Action pattern of polysaccharide lyases on glycosaminoglycans

Jandik, Kenneth A.; Gu, Kenan; Linhardt, Robert J.

doi:10.1093/glycob/4.3.289

Cited by 125 publications

(129 citation statements)

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“…This finding supports the evidence that CS B is present on versican, because chondroitinase ABC cleaves all types of CS chains, whereas chondroitinase ACII cleaves all CS chains except CS B (Ref. 44 and data not shown). The mAb 3-B-3, which recognizes stubs with the ⌬Di-6S terminal structure exposed by chondroitinase digestion (45), reacted strongly with chondroitinase ABC-treated versican, indicating that versican contains CS C as well.…”

Section: Figsupporting

confidence: 89%

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Binding of a Large Chondroitin Sulfate/Dermatan Sulfate Proteoglycan, Versican, to L-selectin, P-selectin, and CD44

Kawashima¹,

Hirose²,

Hirose³

et al. 2000

Journal of Biological Chemistry

242

194

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Here we show that a large chondroitin sulfate proteoglycan, versican, derived from a renal adenocarcinoma cell line ACHN, binds L-selectin, P-selectin, and CD44. The binding was mediated by the interaction of the chondroitin sulfate (CS) chain of versican with the carbohydrate-binding domain of L-and P-selectin and CD44. The binding of versican to L-and P-selectin was inhibited by CS B, CS E, and heparan sulfate (HS) but not by any other glycosaminoglycans tested. On the other hand, the binding to CD44 was inhibited by hyaluronic acid, chondroitin (CH), CS A, CS B, CS C, CS D, and CS E but not by HS or keratan sulfate. A crossblocking study indicated that L-and P-selectin recognize close or overlapping sites on versican, whereas CD44 recognizes separate sites. We also show that soluble L-and P-selectin directly bind to immobilized CS B, CS E, and HS and that soluble CD44 directly binds to immobilized hyaluronic acid, CH, and all the CS chains examined. Consistent with these results, structural analysis showed that versican is modified with at least CS B and CS C. Thus, proteoglycans sufficiently modified with the appropriate glycosaminoglycans should be able to bind L-selectin, P-selectin, and/or CD44.

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Section: Figsupporting

confidence: 89%

“…Because this enzyme selectively cleaves CS B (Ref. 44 and data not shown), this result indicated that versican contains CS B. This mAb also reacted with chondroitinase ABC-treated versican but not with chondroitinase ACII-treated versican.…”

Section: Figmentioning

confidence: 72%

Binding of a Large Chondroitin Sulfate/Dermatan Sulfate Proteoglycan, Versican, to L-selectin, P-selectin, and CD44

Kawashima¹,

Hirose²,

Hirose³

et al. 2000

Journal of Biological Chemistry

242

194

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“…Implications for Mode of Action-The structural differences between HL and CL may be correlated to their modes of action, as revealed by kinetic analysis with a variety of substrates (16,(71)(72)(73)76). As mentioned, biochemical data show that HL cleavage of HA, its primary substrate, proceeds via an initial endolytic cleavage, which is followed by rapid exolytic and processive activity, producing solely an unsaturated disaccharide unit as the end degradation product (3,15,27,28).…”

Section: Mechanism Of S Pneumoniae Hyaluronate Lyase Catalysis and Amentioning

confidence: 99%

“…Twisting motions between the two principal domains, revealed by simulated dynamics, also seem to play a role (15,19). Why, therefore, given the overall structural similarity of HL and CL (see Introduction), expected to lead to similar dynamic behavior (15,19,78), and the conserved hydrophobic interactions with substrate does CL not exhibit processive substrate cleavage (76)? One likely explanation lies in the added substrate bulk caused by sulfation of chondroitin.…”

Section: Mechanism Of S Pneumoniae Hyaluronate Lyase Catalysis and Amentioning

confidence: 99%

Structures of Streptococcus pneumoniae Hyaluronate Lyase in Complex with Chondroitin and Chondroitin Sulfate Disaccharides

Rigden

Jedrzejas²

2003

Journal of Biological Chemistry

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Streptococcus pneumoniae hyaluronate lyase is a surface enzyme of this Gram-positive bacterium. The enzyme degrades hyaluronan and chondroitin/chondroitin sulfates by cleaving the ␤1,4-glycosidic linkage between the glycan units of these polymeric substrates. This degradation helps spreading of this bacterial organism throughout the host tissues and facilitates the disease process caused by pneumococci. The mechanism of this degradative process is based on ␤-elimination, is termed proton acceptance and donation, and involves selected residues of a well defined catalytic site of the enzyme. The degradation of hyaluronan alone is thought to proceed through a processive mode of action. The structures of complexes between the enzyme and chondroitin as well as chondroitin sulfate disaccharides allowed for the first detailed insights into these interactions and the mechanism of action on chondroitins. This degradation of chondroitin/chondroitin sulfates is nonprocessive and is selective for the chondroitin sulfates only with certain sulfation patterns. Chondroitin sulfation at the 4-position on the nonreducing site of the linkage to be cleaved or 2-sulfation prevent degradation due to steric clashes with the enzyme. Evolutionary studies suggest that hyaluronate lyases evolved from chondroitin lyases and still retained chondroitin/chondroitin sulfate degradation abilities while being specialized in the degradation of hyaluronan. The more efficient processive degradation mechanism has come to be preferred for the unsulfated substrate hyaluronan.

