Determination of 24 Variously Sulfated Galactosaminoglycan- and Hyaluronan-Derived Disaccharides by High-Performance Liquid Chromatography

Karamanos, Nikos K.; Syrokou, Alexandra; Vanky, Peter; Nurminen, M.; Hjerpe, Anders

doi:10.1006/abio.1994.1396

Cited by 145 publications

(94 citation statements)

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“…It is unclear whether this represents a variant form of the putative cytoadherence molecule P. fakiparurn erythrocyte membrane protein 1 (31), but multiple ligands on the IEs are thought to mediate endothelial cell adherence in vitro (32), and more than one may be expressed simultaneously (10 The marked difference in inhibition of binding by CSA compared with CSB or CSC was surprising. The sulfation pattern and the proportions of glucuronic acid and its epimer iduronic acid in CS chains may be very variable (22). The porcine rib cartilage CSA used contains predominantly 4-sulfated N-acetylgalactosamine and approximately equal amounts of glucuronic acid and iduronic acid (22), whereas CSB contains a low proportion of glucuronic acid, and N-acetylgalactosamine residues in CSC are predominantly 6-sulfated.…”

Section: Discussionmentioning

confidence: 99%

“…The sulfation pattern and the proportions of glucuronic acid and its epimer iduronic acid in CS chains may be very variable (22). The porcine rib cartilage CSA used contains predominantly 4-sulfated N-acetylgalactosamine and approximately equal amounts of glucuronic acid and iduronic acid (22), whereas CSB contains a low proportion of glucuronic acid, and N-acetylgalactosamine residues in CSC are predominantly 6-sulfated. Although the current study did not elucidate the specific oligosaccharide motif that supports binding to the ligand on IEs, it appears to involve structures present in CSA that occur infrequently in the CSB or CSC preparations used.…”

Section: Discussionmentioning

confidence: 99%

“…The CSA used (from porcine rib cartilage) is composed of predominantly 4-sulfated N-acetylgalactosamine and approximately equal amounts of glucuronic acid and iduronic acid (22). CSA significantly impaired binding of FAF-EA8CHO5 to K1 CHO cells at 10/~g/ml (99.2 _+ 0.2%) and 1/~g/ml (72.5 _+ 3.8%).…”

Section: Selection For Binding To Clio Cells Selects For Binding To Cmentioning

confidence: 99%

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Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes.

Rogerson

Chaiyaroj

et al. 1995

The Journal of Experimental Medicine

319

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SltlmlilaryAdherence of Plasmodium fakiparum-infected erythrocytes to cerebral postcapillary venular endothelium is believed to be a critical step in the development of cerebral malaria. Some of the possible receptors mediating adherence have been identified, but the process of adherence in vivo is poorly understood. We investigated the role of carbohydrate ligands in adherence, and we identified chondroitin sulfate (CS) as a specific receptor for P. falciparum-infected erythrocytes.Parasitized cells bound to Chinese hamster ovary (CHO) cells and C32 melanoma cells in a chondroitin sulfate-dependent manner, whereas glycosylation mutants lacking chondroitin sulfate A (CSA) supported little or no binding. Chondroitinase treatment of wild-type CHO cells reduced binding by up to 90%. Soluble CSA inhibited binding to CHO cells by 99.2 _+ 0.2% at 10 mg/ml and by 72.5 _+ 3.8% at 1 mg/ml, whereas a range of other glycosaminoglycans such as heparan sulfate had no effect. Parasite lines selected for increased binding to CHO cells and most patient isolates bound specifically to immobilized CSA. We conclude that P. falciparum can express or expose proteins at the surface of the infected erythrocyte that mediate specific binding to CSA. This mechanism of adherence may contribute to the pathogenesis of P. J~l-ciparum malaria, but has wider implications as an example of an infectious agent with the capacity to bind specifically to cell-associated or immobilized CS.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Selection For Binding To Clio Cells Selects For Binding To Cmentioning

confidence: 99%

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Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes.

