Heparan Sulfate Proteoglycans as Adhesive and Anti-invasive Molecules

Liu, Wei; Litwack, E. David; Stanley, Michelle J.; Langford, J. Kevin; Lander, Arthur D.; Sanderson, Ralph D.

doi:10.1074/jbc.273.35.22825

Cited by 158 publications

(142 citation statements)

References 59 publications

(44 reference statements)

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“…Several extracellular matrix proteins, including fibronectin, collagen, thrombospondin, laminin, and tenascin, interact with cell surface proteoglycans and are thought to modulate cell adhesion through this interaction (2,21,33,45,50,82). In the present study, we have shown that vitronectin also supports proteoglycan dependent cell adhesion.…”

Section: Discussionsupporting

confidence: 57%

“…Syndecans have been shown to mediate adhesion to other matrix molecules including collagen, fibronectin and laminin (21,22,45,82). To determine whether vitronectin is a ligand for syndecan, ARH-77 cells, each transfected with the cDNA for one of the syndecan family members (syndecans-1, -2, -4) or for a glypican-family member (glypican-1) (42,44,45), were used in cell adhesion assays in order to distinguish which class of proteoglycans can mediate adhesion to vitronectin's heparin binding domain. Figure 5 shows that cells expressing either syndecan-1 or -4 could adhere to wells coated with GST-VnHBD.…”

Section: Vitronectin's Basic Domain Mediates Syndecan Dependent Cell mentioning

confidence: 99%

“…The ARH-77 B lymphoid cell line, stably transfected with either syndecan-1, -2, or -4; a heparan sulfate deficient form of syndecan-1 (TDM); glypican-1, or vector alone (Neo) have been described previously (42,44,45 …”

Section: Cell Culturementioning

confidence: 99%

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Vitronectin's Basic Domain is a Syndecan Ligand which Functionsin transto Regulate Vitronectin Turnover

Wilkins-Port

Sanderson²,

Tominna-Sebald³

et al. 2003

Cell Communication & Adhesion

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During the process of tissue remodeling, vitronectin (Vn) is deposited in the extracellular matrix where it plays a key role in the regulation of pericellular proteolysis and cell motility. In previous studies we have shown that extracellular levels of vitronectin are controlled by receptormediated endocytosis and that this process is dependent upon vitronectin binding to sulfated proteoglycans. We have now identified vitronectin's 12 amino acid "basic domain" which is contained within the larger 40 amino acid heparin binding domain, as a syndecan binding site. Recombinant vitronectins representing wild type vitronectin (rVn) and vitronectin with the basic domain deleted (rVn 347-358) were prepared in a baculoviral expression system. The rVn as well as a glutathione S-transferase (GST) fusion protein, consisting of vitronectin's 40 amino acid heparin binding domain (GST-VnHBD), exhibited dose dependent binding to HT-1080 cell surfaces, which was attenuated following deletion of the basic domain. In addition, GST-VnHBD supported both HT-1080 and dermal fibroblast cell adhesion, which was also dependent upon the basic domain. Similarly, ARH-77 cells transfected with syndecans -1, -2, or -4, but not Glypican-1, adhered to GST-VnHBD coated wells, while adhesion of these same cells was lost following deletion of the basic domain. HT-1080 cells were unable to degrade rVn 347-358. Degradation of rVn 347-358 was completely recovered in the presence of GST-VnHBD but not in the presence of GST-VnHBD 347-358. These results indicate that turnover of soluble vitronectin requires ligation of vitronectin's basic domain and that this binding event can work in trans to regulate vitronectin degradation.

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Section: Discussionsupporting

confidence: 57%

Section: Vitronectin's Basic Domain Mediates Syndecan Dependent Cell mentioning

confidence: 99%

See 1 more Smart Citation

Vitronectin's Basic Domain is a Syndecan Ligand which Functionsin transto Regulate Vitronectin Turnover

Wilkins-Port

Sanderson²,

Tominna-Sebald³

et al. 2003

Cell Communication & Adhesion

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“…5 Among these proteins involved in cell adhesion mechanisms are syndecans, a four-member family of heparan sulphate proteoglycans expressed on adherent and non-adherent cells. 6 Syndecans have been evaluated in tumour progression owing to their function in cell proliferation, cell-cell and cell-matrix adhesion, cell motility and invasiveness. These heparan sulphate proteoglycans are expressed in several cell types.…”

