Adhesion of glycosaminoglycan-deficient chinese hamster ovary cell mutants to fibronectin substrata.

LeBaron, Richard G.; Woods, Anne; Johansson, Staffan; Höök, Magnus

doi:10.1083/jcb.106.3.945

Cited by 148 publications

(62 citation statements)

References 35 publications

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“…Evidence that cellsurface heparan sulphate molecules are required for the activity of the peptide was provided by the finding that treatment of the cells with heparinase significantly inhibits peptide-stimulated focal-adhesion formation. Results similar to these were obtained when Chinese-hamster ovary (CHO) cell lines that are genetically deficient in their ability to synthesize heparan sulphate were examined [119]. Wild-type CHO cells adhere to intact fibronectin, to the 105 kDa integrin-binding fragment and to a 31 kDa fragment that contains the heparin-binding domain but lacks the integrin-binding domain.…”

Section: Cell-extracellular Matrix Adhesionmentioning

confidence: 65%

Syndecans: multifunctional cell-surface co-receptors

Carey

1997

Biochemical Journal

621

497

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This review will summarize our current state of knowledge of the structure, biochemical properties and functions of syndecans, a family of transmembrane heparan sulphate proteoglycans. Syndecans bind a variety of extracellular ligands via their covalently attached heparan sulphate chains. Syndecans have been proposed to play a role in a variety of cellular functions, including cell proliferation and cell–matrix and cell–cell adhesion. Syndecan expression is highly regulated and is cell-type- and developmental-stage-specific. The main function of syndecans appears to be to modulate the ligand-dependent activation of primary signalling receptors at the cell surface. Principal functions of the syndecan core proteins are to target the heparan sulphate chains to the appropriate plasma-membrane compartment and to interact with components of the actin-based cytoskeleton. Several functions of the syndecans, including syndecan oligomerization and actin cytoskeleton association, have been localized to specific structural domains of syndecan core proteins.

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Section: Cell-extracellular Matrix Adhesionmentioning

confidence: 65%

Syndecans: multifunctional cell-surface co-receptors

Carey

1997

Biochemical Journal

621

497

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“…Although less well understood, fibronectin heparin-binding domains also appear to interact with glycosaminoglycans on cell surface proteoglycans to augment the interaction of cells with fibronectin (Bultmann et al, 1998;Christopher et al, 1997;Hocking et al, 1994;McDonald et al, 1987;Schwarzbauer, 1991;Whiteford et al, 2007;Woods et al, 1988). Cells that lack glycosaminoglycan synthesis cannot adhere normally to fibronectin or establish a fibronectin matrix (Chung and Erickson, 1997;LeBaron et al, 1988). Dominant-negative syndecan 2 (Sdc2), a transmembrane heparin sulfate proteoglycan, blocks fibronectin fibrillogenesis in CHO cells (Klass et al, 2000) and in Xenopus animal cap ectoderm (Kramer and Yost, 2002).…”

Section: Introductionmentioning

confidence: 99%

Extra-embryonic syndecan 2 regulates organ primordia migration and fibrillogenesis throughout the zebrafish embryo

Arrington

Yost

2009

Development

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One of the first steps in zebrafish heart and gut organogenesis is the migration of bilateral primordia to the midline to form cardiac and gut tubes. The mechanisms that regulate this process are poorly understood. Here we show that the proteoglycan syndecan 2 (Sdc2) expressed in the extra-embryonic yolk syncytial layer (YSL) acts locally at the YSL-embryo interface to direct organ primordia migration, and is required for fibronectin and laminin matrix assembly throughout the embryo. Surprisingly, neither endogenous nor exogenous sdc2 expressed in embryonic cells can compensate for knockdown of sdc2 in the YSL, indicating that Sdc2 expressed in extra-embryonic tissues is functionally distinct from Sdc2 in embryonic cells. The effects of sdc2 knockdown in the YSL can be rescued by extra-embryonic Sdc2 lacking an extracellular proteolytic cleavage (shedding) site, but not by extra-embryonic Sdc2 lacking extracellular glycosaminoglycan (GAG) addition sites, suggesting that distinct GAG chains on extra-embryonic Sdc2 regulate extracellular matrix assembly, cell migration and epithelial morphogenesis of multiple organ systems throughout the embryo.