Rogerson

Chaiyaroj

et al. 1995

The Journal of Experimental Medicine

319

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“…Chondroitin sulfate proteoglycans bind significant amounts of water, which allows protection and cushioning of surrounding structures, and limit the freedom of diffusion of other macromolecules. Chondroitin sulfate is cleaved by hyaluronate lyase only at regions with certain sulfation patterns (78,93,123). Sulfation patterns of glycosaminoglycans (GAGs) appear to be critical for their biological function.…”

Section: Hyaluronanmentioning

confidence: 99%

Pneumococcal Virulence Factors: Structure and Function

Jedrzejas

2001

Microbiol Mol Biol Rev

411

354

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The overall goal for this review is to summarize the current body of knowledge about the structure and function of major known antigens of Streptococcus pneumoniae, a major gram-positive bacterial pathogen of humans. This information is then related to the role of these proteins in pneumococcal pathogenesis and in the development of new vaccines and/or other antimicrobial agents. S. pneumoniae is the most common cause of fatal community-acquired pneumonia in the elderly and is also one of the most common causes of middle ear infections and meningitis in children. The present vaccine for the pneumococcus consists of a mixture of 23 different capsular polysaccharides. While this vaccine is very effective in young adults, who are normally at low risk of serious disease, it is only about 60% effective in the elderly. In children younger than 2 years the vaccine is ineffective and is not recommended due to the inability of this age group to mount an antibody response to the pneumococcal polysaccharides. Antimicrobial drugs such as penicillin have diminished the risk from pneumococcal disease. Several pneumococcal proteins including pneumococcal surface proteins A and C, hyaluronate lyase, pneumolysin, autolysin, pneumococcal surface antigen A, choline binding protein A, and two neuraminidase enzymes are being investigated as potential vaccine or drug targets. Essentially all of these antigens have been or are being investigated on a structural level in addition to being characterized biochemically. Recently, three-dimensional structures for hyaluronate lyase and pneumococcal surface antigen A became available from X-ray crystallography determinations. Also, modeling studies based on biophysical measurements provided more information about the structures of pneumolysin and pneumococcal surface protein A. Structural and biochemical studies of these pneumococcal virulence factors have facilitated the development of novel antibiotics or protein antigen-based vaccines as an alternative to polysaccharide-based vaccines for the treatment of pneumococcal disease

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“…Following removal of the chondroitinase -resistant GAGs, i.e., heparan sulphate (HS) and/or keratan sulphate, by ethanol precipitation, aliquots from the supernatant were analysed by ion-suppression HPLC for HA-derived D-disaccharides using radiochemical detection (37).…”

Section: Determination Of Hamentioning

confidence: 99%

Transforming Growth Factor-β as a key molecule triggering the expression of versican isoforms v0 and v1, Hyaluronan Synthase-2 and synthesis of Hyaluronan in Malignant Osteosarcoma cells

Nikitovic

Zafiropoulos

Katonis

et al. 2006

TBMB

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SummaryVersican, a large sized chondroitin-sulphate proteoglycan (PG), and its binding partner, hyaluronan (HA), are extracellular matrix (ECM) components that play an essential role in transformed cell behavior. Expression of certain versican isoforms has been implicated in cell migration and proliferation of cancer cells and, on the other hand, disruption of HA synthesis by inhibiting hyaluronan synthase-2 (HAS2) expression in osteosarcoma cells by suppressing cell proliferation, invasiveness and motility. Considering that growth factors, such as TGF-b, bFGF and PDGF-BB, are important regulators for the expression of the ECM macromolecules, in this study we examined the effect of these growth factors on the expression of the various versican isoforms, HA synthases as well as HA synthesis by MG-63 osteosarcoma cells and normal human osteoblastic periodontal ligament cells (hPDL). Real-time PCR and metabolic labelling followed by fine HPLC analysis coupled to radiochemical detection were the methods utilized. It was found that, contrary to normal hPDL cells, osteosarcoma MG-63 cells do not constitutively express the versican isoforms V0 and V1. Exogenous addition of TGFb2 stimulated the versican transcript levels mainly by forcing osteosarcoma cells to express V1 and V0 isoforms. PDGF-BB and bFGF had only minor effects in these cells. In hPDL cells a strong stimulation of the V3 transcript by all growth factors was observed. TGF-b2 was also the major stimulator of HAS2 isoform expression as well as hyaluronan synthesis in osteosarcoma cells, while PDGF-BB exerted dominant influence on HAS2 isoform expression and hyaluronan biosynthesis by osteoblasts. The obtained results show for the first time that TGF-b2 triggers the malignant phenotype pattern of versican and hyaluronan expression in human osteosarcoma cells and indicate that this growth factor may account for the metastatic potential of these cells. IUBMB Life, 58: 47 -53, 2006

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Determination of 24 Variously Sulfated Galactosaminoglycan- and Hyaluronan-Derived Disaccharides by High-Performance Liquid Chromatography

Cited by 145 publications

References 0 publications

Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes.

Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes.

Pneumococcal Virulence Factors: Structure and Function

Transforming Growth Factor-β as a key molecule triggering the expression of versican isoforms v0 and v1, Hyaluronan Synthase-2 and synthesis of Hyaluronan in Malignant Osteosarcoma cells

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