Section: Introductionmentioning

confidence: 99%

“…Syndecan-1 is expressed mainly in epithelial cells, whereas syndecan-2 has been described in mesenchymal cells. 6 Recent evidence indicates that the pattern of syndecan-1 expression is altered in a number of types of carcinomas, and down-or upregulation of syndecan-1 has been associated with progression and a poor prognosis. 7 In prostate cancer, the expression of syndecan-1 has been investigated with contradictory results.…”

Section: Introductionmentioning

confidence: 99%

Altered expression patterns of syndecan-1 and -2 predict biochemical recurrence in prostate cancer

Ledezma¹,

Cifuentes²,

M³

et al. 2011

Asian J Androl

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The clinical features of prostate cancer do not provide an accurate determination of patients undergoing biochemical relapse and are therefore not suitable as indicators of prognosis for recurrence. New molecular markers are needed for proper pre-treatment risk stratification of patients. Our aim was to assess the value of altered expression of syndecan-1 and -2 as a marker for predicting biochemical relapse in patients with clinically localized prostate cancer treated by radical prostatectomy. The expression of syndecan-1 and -2 was examined by immunohistochemical staining in a series of 60 paraffin-embedded tissue samples from patients with localized prostate cancer. Ten specimens from patients with benign prostatic hyperplasia were used as non-malignant controls. Semiquantitative analysis was performed to evaluate the staining patterns. To investigate the prognostic value, Kaplan-Meier survival curves were performed and compared by a log-rank test. In benign samples, syndecan-1 was expressed in basal and secretory epithelial cells with basolateral membrane localisation, whereas syndecan-2 was expressed preferentially in basal cells. In prostate cancer samples, the expression patterns of both syndecans shifted to granular-cytoplasmic localisation. Survival analysis showed a significant difference (P,0.05) between normal and altered expression of syndecan-1 and -2 in free prostate-specific antigen recurrence survival curves. These data suggest that the expression of syndecan-1 and -2 can be used as a prognostic marker for patients with clinically localized prostate cancer, improving the prostate-specific antigen recurrence risk stratification.

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Identification of cell-binding site of angiomodulin (AGM/TAF/Mac25) that interacts with heparan sulfates on cell surface

et al. 1999

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Angiomodulin (AGM/TAF/mac25) is a 30-kDa glycoprotein that was identified as an integrin-independent cell adhesion protein secreted by human bladder carcinoma cells. AGM is highly accumulated in small blood vessels of tumor tissues. In the present study, we attempted to identify the cell surface receptor and the cell-binding site of AGM using ECV-304 human vascular endothelial cells and BALB/c3T3 mouse fibroblasts. Heparin, heparan sulfate, and dextran sulfate, but not chondroitin sulfate, inhibited both adhesion of the two cell lines to AGM-coated plates and binding of AGM to these cells. Treatment of cells with heparinase, but not chondroitinase, inhibited both cell adhesion to AGM and AGM binding to cells. These results strongly suggested that heparan sulfates are the major receptor for AGM. Furthermore, we determined a 20-amino acid sequence within AGM molecule as its major cell-binding site. The synthetic peptide for the cell-binding sequence showed cell adhesion activity comparable to that of AGM, and the activity was inhibited by heparin and heparan sulfate. The peptide competitively inhibited cell adhesion to AGM and the binding of AGM to cells. These results indicated that AGM binds to cells through interaction of the identified cell-binding sequence with heparan sulfates on cell surface. It was also found that the heparan sulfate-binding peptide inhibited the formation of capillary tube-like structures of vascular endothelial cells in culture.

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Heparan Sulfate Proteoglycans as Adhesive and Anti-invasive Molecules

Cited by 158 publications

References 59 publications

Vitronectin's Basic Domain is a Syndecan Ligand which Functionsin transto Regulate Vitronectin Turnover

Vitronectin's Basic Domain is a Syndecan Ligand which Functionsin transto Regulate Vitronectin Turnover

Altered expression patterns of syndecan-1 and -2 predict biochemical recurrence in prostate cancer

Identification of cell-binding site of angiomodulin (AGM/TAF/Mac25) that interacts with heparan sulfates on cell surface

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