Sulfate de dermatane et sulfate d'heparitine du foie de boeuf

Gregoire, Paul E.; Dictus-Vermeulen, C.; Ameryckx, Jean Pierre

doi:10.1016/0304-4165(72)90245-0

Cited by 20 publications

(6 citation statements)

References 29 publications

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“…the polysaccharide side chains of proteoglycans, in liver is low (1)(2)(3)(4), but they are metabolized at a rather high rate (5,6). Heparan sulfate, the preponderant type of glycosaminoglycan in liver (7,8) occurs predominantly in the microenvironment of the cell, i.e. the external surface of the hepatocyte (6,(9)(10)(11)(12) and piay there control the exchange of metabolites, ions, fluids, and wateir, exert some effects on hepatocellular proliferation and may regulate the accessibility of cell surface receptors (13-15).…”

Section: Introductionmentioning

confidence: 99%

The Sequence of Changes in the Biosynthesis of Sulfated Glycosaminoglycans in Acute, Experimental Liver Disease

Gressner¹,

Heinrigs²,

Grouls³

1982

CCLM

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The incorporation of [ 35 S]sulfate into total and specific glycosaminoglycans of the liver of rats injured acutely by a singie intraperitoneal dose of either jD-galactosamine (700 and 350 mg/kg body weight, respectively) or thioacetamide (100 mg/kg body weight) was studied in vivo and in liver slices. Regardless of the chemical nature of the hepatotoxic agent and its mechanism of action the incorporation of isotope in vivo is changed biphasically: a rapidly occurring and strong Inhibition is followed by pronounced elevation in later stages of injury. In contrast to the dose-dependent Inhibition of heparan sulfate formation the production of chondroitin sulfate and dermatan sulfate is only slightly and for a rather short period of time diminished. The synthesis of the latter glycosaminoglycans is stimulated 3 to 4 fold 8 to 24 h after onset of liver damage, fhat of heparan sulfate about 2 fold. Impaired synthesis of heparan sulfate occurs before the elevation of the activities of aspartate aminotransferase, alanine aminotransferase, and leucine arylamidase in serum. The specific radioactivity of 3'-phosphoadenosine-5'-phosphosulfate remains nearly constant in galactosamine-damaged livers. Similar time-dependent changes of [ 3S S]sulfate incorporation into heparan sulfate, chondroitin sulfate and dermatan sulfate were measured in slices from livers injured in vivo for various times with -D-galactosamine or thioacetamide. Neither serum from normal nor galactosaniine-treated rats influences the total amount and the pattern of glycosaminoglycans synthesized in normal or injured liver slices. Hepatic glycosaminoglycan formation of 3.5 and 33 months old rats responds quantitatively and qualitatively in a simüar way to £>-galactosamine; 50% Inhibition is reached with about 80 mg/kg of the hepatotoxin. The Inhibition of heparan sulfate synthesis in early injured livers could not be reversed by addition of p-nitrophenyl-/3-Z)-xylopyranoside to the medium (final concentration l mmol/1), but in rats treated with diethyldithiocarbamate or the flavonoid (+)-cianidanol-3, prior to injection of Z)-galactosamine, a partial restoration of the diminished synthesis of total glycosaminoglycans and of heparan sulfate is achieved. Die Sequenz der Änderungen der Biosynthese sulfatierter Glykosaminoglykane bei akuten, experimentellen LebererkrankungenZusammenfassung: Der Einbau von [ 3 *S]Sulfat in die gesamten und spezifischen Glykosaminoglykane der Leber von Ratten, die akut geschädigt wurden durch eine intraperitoneale Einzelinjektion von entweder Z)-Galaktosamin (700 mg/kg oder 350 mg/kg Körpergewicht) oder Thioacetamid (100 mg/kg), wurde in vivo und in Leberschnitten untersucht. Ungeachtet der chemischen Natur der hepatotoxischen Substanz und ihres Wirkungsmechanismus kommt es zu einer biphasischen Änderung des Isotopeinbaues: eine unmittelbar auftretende und starke Hemmung wird gefolgt von einer ausgeprägten Erhöhung in späteren Stadien der Schädigung. Im Gegensatz zu der dosisabhängigen Hemmung der Heparansulfatbildung ist die Pr...

