is not restricted to 1H NMR now that the desulfation-enzymolysis methodology has been established; rather, it can be performed using HPLC or GLC (with derivatization).

Catalysis↗
PubMed2005

The effect of sulfate-delta18O upon on-line sulfate-delta34S analysis, and implications for measurements of delta33S and Delta33S.

On-line delta34S analysis of sulfate using an elemental analyzer has a number of advantages vs. conventional off-line techniques, such as ease of operation, rapidity, and the requirement for small amounts of material. Although the analyses are performed by converting sulfate into SO2 gas, the effect of sulfate-delta18O composition upon the SO2-delta18O composition and the value of delta66 during elemental analysis, and ultimately the calculated sulfate-delta34S composition, has rarely been addressed. Three BaSO4 samples were prepared with known identical delta34S compositions, but with a wide range of delta18O compositions. delta18O values were shown to range over 40 per thousand, but conventional on-line delta34S analyses verified that the sulfate-delta34S compositions were identical. These results indicate that conventional on-line analysis of sulfate-delta34S is unaffected by the value of sulfate-delta18O, and suggest that sulfide-delta34S standards can be used to calibrate sulfate-delta34S analyses (and vice versa). Moreover, these results suggest that it may be possible to use on-line sulfur isotope analysis of SO2 to measure delta33S and Delta33S in addition to delta34S, as a faster and safer alternative to the SF6 technique currently utilized, and hence promote further study of mass-independent sulfur isotope fractionation effects.

Environmental Monitoring↗
PubMed1993

Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate.

The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. On a mass basis, the effect of both heparin and oligosaccharide are equivalent whereas on a molar basis, heparin, which contains about seven hexasaccharide repeats, is more efficient. On the other hand, a pentasulfated tetrasaccharide or di- and tri-sulfated disaccharides are much less effective in potentiating aFGF activity than the hexasaccharide. If the growth factor is pre-incubated with the hexasaccharide at pH 7.2 and then exposed to pH 3.5 the 306/345 nm fluorescence ratio is similar to that of native aFGF indicating that the oligosaccharide stabilizes a native conformation of the protein. Heparan sulfates extracted from various mammalian tissues were also able to potentiate aFGF mitogenic activity. On a mass basis they were in general less efficient than heparin; however, heparan sulfate prepared from medium conditioned by 3T3 fibroblasts is more efficient than heparin both on a mass and molar basis. A highly sulfated oligosaccharide isolated after digestion of pancreas heparan sulfate with heparitinase I is more active than the intact molecule, reaching a potentiating effect equivalent to that of lung heparin, whereas an N-acetylated oligosaccharide isolated after nitrous acid degradation is inactive. These data suggest that the mitogenic activity of aFGF is primarily potentiated by interacting with highly sulfated regions of heparan sulfates chains.

Animals↗
PubMed1978

Galactose-6-sulfatase from Actinobacillus sp. IFO-13310 and its action on sulfated oligosaccharides from keratan sulfate.

A 6-sulfatase specific for sugasr of the galactose configuration was purified 81-fold from the crude extract of Actinobacillus sp. IFO-13310. This preparation contained activity towards both N-acetylgalactosamine 6-sulfate and galactose 6-sulfate (relative activity, 2.4 : 1). The enzyme also release inorganic sulfate from the non-reducing galactose 6-sulfate end group of a trisaccharide disulfate prepared from keratan sulfate by sequential degradation with endo-beta-galactosidase, N-acetylglucosamine-6-sulfatase and exo-beta-N-acetylglucosaminidase. In addition, a tetrasaccharide trisulfate bearing the non-reducing N-acetylglucosamine 6-sulfate end group, also enzymatically prepared from keratan sulfate, was degraded to give rise to inorganic sulfate, N-acetylglucosamine and galactose by the sequential action of this enzyme, N-acetylglucosamine-6-sulfatase, exo-beta-N-acetylglucosaminidase and exo-beta-galactosidase (Charonia lampas).

Acetylgalactosamine↗
PubMed1980

Metabolism of sulfated glycosaminoglycans in rat hepatocytes. Synthesis of heparan sulfate and distribution into cellular and extracellular pools.

Primary cultures of rat hepatocytes grown in a serum-free medium supplemented with [35S]sulfate synthesize 35S-labelled glycosaminoglycans at an almost constant rate for 58 h. Approx. 57% of the newly synthesized 35S-labelled glycosaminoglycans remain within the hepatocytes, approx. 30% become associated with the cell surface and only 13% are secreted into the medium. The amount of cell-surface-associated 35S-labelled glycosaminoglycans became constant within 36 h, whereas no equilibrium was reached in the intra- and extracellular pool. During a 24 h chase more than 50% of the intracellular and cell-surface-associated 35S-labelled glycosaminoglycans disappears, more than 80% of this material is degraded and radioactivity is recovered as inorganic sulfate. A minor part is released into the medium in a macromolecular form. Heparan sulfate accounts for more than 95% of the 35S-labelled glycosaminoglycans in each of the three pools. It is distinguished from heparan sulfates from other sources by the presence of unsubstituted glucosamine residues. In all three pools, heparan sulfate chains of mean molecular weights between 24 000 and 30 000 are part of an alkali labile proteoglycan. Intra- and extracellularly, however, part of the heparan sulfate appears to have little, if any, protein attached. Hepatocytes contain heparan sulfate-degrading endoglycosidase activity, which may contribute to the variation of molecular weights observed for the heparan sulfate.

Animals↗