A transformation-dependent difference in the heparan sulfate associated with the cell surface

Underhill, Charles B.; Keller, Joseph B.

doi:10.1016/0006-291x(75)90708-1

Cited by 107 publications

(48 citation statements)

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“…Thus an alteration in the overall level of heparan sulphate sulphation is almost certainly not a factor in the ECM alterations which are observed in transformed keratinocytes (Brown & Parkinson, 1984;; although we cannot rule out the possibility that changes in the distribution of ester (o) sulphate groups may have occurred, since this would not have been detected by the methods employed here. Furthermore, these results contrast the many other reports of undersulphated heparan sulphates being produced by other types of transformed cells (Underhill & Keller, 1975;Winterbourne & Mora, 1981;Stamatoglou & Keller, 1983;David & van den Berghe, 1983;Robinson et al, 1984).…”

contrasting

confidence: 91%

“…One important factor in this loss of ECM is probably a decrease in the sulphation of heparan sulphate, which has been reported in several systems (Underhill & Keller, 1975;Winterbourne & Mora, 1981; Stamatoglou & Keller, 1983;David & van den Berghe, 1983;Robinson et al, 1984). This decrease in sulphation reduces the affinity of heparan sulphate for fibronectin (Stamatoglou & Keller, 1983;Robinson et al, 1984) and may therefore interfere with the complex interactions between the various glycoprotein and proteoglycan components of the ECM, in which heparan sulphate is thought to play a central role (Gallagher et al, 1986 (Rheinwald, 1980), as previously described (Brown & Parkinson, 1983).…”

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confidence: 85%

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Sulphation and fibronectin-binding properties of heparan sulphate glycosaminoglycans from transformed cultured human keratinocytes

Kw¹

1987

Br J Cancer

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confidence: 91%

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confidence: 85%

Sulphation and fibronectin-binding properties of heparan sulphate glycosaminoglycans from transformed cultured human keratinocytes

Kw¹

1987

Br J Cancer

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“…In numerous reports a change in glycosaminoglycan synthesis upon neoplastic transformation has been described (Underhill & Keller, 1975;Winterbourne & Mora, 1978Keller et al, 1980;Fransson et al, 1982;Underhill & Toole, 1982;Shanley et al, 1983). When analysed for transformation-associated changes, spontaneously transformed MuMG cells that produce invasive tumours in vivo were found to produce basement-membrane heparan sulphate of lower Mr and of lower anionic charge density than the untransformed parental counterpart (David & Van den Berghe, 1983).…”

Section: Vol 248mentioning

confidence: 99%

Basement-membrane heparan sulphate with high affinity for antithrombin synthesized by normal and transformed mouse mammary epithelial cells

Pejler

Gourichon

1987

Biochemical Journal

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Basement-membrane proteoglycans, biosynthetically labelled with [35S]sulphate, were isolated from normal and transformed mouse mammary epithelial cells. Proteoglycans synthesized by normal cells contained mainly heparan sulphate and, in addition, small amounts of chondroitin sulphate chains, whereas transformed cells synthesized a relatively higher proportion of chondroitin sulphate. Polysaccharide chains from transformed cells were of lower average Mr and of lower anionic charge density compared with chains isolated from the untransformed counterparts, confirming results reported previously [David & Van den Berghe (1983) J. Biol. Chem. 258, 7338-7344]. A large proportion of the chains isolated from normal cells bound with high affinity to immobilized antithrombin, and the presence of 3-O-sulphated glucosamine residues, previously identified as unique markers for the antithrombin-binding region of heparin [Lindahl, Bäckström, Thunberg & Leder (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6551-6555], could be demonstrated. A significantly lower proportion of the chains derived from transformed cells bound with high affinity to antithrombin, and a corresponding decrease in the amount of incorporated 3-O-sulphate was observed.

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“…(a) mAb 48.7 affinity-purified proteoglycan (CSPG) J (11,20,27,33,34,55) and viral transformation can block proteoglycan synthesis (43). There is evidence that neoplastic cells can synthesize proteoglycans that are chemically modified, e.g., undersulfated (30,40,56,63), or structurally altered, e.g., keratan sulfate glycosaminoglycan chains (39,44). Such modified proteoglycans may account for the fact that transformed ceils fail to assemble a pericellular matrix as compared with their normal counterparts (16,21,25,57,58).…”

mentioning

confidence: 99%

The melanoma proteoglycan: restricted expression on microspikes, a specific microdomain of the cell surface.

Garrigues

Lark

Lara

et al. 1986

The Journal of Cell Biology

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Abstract.A cell surface chondroitin sulfate proteoglycan associated with human melanomas and defined by mAb's F24.47 and 48.7 has been characterized biochemically and localized by indirect immunogold electron microscopy. These antibodies recognize distinct epitopes on the intact proteoglycan. In addition, mAb 48.7 also recognizes an epitope on a 250,000-D glycoprotein and is therefore similar to antibody 9.2.27 (described by Bumol, T. E, and R. A. Reisfeld, 1982, Proc. Natl. Acad. Sci. USA., 79:1245-1249. Furthermore, it was shown that the glycosaminoglycan chains released by alkaline borohydride treatment of the proteoglycan recognized by mAb 48.7 had a size of '~60,000 D. Since the intact proteoglycan was estimated to be 420,000 D, there are probably three chondroitin sulfate chains attached to the 250,000-D core glycoprotein. Furthermore, an oligosaccharide fraction containing 42 % of the 3H activity (glucosamine as precursor) was isolated.Immunolocalization studies using whole-mount electron microscopy revealed that the chondroitin sulfate proteoglycan was present almost exclusively on microspikes, a microdomain of the melanoma cell surface. These processes were present as 1-2-~tm structures on the upper cell surface and as longer (up to 20 ~tm) structures at the cell periphery. Peripheral microspikes were involved in the initial interactions between adjacent cells and formed complex footpads that made contact with the substratum. Immunogold-labeled cells were also thin sectioned and the specific localization of the chondroitin sulfate proteoglycan antigen was quantitated. The data confirmed the results of wholemount microscopy and demonstrated a statistically significant association of the antigen with the microspike processes as compared with other areas of the cell surface. By using two different mAb's (48.7 and F24.47) that recognize epitopes on either the core glycoprotein or the intact proteoglycan, respectively, we have demonstrated that both molecules have the same restricted distribution at the cell surface. The specific localization of the antigen to microspikes at the cell surface suggests it may play a role in cell-cell contact and cell-substratum adhesion, which could be important in the metastatic process.

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A transformation-dependent difference in the heparan sulfate associated with the cell surface

Cited by 107 publications

References 11 publications

Sulphation and fibronectin-binding properties of heparan sulphate glycosaminoglycans from transformed cultured human keratinocytes

Sulphation and fibronectin-binding properties of heparan sulphate glycosaminoglycans from transformed cultured human keratinocytes

Basement-membrane heparan sulphate with high affinity for antithrombin synthesized by normal and transformed mouse mammary epithelial cells

The melanoma proteoglycan: restricted expression on microspikes, a specific microdomain of the cell surface.

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