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Section: Introductionmentioning

confidence: 99%

The Sequence of Changes in the Biosynthesis of Sulfated Glycosaminoglycans in Acute, Experimental Liver Disease

Gressner¹,

Heinrigs²,

Grouls³

1982

CCLM

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“…Oldberg et al (1979) have recently isolated and characterized a heparan sulphate proteoglycan from a liver plasma-membrane preparation. Even though other acid glycosaminoglycans, such' as chondroitin 4-and 6-sulphate, dermatan sulphate and hyaluronic acid, are reported to occur in liver (Delbriick, 1968;Gregoire et al, 1972;Suzuki et al, 1976;Dietrich et al, 1976), primary cultures of hepatocytes synthesize predominantly f Present address: Department of Biochemistry, University of Kerala, Trivandrum, India. heparan sulphate (Oldberg et al, 1977). Recent studies from this laboratory (Prinz et al, 1980) showed that freshly isolated rat hepatocytes maintained in culture in a serum-free medium synthesize almost exclusively heparan sulphate at an almost constant rate for at least 3 days.…”

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Regulation of heparan sulphate metabolism by adenosine 3′:5′-cyclic monophosphate in hepatocytes in culture

Sudhakaran¹,

Sinn

Figura

1980

Biochemical Journal

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Freshly isolated rat hepatocytes maintained as monolayers in a serum-free medium synthesize sulphated glycosaminoglycans, most of which behave as heparan sulphate and are mainly distributed into intracellular compartments. Cyclic AMP, dibutyryl cyclic AMP, glucagon, noradrenaline, prostaglandin E(1), and theophylline, all drugs and hormones known to increase intracellular cyclic AMP concentrations, decreased the incorporation of (35)SO(4) (2-) into heparan sulphate of intra-, extra- and peri-cellular pools. The inhibition mediated by dibutyryl cyclic AMP was dose-dependent and observed as early as 2h after exposure to the drug. In the presence of 1mm-dibutyryl cyclic AMP, incorporation of (35)SO(4) (2-) or [(14)C]glucosamine into heparan sulphate was decreased to 40-50%, suggesting that dibutyryl cyclic AMP interfered with the synthesis of heparan sulphate. This was further supported by pulse-chase experiments, where dibutyryl cyclic AMP had no effect on the degradation of sulphated glycosaminoglycans. Heparan sulphates synthesized and secreted into the extracellular pool in the presence of dibutyryl cyclic AMP were smaller in size, whereas the degree of sulphation and molecular size of the heparan sulphate chains released by beta-elimination from these proteoglycans were not different from control values. In the presence of 1mm-cycloheximide, (35)SO(4) (2-) incorporation was decreased to 5%. Addition of p-nitrophenyl beta-d-xyloside, an artificial acceptor of glycosaminoglycan chain synthesis, enhanced this incorporation to 18%. Dibutyryl cyclic AMP did not have any inhibitory effect on the synthesis of chains initiated on p-nitrophenyl beta-d-xylosides. Incorporation of [(3)H]serine into heparan sulphate was not affected by dibutyryl cyclic AMP, whereas the degree of substitution of serine residues with heparan sulphate chains was less in heparan sulphate synthesized in the presence of dibutyryl cyclic AMP, suggesting that cyclic AMP exerts its effect on the metabolism of sulphated glycosaminoglycans by affecting the transfer of xylose on to the protein core.