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“…The latter plays biological roles in cell recognition (1), cell adhesion (2,3), developmental regulation of neural tissues (4), and as receptor for endocytosis (5), basic fibroblast growth factor (6 -8), and viruses (9), whereas heparin is involved in blood clotting (10). Heparin and heparan sulfate also occur in different tissues, the latter being present in virtually all mammalian ones, whereas heparin is restricted to connective tissue mast cells (11).…”

mentioning

confidence: 99%

The Putative Heparin-specific N-AcetylglucosaminylN-Deacetylase/N-Sulfotransferase Also Occurs in Non-heparin-producing Cells

Toma¹,

Berninsone

Hirschberg

1998

Journal of Biological Chemistry

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N-Deacetylation and N-sulfation of N-acetylglucosamine of heparin and heparan sulfate are hypothesized to be mediated by different tissue-specific N-acetylglucosaminyl N-deacetylases/N-sulfotransferases, which in turn lead to the higher L-iduronic acid and sulfate content of heparin versus heparan sulfate. Furthermore, the putative heparin-specific N-acetylglucosaminyl Ndeacetylase/N-sulfotransferase has been reported to require auxiliary proteins for its N-acetylglucosaminyl Ndeacetylase activity in vivo based on its requirement of polycations in vitro. We have now found that cells derived from embryonic bovine trachea, a tissue that does not synthesize heparin, has a N-acetylglucosaminyl Ndeacetylase/N-sulfotransferase, which has 95% amino acid sequence identity to the above enzyme postulated to be involved in the biosynthesis of heparin. Both enzymes also have very similar affinity for their substrates. The trachea enzyme does not require additional effectors for its N-acetylglucosaminyl N-deacetylase activity in vitro even though its biochemical characteristics are virtually the same as the enzyme previously isolated from cells of a heparin-producing mastocytoma tumor. The trachea enzyme, which is encoded by an abundant 4.6-kilobase mRNA, like mastocytoma cells, has 70% amino acid sequence identity with the corresponding enzyme from rat liver postulated to participate in the biosynthesis of heparan sulfate. Heparan sulfate synthesized by trachea cells has a higher content of sulfated iduronic acid than from other tissues. Together, the above results strongly suggest that the above enzymes from mastocytoma, liver, and trachea, per se, are not solely responsible for the selective tissue-specific synthesis of heparin or heparan sulfate; more likely cellular factors, additional enzymes, and availability of substrates in the Golgi lumen also play important roles in the differential synthesis of the above proteoglycans.Heparan sulfate and heparin are proteoglycans with sulfated glycosaminoglycans of alternating glucosamine and uronic acid; heparin has a higher content of iduronic acid and sulfate than heparan sulfate. The latter plays biological roles in cell recognition (1), cell adhesion (2, 3), developmental regulation of neural tissues (4), and as receptor for endocytosis (5), basic fibroblast growth factor (6 -8), and viruses (9), whereas heparin is involved in blood clotting (10). Heparin and heparan sulfate also occur in different tissues, the latter being present in virtually all mammalian ones, whereas heparin is restricted to connective tissue mast cells (11). Nevertheless, they appear to share biosynthetic pathways, beginning with the polymerization of glucuronic acid and N-acetylglucosamine, followed by the N-deacetylation and N-sulfation of N-acetylglucosamine, subsequent epimerization of glucuronic acid to L-iduronic acid, 2-O-sulfation of this latter sugar and 6-O-sulfation of glucosamine (12). Heparin, in addition, undergoes 3-O-sulfation of this latter sugar.Up to now, proteins from rat liver (13,...

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Adhesion of glycosaminoglycan-deficient chinese hamster ovary cell mutants to fibronectin substrata.

Cited by 148 publications

References 35 publications

Syndecans: multifunctional cell-surface co-receptors

Syndecans: multifunctional cell-surface co-receptors

Extra-embryonic syndecan 2 regulates organ primordia migration and fibrillogenesis throughout the zebrafish embryo

The Putative Heparin-specific N-AcetylglucosaminylN-Deacetylase/N-Sulfotransferase Also Occurs in Non-heparin-producing Cells

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