Cell surface proteoglycan associates with the cytoskeleton at the basolateral cell surface of mouse mammary epithelial cells.

Rapraeger, Alan C.; Jalkanen, Markku; Bernfield, Merton

doi:10.1083/jcb.103.6.2683

Cited by 300 publications

(200 citation statements)

References 47 publications

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“…Among epithelial cell types, the distribution of staining on the plasma membrane ranges from staining over the entire cell surface (squamous epithelia, such as cornea and tongue) to staining of only the basolateral surface (cuboidal and columnar epithelia, such as mammary duct and trachea) [40]. An analysis of syndecan-1 distribution on the surface of cultured mammary epithelial cells revealed that, in newly plated cultures, the proteoglycan is present initially over the entire cell surface, but becomes restricted to the basolateral surface as the cells become polarized [71].…”

Section: Membrane Localization Of Syndecansmentioning

confidence: 99%

“…There is evidence suggesting a role for syndecan binding to the actin cytoskeleton in this process, perhaps triggered by extracellular-matrix-dependent cross-linking of syndecan molecules on the cell surface [71]. Such a mechanism would indicate a role for the cytoplasmic domain of syndecan-1 in targeting of the proteoglycan in polarized epithelial cells.…”

Section: Membrane Localization Of Syndecansmentioning

confidence: 99%

“…An early study provided indirect evidence that syndecan-1 on the basal surface of epithelial cells could associate with the actin cytoskeleton [71]. It was proposed that cytoskeleton association was triggered in response to binding of syndecans in the membrane to fibronectin molecules in the basal extracellular matrix.…”

Section: Syndecan-cytoskeleton Associationmentioning

confidence: 99%

See 2 more Smart Citations

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: Membrane Localization Of Syndecansmentioning

confidence: 99%

Section: Membrane Localization Of Syndecansmentioning

confidence: 99%

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Syndecans: multifunctional cell-surface co-receptors

Carey

1997

Biochemical Journal

621

497

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“…Fibronectin contains a heparinbinding domain and has been found to interact with syndecan-4 and glypican-1 (12). Therefore, HSPG have been proposed to function as receptors for anchoring heparin-binding ECM proteins, like fibronectin, to endothelial cells (13,14). Recently fibronectin has also been shown to bind VEGF, suggesting an additional role for this ECM protein in the storage of VEGF (15).…”

mentioning

confidence: 99%

pH Regulates Vascular Endothelial Growth Factor Binding to Fibronectin

Goerges

Nugent

2004

Journal of Biological Chemistry

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Hypoxia is one of the major signals that induces angiogenesis. Hypoxic conditions lead to reduced extracellular pH. Vascular endothelial growth factor (VEGF) binding to endothelial cells and the extracellular matrix (ECM) increases at acidic pH (7.0 -5.5). These interactions are dependent on heparan sulfate proteoglycans, but do not depend on the presence of VEGF receptors. Here we report that VEGF 165 and VEGF 121 binding to fibronectin also increased at acidic pH, and that these interactions are further enhanced by the addition of heparin. These results reveal that the accepted nonheparin-binding isoform of VEGF (VEGF 121 ) is converted into a heparin-binding growth factor under acidic conditions. Interestingly, we did not observe increased binding of VEGF to collagen type I at acidic pH in the presence or absence of heparin, indicating that this effect is not a general property of all heparin-binding ECM proteins. The high level of VEGF binding at acidic pH was also rapidly reversed as demonstrated by increased rates of VEGF dissociation from fibronectin and fibronectin-heparin matrices as the pH was raised. The VEGF released from fibronectin retained its ability to stimulate the activation of extracellular-regulated kinase 1/2 in endothelial cells. These results suggest that VEGF may be stored in the extracellular matrix via interactions with fibronectin and heparan sulfate in tissues that are in need of vascularization so that it can aid in directing the dynamic process of growth and migration of new blood vessels.