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“…As heparitinase acts specifically on heparan sulphate (Jandik et al, 1994), this suggests that the active material is a species of heparan sulphate. As the purified material was protease treated before fractionation, and only minimal absorbance at 280 nm was observed around the active fractions, suggesting that little residual protein remained, the activity may lie in the carbohydrate moiety.…”

Section: +mentioning

confidence: 99%

Activation of paracrine growth factors by heparan sulphate induced by glucocorticoid in A549 lung carcinoma cells

Yevdokimova

Freshney²

1997

Br J Cancer

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Summary Alkaline phosphatase, a marker of differentiation in the human alveolar adenocarcinoma cell line A549, is inducible by conditioned medium from lung fibroblasts and by cytokines including oncostatin M and interleukin 6, but only in the presence of a glucocorticoid, dexamethasone. Dexamethasone was shown to induce incorporation of [3H]glucosamine into three fractions of medium and cell trypsinate from subconfluent A549 cells, eluting from DEAE ion-exchange chromatography. The first peak did not correspond to any of the unlabelled glycosaminoglycans and was not characterized further. Induction was seen in two other peaks, corresponding to hyaluronic acid and heparan sulphate. Of these, heparan sulphate, eluting as one well-defined peak (referred to as HS1) and another of lower activity and less well defined (HS2), was selected as the most likely to interact with growth factors and cytokines and was isolated from the eluate, concentrated and desalted, and used in alkaline phosphatase induction experiments in place of dexamethasone. HS1 isolated from the medium (HS1m) of subconfluent A549 cells was shown to replace dexamethasone in induction experiments with fibroblast-conditioned medium, oncostatin M and interleukin 6. HS1 from the cell trypsinate and HS2 from the medium and trypsinate were inactive. As the activity of HS1m could be abolished by heparinase and heparitinase but not by chondroitinase ABC, it was concluded that HS1 m was a fraction of heparan sulphate involved in the regulation of paracrine growth factor activity in lung fibroblast-conditioned medium, and in the regulation of other growth factors with potential roles in the paracrine control of cell differentiation.Keywords: glucocorticoid; heparan sulphate; adenocarcinoma; oncostatin M; interleukin 6; paracrine; fibroblast Differentiation of the mature phenotype in alveolar type II pneumocytes is marked by the production of lipid pulmonary surfactant (PS) and surfactant-associated proteins (Hawgood and Clements, 1990) and by an increase in alkaline phosphatase (AP) activity (Edelson et al, 1988). Perinatal induction of differentiation is mediated by glucocorticoids and a paracrine factor, or factors, from mesenchymally derived cells in the lung (Caniggia et al, 1991). In vitro, the synthesis of pulmonary surfactant and alkaline phosphatase can be induced in A549, a cell line derived from a human lung adenocarcinoma (Giard et al 1972), of reputedly type II cell origin (Lieber et al, 1976), by conditioned medium from lung fibroblasts (CM) (Speirs et al, 1991). Whereas induction of PS synthesis by CM was enhanced by treating the fibroblasts with dexamethasone (DX) before and during the conditioning process, DX was not required for the action of the CM on the A549 cells (Speirs et al, 1991). It is, however, required for the induction of alkaline phosphatase by CM and by several cytokines, such as oncostatin M (OSM), interleukin 6 (IL-6), and interferons a and [3, and by insulin (McCormick et al, 1995;McCormick and Freshney, 1996). OSM has been fou...

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Action pattern of polysaccharide lyases on glycosaminoglycans

Cited by 125 publications

References 0 publications

Binding of a Large Chondroitin Sulfate/Dermatan Sulfate Proteoglycan, Versican, to L-selectin, P-selectin, and CD44

Binding of a Large Chondroitin Sulfate/Dermatan Sulfate Proteoglycan, Versican, to L-selectin, P-selectin, and CD44

Structures of Streptococcus pneumoniae Hyaluronate Lyase in Complex with Chondroitin and Chondroitin Sulfate Disaccharides

Activation of paracrine growth factors by heparan sulphate induced by glucocorticoid in A549 lung carcinoma cells

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