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“…CS-D and CS-E have been found in human rib cartilage in small proportions (13). Another disaccharide unit, IdceAGalNAc(4S,6S), has also been identified in dermatan sulfate (DS) from hagfish notochord (14), mammalian liver (15), and bovine kidney (16). This type of DS is designated as DS-E in this article.…”

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Novel Tetrasaccharides Isolated from Squid Cartilage Chondroitin Sulfate E Contain Unusual Sulfated Disaccharide Units GlcA(3-O-sulfate)β1–3GalNAc(6-O-sulfate) or GlcA(3-O-sulfate)β1–3GalNAc(4,6-O-disulfate)

Kinoshita

Yamada

Haslam

et al. 1997

Journal of Biological Chemistry

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We previously isolated novel tetrasaccharides containing 3-O-sulfated glucuronic acid from king crab cartilage chondroitin sulfate K and demonstrated that the disaccharide units containing 3-O-sulfated glucuronic acid were decomposed by chondroitinase ABC digestion (Sugahara, K., Tanaka, Y., Yamada, S., Seno, N., Kitagawa, H., Haslam, S. M., Morris, H. R., and Dell, A. (1996) J. Biol. Chem. 271, 26745-26754). The findings indicated the necessity to re-evaluate the disaccharide compositions of chondroitin sulfate preparations purified from other biological sources and analyzed using the above enzyme. In this study, to evaluate squid cartilage chondroitin sulfate E a series of even-numbered oligosaccharides were isolated after exhaustive digestion with sheep testicular hyaluronidase and subsequent fractionation by gel chromatography. The tetrasaccharide fraction was subfractionated by high performance liquid chromatography on an amine-bound silica column. Systematic structural analysis of five major fractions, h, l, m, n, and q, by fast atom bombardment mass spectrometry, enzymatic digestions in conjunction with capillary electrophoresis, and 500-MHz 1 H NMR spectroscopy revealed one disulfated, three trisulfated, and one tetrasulfated tetrasaccharide structure: fraction h, GlcA␤1-3GalNAc(4S)␤1-4GlcA␤1-3GalNAc(4S); fraction l, GlcA-(3S)␤1-3GalNAc(6S)␤1-4GlcA␤1-3GalNAc(4S); fraction m, GlcA(3S)␤1-3GalNAc(4S)␤1-4GlcA␤1-3GalNAc(4S); fraction n, GlcA␤1-3GalNAc(4S,6S)␤1-4GlcA␤1-3Gal-NAc(4S); and fraction q, GlcA(3S)␤1-3GalNAc(4S,6S)␤1-4GlcA␤1-3GalNAc(4S), where 3S, 4S, and 6S represent 3-O-, 4-O-and 6-O-sulfate, respectively. The structures found in fractions h and m as well as the unsaturated counterpart of that found in fraction n have been reported, whereas those in fractions l and q are novel in that they contained unusual disulfated and trisulfated disaccharide units where GlcA(3S) is directly linked to GalNAc(6S) and GalNAc(4S,6S), respectively. These novel tetrasaccharide sequences are distinct from those found in other chondroitin sulfate isoforms and may play key roles in the biological functions and activities of chondroitin sulfate E not only from squid cartilage but also from mammalian cells and tissues.

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Sulfate de dermatane et sulfate d'heparitine du foie de boeuf

Cited by 20 publications

References 29 publications

The Sequence of Changes in the Biosynthesis of Sulfated Glycosaminoglycans in Acute, Experimental Liver Disease

The Sequence of Changes in the Biosynthesis of Sulfated Glycosaminoglycans in Acute, Experimental Liver Disease

Regulation of heparan sulphate metabolism by adenosine 3′:5′-cyclic monophosphate in hepatocytes in culture

Novel Tetrasaccharides Isolated from Squid Cartilage Chondroitin Sulfate E Contain Unusual Sulfated Disaccharide Units GlcA(3-O-sulfate)β1–3GalNAc(6-O-sulfate) or GlcA(3-O-sulfate)β1–3GalNAc(4,6-O-disulfate)

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