Heparan sulfates from Swiss mouse 3T3 and SV3T3 cells: O-sulfate difference

Keller, Katharyn L.; Keller, Joseph B.; Moy, James N.

doi:10.1021/bi00552a035

Cited by 63 publications

(42 citation statements)

References 16 publications

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“…For example, an adhesion-deficient BHK cell mutant, although expressing normal HSPG levels, synthesizes HS chains with markedly decreased sulfation and reduced fibronectin affinity in vitro (40). Frequently, there is also a marked reduction in HS sulfation upon cellular transformation (41)(42)(43), which in some cases is paralleled by a reduced ability of both the HS and the cells to adhere to fibronectin (44).…”

Section: Discussionmentioning

confidence: 99%

Elucidation of the Structural Features of Heparan Sulfate Important for Interaction with the Hep-2 Domain of Fibronectin

Lyon¹,

Rushton²,

Askari³

et al. 2000

Journal of Biological Chemistry

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The interaction of fibronectin with cell surface heparan sulfate proteoglycans is important biologically in inducing reorganization of the cytoskeleton and the assembly of focal adhesions. The major heparan sulfatebinding site in fibronectin, which is also implicated in these morphological events, is the COOH-terminal Hep-2 domain. We describe the first extensive study of the structural determinants required for the interaction between heparan sulfate/heparin and Hep-2. It is clear that, in heparan sulfate, there is a very prominent role for N-sulfate groups, as opposed to a relatively small apparent contribution from carboxyl groups. Furthermore, a minimal octasaccharide binding sequence appeared to contain at least two 2-O-sulfated iduronate residues, but no 6-O-sulfate groups. However, affinity was enhanced by the presence of 6-O-sulfates, and the interaction with Hep-2 also increased progressively with oligosaccharide size up to a maximum length of a tetradecasaccharide. This overall specificity is compatible with recent information on the structure of Hep-2

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Section: Discussionmentioning

confidence: 99%

Elucidation of the Structural Features of Heparan Sulfate Important for Interaction with the Hep-2 Domain of Fibronectin

Lyon¹,

Rushton²,

Askari³

et al. 2000

Journal of Biological Chemistry

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“…The HS-GAGs show distinct alterations in sulfation patterns, total chain length, and the number of sulfated domains. A number of earlier studies have indicated malignancy-associated undersulfation of cell surface HS (43)(44)(45). Recent detailed structural analysis has revealed the specific structural changes of HS isolated from human adenoma and carcinoma cells during the colon carcinogenesis (46).…”

Section: Table III Effects Of Gags On the Collagen-induced Cord Formamentioning

confidence: 99%

Structural Requirements of Heparan Sulfate for the Binding to the Tumor-derived Adhesion Factor/Angiomodulin That Induces Cord-like Structures to ECV-304 Human Carcinoma Cells

Kishibe¹,

Yamada²,

Okada³

et al. 2000

Journal of Biological Chemistry

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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).…”

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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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Heparan sulfates from Swiss mouse 3T3 and SV3T3 cells: O-sulfate difference

Cited by 63 publications

References 16 publications

Elucidation of the Structural Features of Heparan Sulfate Important for Interaction with the Hep-2 Domain of Fibronectin

Elucidation of the Structural Features of Heparan Sulfate Important for Interaction with the Hep-2 Domain of Fibronectin

Structural Requirements of Heparan Sulfate for the Binding to the Tumor-derived Adhesion Factor/Angiomodulin That Induces Cord-like Structures to ECV-304 Human Carcinoma Cells

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

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