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“…HSPGs are members of a family of cell surface proteins with polysaccharide side chains characterized by alternating uronic acid and glucosamine units (12,13). They occur as either integral membrane (14,15) or as secreted extracellular matrix proteins (12). The polysaccharide chains are connected to the core proteins through serine of the Ser-Gly (SG) consensus sequence whereby the presence of nearby acidic amino acids and the repetition of SGs are factors that promote attachment of glycosaminoglycan (GAG) side chains and favor synthesis of heparan sulfate (HS) over chondroitin sulfate (CS) side chains (16,17).…”

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confidence: 99%

Expression of Collagen XVIII and Localization of Its Glycosaminoglycan Attachment Sites

Dong

Cole²,

Halfter

2003

Journal of Biological Chemistry

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Collagen XVIII is the only currently known collagen that carries heparan sulfate glycosaminoglycan side chains. The number and location of the glycosaminoglycan attachment sites in the core protein were determined by eukaryotic expression of full-length chick collagen XVIII and site-directed mutagenesis. Three SerGly consensus sequences carrying glycosaminoglycan side chains were detected in the middle and N-terminal part of the core protein. One of the Ser-Gly consensus sequences carried a heparan sulfate side chain, and the remaining two had mixed chondroitin and heparan sulfate side chains; thus, recombinant collagen XVIII was a hybrid of heparan sulfate and chondroitin proteoglycan. In contrast, collagen XVIII from all chick tissues so far assayed have exclusively heparan sulfate side chains, indicating that the posttranslational modification of proteins expressed in vitro is not entirely identical to the processing that occurs in a living embryo. Incubating the various mutated collagen XVIIIs with retinal basement membranes showed that the heparan sulfate glycosaminoglycan side chains mediate the binding of collagen XVIII to basement membranes.The collagens type XVIII and XV are members of the multiplexins, a collagen subfamily that is characterized by multiple alternating collagen and non-collagenous domains in the protein sequence (1, 2). Collagen XVIII came into the public spotlight by the discovery that the C-terminal peptide of collagen XVIII, named endostatin, has anti-angiogenic and anti-tumor activities (3, 4). The anti-angiogenic activity of the peptide led to the idea that collagen XVIII might be involved in the development of the vascular system. The targeted deletion of collagen XVIII in mice (5) and a naturally occurring mutation in human (6), however, showed that its main function is restricted to the development of the vasculature in the eye but has no function in blood vessel development in other parts of the body. The fact that collagen XVIII is, next to collagen IV, the only collagen that is conserved from Drosophila (7) and Caenorhabditis elegans (8) to humans suggests an important function of the protein in evolution. The deduced amino acid sequences from collagen XVIII cDNA in mouse and human suggested that collagen XVIII is a proteoglycan (1, 9). It was later revealed by investigating the naturally occurring protein from chick embryos (10) that collagen XVIII is a heparan sulfate proteoglycan (HSPG), 1 which is, next to perlecan and agrin, the third extracellular matrix HSPG currently known (10, 11). HSPGs are members of a family of cell surface proteins with polysaccharide side chains characterized by alternating uronic acid and glucosamine units (12, 13). They occur as either integral membrane (14, 15) or as secreted extracellular matrix proteins (12). The polysaccharide chains are connected to the core proteins through serine of the Ser-Gly (SG) consensus sequence whereby the presence of nearby acidic amino acids and the repetition of SGs are factors that promote attachment of glyco...

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Cell surface proteoglycan associates with the cytoskeleton at the basolateral cell surface of mouse mammary epithelial cells.

Cited by 300 publications

References 47 publications

Syndecans: multifunctional cell-surface co-receptors

Syndecans: multifunctional cell-surface co-receptors

pH Regulates Vascular Endothelial Growth Factor Binding to Fibronectin

Expression of Collagen XVIII and Localization of Its Glycosaminoglycan Attachment Sites

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